A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.
An aldose-ketose isomerase that catalyzes the reversible interconversion of glucose 6-phosphate and fructose 6-phosphate. In prokaryotic and eukaryotic organisms it plays an essential role in glycolytic and gluconeogenic pathways. In mammalian systems the enzyme is found in the cytoplasm and as a secreted protein. This secreted form of glucose-6-phosphate isomerase has been referred to as autocrine motility factor or neuroleukin, and acts as a cytokine which binds to the AUTOCRINE MOTILITY FACTOR RECEPTOR. Deficiency of the enzyme in humans is an autosomal recessive trait, which results in CONGENITAL NONSPHEROCYTIC HEMOLYTIC ANEMIA.
Glucose-6-Phosphate Dehydrogenase (G6PD) is an enzyme that plays a critical role in the pentose phosphate pathway, catalyzing the oxidation of glucose-6-phosphate to 6-phosphoglucono-δ-lactone while reducing nicotinamide adenine dinucleotide phosphate (NADP+) to nicotinamide adenine dinucleotide phosphate hydrogen (NADPH), thereby protecting cells from oxidative damage and maintaining redox balance.
An autosomal recessive disorder of fatty acid oxidation, and branched chain amino acids (AMINO ACIDS, BRANCHED-CHAIN); LYSINE; and CHOLINE catabolism, that is due to defects in either subunit of ELECTRON TRANSFER FLAVOPROTEIN or its dehydrogenase, electron transfer flavoprotein-ubiquinone oxidoreductase (EC 1.5.5.1).
An autosomal recessive disorder affecting DIHYDROPYRIMIDINE DEHYDROGENASE and causing familial pyrimidinemia. It is characterized by thymine-uraciluria in homozygous deficient patients. Even a partial deficiency in the enzyme leaves individuals at risk for developing severe 5-FLUOROURACIL-associated toxicity.
A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.
Errors in the metabolism of LIPIDS resulting from inborn genetic MUTATIONS that are heritable.
A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
Brain disorders resulting from inborn metabolic errors, primarily from enzymatic defects which lead to substrate accumulation, product reduction, or increase in toxic metabolites through alternate pathways. The majority of these conditions are familial, however spontaneous mutation may also occur in utero.
Hemolytic anemia due to the ingestion of fava beans or after inhalation of pollen from the Vicia fava plant by persons with glucose-6-phosphate dehydrogenase deficient erythrocytes.
An inherited metabolic disorder caused by deficient enzyme activity in the PYRUVATE DEHYDROGENASE COMPLEX, resulting in deficiency of acetyl CoA and reduced synthesis of acetylcholine. Two clinical forms are recognized: neonatal and juvenile. The neonatal form is a relatively common cause of lactic acidosis in the first weeks of life and may also feature an erythematous rash. The juvenile form presents with lactic acidosis, alopecia, intermittent ATAXIA; SEIZURES; and an erythematous rash. (From J Inherit Metab Dis 1996;19(4):452-62) Autosomal recessive and X-linked forms are caused by mutations in the genes for the three different enzyme components of this multisubunit pyruvate dehydrogenase complex. One of the mutations at Xp22.2-p22.1 in the gene for the E1 alpha component of the complex leads to LEIGH DISEASE.
An enzyme that plays a role in the GLUTAMATE and butanoate metabolism pathways by catalyzing the oxidation of succinate semialdehyde to SUCCINATE using NAD+ as a coenzyme. Deficiency of this enzyme, causes 4-hydroxybutyricaciduria, a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA).
The identification of selected parameters in newborn infants by various tests, examinations, or other procedures. Screening may be performed by clinical or laboratory measures. A screening test is designed to sort out healthy neonates (INFANT, NEWBORN) from those not well, but the screening test is not intended as a diagnostic device, rather instead as epidemiologic.
An NAD-dependent 3-hydroxyacyl CoA dehydrogenase that has specificity for acyl chains containing 8 and 10 carbons.
Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.
A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.
Disorders affecting amino acid metabolism. The majority of these disorders are inherited and present in the neonatal period with metabolic disturbances (e.g., ACIDOSIS) and neurologic manifestations. They are present at birth, although they may not become symptomatic until later in life.
Errors in metabolic processes resulting from inborn genetic mutations that are inherited or acquired in utero.
A flavoprotein enzyme that is responsible for the catabolism of LYSINE; HYDROXYLYSINE; and TRYPTOPHAN. It catalyzes the oxidation of GLUTARYL-CoA to crotonoyl-CoA using FAD as a cofactor. Glutaric aciduria type I is an inborn error of metabolism due to the deficiency of glutaryl-CoA dehydrogenase.
A flavoprotein oxidoreductase that has specificity for short-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
Scattered islands in the Mediterranean Sea. The chief islands are the Balearic Islands (belong to Spain; Majorca and Minorca are among these), Corsica (belongs to France), Crete (belongs to Greece), CYPRUS (a republic), the Cyclades, Dodecanese and Ionian Islands (belong to Greece), MALTA (a republic), Sardinia and SICILY (belong to Italy). (From Webster's New Geographical Dictionary, 1988, p747)
A condition of inadequate circulating red blood cells (ANEMIA) or insufficient HEMOGLOBIN due to premature destruction of red blood cells (ERYTHROCYTES).
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
Flavoproteins that serve as specific electron acceptors for a variety of DEHYDROGENASES. They participate in the transfer of electrons to a variety of redox acceptors that occur in the respiratory chain.
Inborn errors of purine-pyrimidine metabolism refer to genetic disorders resulting from defects in the enzymes responsible for the metabolic breakdown and synthesis of purines and pyrimidines, leading to the accumulation of toxic metabolites or deficiency of necessary nucleotides, causing various clinical manifestations such as neurological impairment, kidney problems, and developmental delays.
The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).
Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.
A term used pathologically to describe BILIRUBIN staining of the BASAL GANGLIA; BRAIN STEM; and CEREBELLUM and clinically to describe a syndrome associated with HYPERBILIRUBINEMIA. Clinical features include athetosis, MUSCLE SPASTICITY or hypotonia, impaired vertical gaze, and DEAFNESS. Nonconjugated bilirubin enters the brain and acts as a neurotoxin, often in association with conditions that impair the BLOOD-BRAIN BARRIER (e.g., SEPSIS). This condition occurs primarily in neonates (INFANT, NEWBORN), but may rarely occur in adults. (Menkes, Textbook of Child Neurology, 5th ed, p613)
An enzyme that catalyzes the oxidation of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It takes part in the L-SERINE biosynthesis pathway.
An aminoquinoline that is given by mouth to produce a radical cure and prevent relapse of vivax and ovale malarias following treatment with a blood schizontocide. It has also been used to prevent transmission of falciparum malaria by those returning to areas where there is a potential for re-introduction of malaria. Adverse effects include anemias and GI disturbances. (From Martindale, The Extra Pharmacopeia, 30th ed, p404)
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.
Acquired or inborn metabolic diseases that produce brain dysfunction or damage. These include primary (i.e., disorders intrinsic to the brain) and secondary (i.e., extracranial) metabolic conditions that adversely affect cerebral function.
A FLAVOPROTEIN enzyme that catalyzes the oxidative demethylation of dimethylglycine to SARCOSINE and FORMALDEHYDE.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.
A form of encephalopathy with fatty infiltration of the LIVER, characterized by brain EDEMA and VOMITING that may rapidly progress to SEIZURES; COMA; and DEATH. It is caused by a generalized loss of mitochondrial function leading to disturbances in fatty acid and CARNITINE metabolism.
An infant during the first month after birth.
Used as an electron carrier in place of the flavine enzyme of Warburg in the hexosemonophosphate system and also in the preparation of SUCCINIC DEHYDROGENASE.
Yellow discoloration of the SKIN; MUCOUS MEMBRANE; and SCLERA in the NEWBORN. It is a sign of NEONATAL HYPERBILIRUBINEMIA. Most cases are transient self-limiting (PHYSIOLOGICAL NEONATAL JAUNDICE) occurring in the first week of life, but some can be a sign of pathological disorders, particularly LIVER DISEASES.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
A benign familial disorder, transmitted as an autosomal dominant trait. It is characterized by low-grade chronic hyperbilirubinemia with considerable daily fluctuations of the bilirubin level.
A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.
An autosomal recessive disease in which gene expression of glucose-6-phosphatase is absent, resulting in hypoglycemia due to lack of glucose production. Accumulation of glycogen in liver and kidney leads to organomegaly, particularly massive hepatomegaly. Increased concentrations of lactic acid and hyperlipidemia appear in the plasma. Clinical gout often appears in early childhood.
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.
An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
The destruction of ERYTHROCYTES by many different causal agents such as antibodies, bacteria, chemicals, temperature, and changes in tonicity.
A condition observed in WOMEN and CHILDREN when there is excess coarse body hair of an adult male distribution pattern, such as facial and chest areas. It is the result of elevated ANDROGENS from the OVARIES, the ADRENAL GLANDS, or exogenous sources. The concept does not include HYPERTRICHOSIS, which is an androgen-independent excessive hair growth.
A mitochondrial protein consisting of four alpha-subunits and four beta-subunits. It contains enoyl-CoA hydratase, long-chain-3-hydroxyacyl-CoA dehydrogenase, and acetyl-CoA C-acyltransferase activities and plays an important role in the metabolism of long chain FATTY ACIDS.
A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Glycerolphosphate Dehydrogenase is an enzyme (EC 1.1.1.8) that catalyzes the reversible conversion of dihydroxyacetone phosphate to glycerol 3-phosphate, using nicotinamide adenine dinucleotide (NAD+) as an electron acceptor in the process.
Accumulation of BILIRUBIN, a breakdown product of HEME PROTEINS, in the BLOOD during the first weeks of life. This may lead to NEONATAL JAUNDICE. The excess bilirubin may exist in the unconjugated (indirect) or the conjugated (direct) form. The condition may be self-limiting (PHYSIOLOGICAL NEONATAL JAUNDICE) or pathological with toxic levels of bilirubin.
Repetitive withdrawal of small amounts of blood and replacement with donor blood until a large proportion of the blood volume has been exchanged. Used in treatment of fetal erythroblastosis, hepatic coma, sickle cell anemia, disseminated intravascular coagulation, septicemia, burns, thrombotic thrombopenic purpura, and fulminant malaria.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
A 21-carbon steroid that is converted from PREGNENOLONE by STEROID 17-ALPHA-HYDROXYLASE. It is an intermediate in the delta-5 pathway of biosynthesis of GONADAL STEROID HORMONES and the adrenal CORTICOSTEROIDS.
Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.
A condition characterized by an abnormal increase of BILIRUBIN in the blood, which may result in JAUNDICE. Bilirubin, a breakdown product of HEME, is normally excreted in the BILE or further catabolized before excretion in the urine.
A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
The Ketoglutarate Dehydrogenase Complex is a multi-enzyme complex involved in the citric acid cycle, catalyzing the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA and CO2, thereby connecting the catabolism of amino acids, carbohydrates, and fats to the generation of energy in the form of ATP.
Oxidoreductases that are specific for ALDEHYDES.
Diseases caused by abnormal function of the MITOCHONDRIA. They may be caused by mutations, acquired or inherited, in mitochondrial DNA or in nuclear genes that code for mitochondrial components. They may also be the result of acquired mitochondria dysfunction due to adverse effects of drugs, infections, or other environmental causes.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The condition of being heterozygous for hemoglobin S.
A dimeric protein found in liver peroxisomes that plays an important role in FATTY ACID metabolism and steroid metabolism. The dimer is formed by cleavage of a single protein precursor and contains an enoyl-CoA hydratase-2 domain and a second domain that displays (S)-3-hydroxyacyl-CoA dehydrogenase and 17-beta-estradiol dehydrogenase activities. The enzyme is stereospecific with regards to arrangement of the substrate double bonds and position of the 3-hydroxy group of the reaction intermediate. It is complemented by PEROXISOMAL BIFUNCTIONAL ENZYME, which has the opposite reaction stereospecificity.
Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.
An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.
A group of inherited disorders of the ADRENAL GLANDS, caused by enzyme defects in the synthesis of cortisol (HYDROCORTISONE) and/or ALDOSTERONE leading to accumulation of precursors for ANDROGENS. Depending on the hormone imbalance, congenital adrenal hyperplasia can be classified as salt-wasting, hypertensive, virilizing, or feminizing. Defects in STEROID 21-HYDROXYLASE; STEROID 11-BETA-HYDROXYLASE; STEROID 17-ALPHA-HYDROXYLASE; 3-beta-hydroxysteroid dehydrogenase (3-HYDROXYSTEROID DEHYDROGENASES); TESTOSTERONE 5-ALPHA-REDUCTASE; or steroidogenic acute regulatory protein; among others, underlie these disorders.
D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.
Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.
##### I apologize, but the term "Jordan" does not have a specific medical definition in the English language. It is primarily used as a personal name or to refer to the country in the Middle East.
A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.
The abrupt and unexplained death of an apparently healthy infant under one year of age, remaining unexplained after a thorough case investigation, including performance of a complete autopsy, examination of the death scene, and review of the clinical history. (Pediatr Pathol 1991 Sep-Oct;11(5):677-84)
A group of hereditary hemolytic anemias in which there is decreased synthesis of one or more hemoglobin polypeptide chains. There are several genetic types with clinical pictures ranging from barely detectable hematologic abnormality to severe and fatal anemia.
An individual having different alleles at one or more loci regarding a specific character.
An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.
Acquired, familial, and congenital disorders of SKELETAL MUSCLE and SMOOTH MUSCLE.
Alcohol oxidoreductases with substrate specificity for LACTIC ACID.
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.
An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.

Gilbert's syndrome and jaundice in glucose-6-phosphate dehydrogenase deficient neonates. (1/317)

BACKGROUND AND OBJECTIVE: The pathogenesis of the hyperbilirubinemia present in approximately 30% of neonates affected by glucose-6-phosphate dehydrogenase deficiency is an unsolved problem. We evaluated the effect of Gilbert's syndrome, the most common defect of bilirubin conjugation, on the hyperbilirubinemia of these neonates. DESIGN AND METHODS: One hundred and two neonates affected by glucose-6-phosphate dehydrogenase deficiency were enrolled in this study: 56 had hyperbilirubinemia and 46 had normal bilirubin levels. The analysis of the A(TA)nTAA motif in the promoter region of the UGT1A gene was performed by means of PCR, followed by separation on 6% denaturing polycrylamide gel. RESULTS: The frequency of the three different genotypes of the A(TA)nTAA motif was similar in the study and control groups. Our results demonstrated no difference in the percentage of homozygotes for the UGT1A (TA)7 variant associated with Gilbert's syndrome. INTERPRETATION AND CONCLUSIONS: These findings indicate that Gilbert's syndrome does not account for the hyperbilirubinemia occurring in some neonates with glucose-6-phosphate dehydrogenase deficiency. Furthermore our results suggest that hemolysis is not the major event in the pathogenesis of hyperbilirubinemia in these patients.  (+info)

Effect of vitamin K1 on glucose-6-phosphate dehydrogenase deficient neonatal erythrocytes in vitro. (2/317)

AIM: To determine whether vitamin K1, which is routinely administered to neonates, could act as an exogenous oxidising agent and be partly responsible for haemolysis in glucose-6-phosphat-dehydrogenase (G-6-PD). METHODS: G-6-PD deficient (n = 7) and control (n = 10) umbilical cord blood red blood cells were incubated in vitro with a vitamin K1 preparation (Konakion). Two concentrations of Vitamin K1 were used, both higher than that of expected serum concentrations, following routine injection of 1 mg vitamin K1. Concentrations of reduced glutathione (GSH) and methaemoglobin, indicators of oxidative red blood cell damage, were determined before and after incubation, and the mean percentage change from baseline calculated. RESULTS: Values (mean (SD)) for GSH, at baseline, and after incubation with vitamin K1 at concentrations of 44 and 444 microM, respectively, and percentage change from baseline (mean (SD)) were 1.97 + 0.31 mumol/g haemoglobin, 1.89 +/- 0.44 mumol/g (-4.3 +/- 13.1%), and 1.69 +/- 0.41 mumol/g (-14.5 +/- 9.3%) for the G-6-PD deficient red blood cells, and 2.27 +/- 0.31 mumol/g haemoglobin, 2.09 +/- 0.56 mumol/g (-7.2 +/- 23.2%), and 2.12 +/- 0.38 mumol/g (-6.0 + 14.1%) for the control cells. For methaemoglobin (percentage of total haemoglobin), the corresponding values were 2.01 +/- 0.53%, 1.93 +/- 0.37% (-0.6 +/- 17.4%) and 2.06 +/- 0.43% (5.7 +/- 14.2%) for the G-6-PD deficient red blood cells, and 1.56 +/- 0.74%, 1.70 +/- 0.78% (12.7 +/- 21.9%), and 1.78 +/- 0.71% (20.6 +/- 26.8%) for the control red blood cells. None of the corresponding percentage changes from baseline was significantly different when G-6-PD deficient and control red blood cells were compared. CONCLUSIONS: These findings suggest that G-6-PD deficient red blood cells are not at increased risk of oxidative damage from vitamin K1.  (+info)

Detection of the most common G6PD gene mutations in Chinese using amplification refractory mutation system. (3/317)

Glucose-6-phosphate dehydrogenase (G6PD) is the most common human enzymopathy. To date more than 122 mutations in the G6PD gene have been discovered, among which 12 point mutations are found in the Chinese. The 2 most common mutations, G1388A and G1376T, account for more than 50% of mutations representing various regions and ethnic groups in China. Setting up a simple and accurate method for detecting these mutations is not only useful for studying the frequency of the G6PD genotypes, but also for finding new mutations. The purpose of this study was to find a simple, inexpensive and accurate method for detecting these common mutations. The amplification refractory mutation system (ARMS) method was used in this study. Samples from 28 G6PD-deficient males were investigated. The natural and mismatched amplification and restriction enzyme digestion method was used as a standard method to evaluate the nature of the point mutations. Sixteen cases were found carrying the G1388A mutation and 12 the G1376T mutation. Fourteen cases of G1388A and 10 cases of G1376T were confirmed by ARMS. Four cases were not in concordance with the results obtained by the mismatched amplification-restriction enzyme digestion. These 4 cases were then judged by direct PCR sequencing at exon 12. The DNA sequencing data supported the results obtained by ARMS. Thus we concluded that the ARMS is a rapid, simple, inexpensive and accurate method for detecting the most common G6PD gene mutations among the Chinese.  (+info)

Serum transferrin receptor levels are increased in asymptomatic and mild Plasmodium falciparum-infection. (4/317)

BACKGROUND AND OBJECTIVE: The serum transferrin receptor (sTfR) concentration in an individual reflects the extent of erythropoietic activity and is considered a useful marker of iron deficiency independent of concurrent inflammation or infection. However, data on the impact of malaria on this parameter are ambiguous. We have examined potential associations of asymptomatic and mild Plasmodium falciparum-infections and of several erythrocyte variants with sTfR values in South West Nigeria. DESIGN AND METHODS: In a cross-sectional study among 161 non-hospitalized children, sTfR concentrations and P. falciparum parasitemia were assessed. In addition, hemoglobin (Hb) and serum ferritin values, Hb-types, glucose-6-phosphate dehydrogenase (G6PD)deficiency and a-globin genotypes were determined and the effects of these factors on sTfR levels were analyzed by univariate and multivariate statistical methods. RESULTS: P. falciparum-infection was present in 77% of the children. Mean sTfR levels were higher in infected than in non-infected children (geometric mean, 3.68, 95% confidence interval [3.5-3.9] vs. 2.99 [2.7-3.3] mg/L; p = 0.0009). There was a significant trend for higher sTfR values with increasing parasite density. sTfR values decreased continuously with age. Hb-types, G6PD-, and a-globin genotypes did not correlate with sTfR levels. In the multivariate analysis, age, Hb and log ferritin values, and parasite density of P. falciparum were independently associated with log sTfR values. INTERPRETATION AND CONCLUSIONS: sTfR concentrations are increased in asymptomatic and mild P. falciparum-infections suggesting adequate bone marrow response in this condition. The diagnostic value of sTfR levels for iron deficiency may be impaired in areas where stable malaria occurs.  (+info)

Identification of glucose 6-phosphate dehydrogenase deficiency in a population with a high frequency of thalassemia. (5/317)

High frequencies of both thalassemia trait (5.2%) and glucose 6-phosphate dehydrogenase (G6PD) deficiency for only males (1.3%) have been observed in the Calabrian population. The G6PD activity measurement was carried out on 1239 samples of whole blood from Calabrian subjects of both sexes (age range 10-55) by a differential pH-metry technique which was quite suitable to determine the G6PD deficiency in mass screenings. The analyzed subjects showed: only the thalassemia trait; or only the G6PD deficiency; or only the total iron serum deficiency; or G6PD deficiency associated with the thalassemia trait or with the total iron serum deficiency. The G6PD heterozygous subjects have an enzymatic activity which is masked by both the thalassemia trait and the total iron serum deficiency. In a population showing high frequencies of both thalassemia trait and G6PD deficiency, the comparison of G6PD activity of heterozygous subjects also affected with the thalassemia trait is more reliable if referred to the enzymatic activity of the carriers of the latter inherited anomaly rather than to G6PD activity of normal subjects.  (+info)

Factors influencing resistance to reinfection with Plasmodium falciparum. (6/317)

A treatment-reinfection study design was used to investigate the relationships between host immunologic and/or genetic factors and resistance to reinfection with Plasmodium falciparum. Sixty-one children in Gabon were enrolled in a cross-sectional study to measure the prevalence of each human plasmodial species. All were given amodiaquine for radical cure of parasites, and 40 were subsequently followed-up for 30 weeks. Successive blood smears were examined to measure the delay of reappearance in blood of asexual stages of P. falciparum parasites. Presence of infection during the cross-sectional survey was associated with male sex, non-deficient glucose-6-phosphate dehydrogenase activity, plasma interleukin-10 level, and anti-LSA-Rep antibody concentration. Resistance to reinfection was related to the presence of anti-LSA-J antibodies, and the absence of anti-LSA-Rep antibodies. Moreover, P. malariae-infected subjects were usually co-infected with P. falciparum, and were also more rapidly reinfected with P. falciparum after treatment, compared with those without P. malariae infection.  (+info)

Glucose-6-phosphate dehydrogenase deficiency in Kuwait, Syria, Egypt, Iran, Jordan and Lebanon. (7/317)

A total of 3,501 male subjects from six Arab countries living in Kuwait were investigated for quantitative and phenotypic distribution of red cell glucose-6-phosphate dehydrogenase (G6PD). The ethnic origins of those investigated were Kuwait, Egypt, Iran, Syria, Lebanon and Jordan. The distribution of G6PD deficiency among the different ethnic groups varied widely, ranging from 1.00% for Egyptians to 11.55% for Iranians. The activity of the normal enzyme was remarkably similar, with values ranging from 6.1 +/- 0.8 to 6.5 +/- 1.1 IU/g Hb. A low frequency of the Gd(A) allele was found in two ethnic groups, Egyptians (0.019) and Iranians (0.014). Gd(A-) was present at the very low frequency of 0.006 in another two ethnic groups, Kuwaitis and Jordanians.  (+info)

Structural defects underlying protein dysfunction in human glucose-6-phosphate dehydrogenase A(-) deficiency. (8/317)

The enzyme variant glucose-6-phosphate dehydrogenase (G6PD) A(-), which gives rise to human glucose-6-phosphate dehydrogenase deficiency, is a protein of markedly reduced structural stability. This variant differs from the normal enzyme, G6PD B, in two amino acid substitutions. A further nondeficient variant, G6PD A, bears only one of these two mutations and is structurally stable. In this study, the synergistic structural defect in recombinant G6PD A(-) was reflected by reduced unfolding enthalpy due to loss of beta-sheet and alpha-helix interactions where both mutations are found. This was accompanied by changes in inner spatial distances between residues in the coenzyme domain and the partial disruption of tertiary structure with no significant loss of secondary structure. However, the secondary structure of G6PD A(-) was qualitatively affected by an increase in beta-sheets substituting beta-turns related to the lower unfolding enthalpy. The structural changes observed did not affect the active site of the mutant proteins, since its spatial position was unmodified. The final result is a loss of folding determinants leading to a protein with decreased intracellular stability. This is suggested as the cause of the enzyme deficiency in the red blood cell, which is unable to perform de novo protein synthesis.  (+info)

Glucose-6-Phosphate Dehydrogenase (G6PD) deficiency is a genetic disorder that affects the normal functioning of an enzyme called G6PD. This enzyme is found in red blood cells and plays a crucial role in protecting them from damage.

In people with G6PD deficiency, the enzyme's activity is reduced or absent, making their red blood cells more susceptible to damage and destruction, particularly when they are exposed to certain triggers such as certain medications, infections, or foods. This can lead to a condition called hemolysis, where the red blood cells break down prematurely, leading to anemia, jaundice, and in severe cases, kidney failure.

G6PD deficiency is typically inherited from one's parents in an X-linked recessive pattern, meaning that males are more likely to be affected than females. While there is no cure for G6PD deficiency, avoiding triggers and managing symptoms can help prevent complications.

Glucose-6-phosphate isomerase (GPI) is an enzyme involved in the glycolytic and gluconeogenesis pathways. It catalyzes the interconversion of glucose-6-phosphate (G6P) and fructose-6-phosphate (F6P), which are key metabolic intermediates in these pathways. This reaction is a reversible step that helps maintain the balance between the breakdown and synthesis of glucose in the cell.

In glycolysis, GPI converts G6P to F6P, which subsequently gets converted to fructose-1,6-bisphosphate (F1,6BP) by the enzyme phosphofructokinase-1 (PFK-1). In gluconeogenesis, the reaction is reversed, and F6P is converted back to G6P.

Deficiency or dysfunction of Glucose-6-phosphate isomerase can lead to various metabolic disorders, such as glycogen storage diseases and hereditary motor neuropathies.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), also known as Glucosephosphate Dehydrogenase, is an enzyme that plays a crucial role in cellular metabolism, particularly in the glycolytic pathway. It catalyzes the conversion of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (1,3-BPG), while also converting nicotinamide adenine dinucleotide (NAD+) to its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has been widely used as a housekeeping gene in molecular biology research due to its consistent expression across various tissues and cells, although recent studies have shown that its expression can vary under certain conditions.

Multiple Acyl Coenzyme A Dehydrogenase Deficiency (MADD) is a rare inherited metabolic disorder that affects the body's ability to break down certain fats and proteins. It is caused by mutations in genes that code for enzymes involved in the electron transfer flavoprotein-ubiquinone (ETF-QO) complex, which is responsible for transferring electrons from various acyl-CoA dehydrogenases to the electron transport chain during fatty acid and amino acid oxidation.

As a result of these genetic defects, there is a buildup of unoxidized acyl-CoA molecules in the body, leading to the accumulation of toxic intermediates that can damage organs and tissues. This can cause a wide range of symptoms, including hypoglycemia, metabolic acidosis, cardiac arrhythmias, muscle weakness, and developmental delays.

MADD is typically classified into three types based on the age of onset and severity of symptoms: neonatal, infantile, and late-onset. The neonatal form is the most severe and often leads to death in early infancy, while the infantile and late-onset forms can present with milder symptoms that may not become apparent until later in life.

Treatment for MADD typically involves a combination of dietary modifications, such as restricting long-chain fatty acids and supplementing with medium-chain triglycerides, and oral supplementation with riboflavin (vitamin B2), which has been shown to improve the activity of the ETF-QO complex in some cases.

Dihydropyrimidine dehydrogenase (DPD) deficiency is a genetic disorder that affects the metabolism of certain chemicals in the body. DPD is an enzyme that helps break down pyrimidines, which are building blocks of DNA, including the chemicals uracil and thymine.

People with DPD deficiency have reduced levels or completely lack DPD activity, leading to an accumulation of pyrimidines and their metabolites in the body. This can cause a range of symptoms, including neurological problems, gastrointestinal issues, and skin abnormalities.

DPD deficiency is often discovered in individuals who experience severe toxicity after receiving fluorouracil (5-FU) chemotherapy, which is metabolized by DPD. In these cases, the accumulation of 5-FU can cause life-threatening side effects such as neutropenia, sepsis, and mucositis.

DPD deficiency is inherited in an autosomal recessive manner, meaning that an individual must inherit two copies of the mutated gene (one from each parent) to have the condition. It is estimated that DPD deficiency affects approximately 1 in 1000 individuals, but many people with the disorder may not experience any symptoms.

Acyl-CoA dehydrogenase is a group of enzymes that play a crucial role in the body's energy production process. Specifically, they are involved in the breakdown of fatty acids within the cells.

More technically, acyl-CoA dehydrogenases catalyze the removal of electrons from the thiol group of acyl-CoAs, forming a trans-double bond and generating FADH2. This reaction is the first step in each cycle of fatty acid beta-oxidation, which occurs in the mitochondria of cells.

There are several different types of acyl-CoA dehydrogenases, each specific to breaking down different lengths of fatty acids. For example, very long-chain acyl-CoA dehydrogenase (VLCAD) is responsible for breaking down longer chain fatty acids, while medium-chain acyl-CoA dehydrogenase (MCAD) breaks down medium-length chains.

Deficiencies in these enzymes can lead to various metabolic disorders, such as MCAD deficiency or LC-FAOD (long-chain fatty acid oxidation disorders), which can cause symptoms like vomiting, lethargy, and muscle weakness, especially during periods of fasting or illness.

Acyl-CoA dehydrogenases are a group of enzymes that play a crucial role in the body's energy production process. They are responsible for catalyzing the oxidation of various fatty acids, which are broken down into smaller molecules called acyl-CoAs in the body.

More specifically, acyl-CoA dehydrogenases facilitate the removal of electrons from the acyl-CoA molecules, which are then transferred to coenzyme Q10 and eventually to the electron transport chain. This process generates energy in the form of ATP, which is used by cells throughout the body for various functions.

There are several different types of acyl-CoA dehydrogenases, each responsible for oxidizing a specific type of acyl-CoA molecule. These include:

* Very long-chain acyl-CoA dehydrogenase (VLCAD), which oxidizes acyl-CoAs with 12 to 20 carbon atoms
* Long-chain acyl-CoA dehydrogenase (LCAD), which oxidizes acyl-CoAs with 14 to 20 carbon atoms
* Medium-chain acyl-CoA dehydrogenase (MCAD), which oxidizes acyl-CoAs with 6 to 12 carbon atoms
* Short-chain acyl-CoA dehydrogenase (SCAD), which oxidizes acyl-CoAs with 4 to 8 carbon atoms
* Isovaleryl-CoA dehydrogenase, which oxidizes isovaleryl-CoA, a specific type of branched-chain acyl-CoA molecule

Deficiencies in these enzymes can lead to various metabolic disorders, such as medium-chain acyl-CoA dehydrogenase deficiency (MCADD) or long-chain acyl-CoA dehydrogenase deficiency (LCADD), which can cause symptoms such as hypoglycemia, muscle weakness, and developmental delays.

Inborn errors of lipid metabolism refer to genetic disorders that affect the body's ability to break down and process lipids (fats) properly. These disorders are caused by defects in genes that code for enzymes or proteins involved in lipid metabolism. As a result, toxic levels of lipids or their intermediates may accumulate in the body, leading to various health issues, which can include neurological problems, liver dysfunction, muscle weakness, and cardiovascular disease.

There are several types of inborn errors of lipid metabolism, including:

1. Disorders of fatty acid oxidation: These disorders affect the body's ability to convert long-chain fatty acids into energy, leading to muscle weakness, hypoglycemia, and cardiomyopathy. Examples include medium-chain acyl-CoA dehydrogenase deficiency (MCAD) and very long-chain acyl-CoA dehydrogenase deficiency (VLCAD).
2. Disorders of cholesterol metabolism: These disorders affect the body's ability to process cholesterol, leading to an accumulation of cholesterol or its intermediates in various tissues. Examples include Smith-Lemli-Opitz syndrome and lathosterolosis.
3. Disorders of sphingolipid metabolism: These disorders affect the body's ability to break down sphingolipids, leading to an accumulation of these lipids in various tissues. Examples include Gaucher disease, Niemann-Pick disease, and Fabry disease.
4. Disorders of glycerophospholipid metabolism: These disorders affect the body's ability to break down glycerophospholipids, leading to an accumulation of these lipids in various tissues. Examples include rhizomelic chondrodysplasia punctata and abetalipoproteinemia.

Inborn errors of lipid metabolism are typically diagnosed through genetic testing and biochemical tests that measure the activity of specific enzymes or the levels of specific lipids in the body. Treatment may include dietary modifications, supplements, enzyme replacement therapy, or gene therapy, depending on the specific disorder and its severity.

Acyl-CoA dehydrogenase, long-chain (LCHAD) is a medical term that refers to an enzyme found in the body that plays a crucial role in breaking down fatty acids for energy. This enzyme is responsible for catalyzing the first step in the beta-oxidation of long-chain fatty acids, which involves the removal of hydrogen atoms from the fatty acid molecule to create a double bond.

Mutations in the gene that encodes LCHAD can lead to deficiencies in the enzyme's activity, resulting in an accumulation of unmetabolized long-chain fatty acids in the body. This can cause a range of symptoms, including hypoglycemia (low blood sugar), muscle weakness, and liver dysfunction. In severe cases, LCHAD deficiency can lead to serious complications such as heart problems, developmental delays, and even death.

LCHAD deficiency is typically diagnosed through newborn screening or genetic testing, and treatment may involve dietary modifications, supplementation with medium-chain triglycerides (MCTs), and avoidance of fasting to prevent the breakdown of fatty acids for energy. In some cases, LCHAD deficiency may require more intensive treatments such as carnitine supplementation or liver transplantation.

Metabolic brain diseases are a group of disorders caused by genetic defects that affect the body's metabolism and result in abnormal accumulation of harmful substances in the brain. These conditions are present at birth (inborn) or develop during infancy or early childhood. Examples of metabolic brain diseases that are present at birth include:

1. Phenylketonuria (PKU): A disorder caused by a deficiency of the enzyme phenylalanine hydroxylase, which leads to an accumulation of phenylalanine in the brain and can cause intellectual disability, seizures, and behavioral problems if left untreated.
2. Maple syrup urine disease (MSUD): A disorder caused by a deficiency of the enzyme branched-chain ketoacid dehydrogenase, which leads to an accumulation of branched-chain amino acids in the body and can cause intellectual disability, seizures, and metabolic crisis if left untreated.
3. Urea cycle disorders: A group of disorders caused by defects in enzymes that help remove ammonia from the body. Accumulation of ammonia in the blood can lead to brain damage, coma, or death if not treated promptly.
4. Organic acidemias: A group of disorders caused by defects in enzymes that help break down certain amino acids and other organic compounds. These conditions can cause metabolic acidosis, seizures, and developmental delays if left untreated.

Early diagnosis and treatment of these conditions are crucial to prevent irreversible brain damage and other complications. Treatment typically involves dietary restrictions, supplements, and medications to manage the underlying metabolic imbalance. In some cases, enzyme replacement therapy or liver transplantation may be necessary.

Favism is a genetic disorder that results in a sensitivity to broad beans (Vicia faba) and related plants. It is most commonly found in populations from the Mediterranean, Middle East, and Asia. The disorder is caused by a deficiency of the enzyme glucose-6-phosphate dehydrogenase (G6PD), which is necessary for protecting red blood cells from damage.

When individuals with favism eat broad beans or inhale their pollen, the beans' metabolites can cause the release of harmful oxidative agents that destroy red blood cells, leading to hemolytic anemia. Symptoms of favism can include weakness, fatigue, abdominal pain, dark urine, and jaundice. In severe cases, it can lead to kidney failure, seizures, or even death.

Avoiding broad beans and related plants is the primary treatment for favism. In some cases, blood transfusions or medications that boost red blood cell production may be necessary to manage symptoms. It's important to note that not all people with G6PD deficiency will develop favism, and not all people with favism have G6PD deficiency.

Pyruvate Dehydrogenase Complex (PDH) Deficiency is a genetic disorder that affects the body's ability to convert certain food molecules into energy. The pyruvate dehydrogenase complex is a group of enzymes that converts pyruvate, a byproduct of glucose metabolism in the cell's cytoplasm, into acetyl-CoA, which then enters the citric acid cycle (also known as the Krebs cycle) in the mitochondria to produce energy in the form of ATP.

PDH deficiency results from mutations in one or more genes encoding the subunits of the PDH complex or its activators, leading to reduced enzymatic activity. This impairs the conversion of pyruvate to acetyl-CoA and causes an accumulation of pyruvate in body tissues and fluids, particularly during periods of metabolic stress such as illness, infection, or fasting.

The severity of PDH deficiency can vary widely, from mild to severe forms, depending on the extent of enzyme dysfunction. Symptoms may include developmental delay, hypotonia (low muscle tone), seizures, poor feeding, and metabolic acidosis. In severe cases, it can lead to neurological damage, lactic acidosis, and early death if not diagnosed and treated promptly.

PDH deficiency is typically diagnosed through biochemical tests that measure the activity of the PDH complex in cultured skin fibroblasts or muscle tissue. Genetic testing may also be used to identify specific gene mutations causing the disorder. Treatment usually involves a low-carbohydrate, high-fat diet and supplementation with thiamine (vitamin B1), which is an essential cofactor for PDH complex activity. In some cases, dialysis or other supportive measures may be necessary to manage metabolic acidosis and other complications.

Succinate-semialdehyde dehydrogenase (SSDH) is an enzyme involved in the metabolism of the neurotransmitter gamma-aminobutyric acid (GABA). Specifically, SSDH catalyzes the conversion of succinic semialdehyde to succinate in the final step of the GABA degradation pathway. This enzyme plays a critical role in maintaining the balance of GABA levels in the brain and is therefore essential for normal neurological function. Deficiencies or mutations in SSDH can lead to neurological disorders, including developmental delays, intellectual disability, and seizures.

Neonatal screening is a medical procedure in which specific tests are performed on newborn babies within the first few days of life to detect certain congenital or inherited disorders that are not otherwise clinically apparent at birth. These conditions, if left untreated, can lead to serious health problems, developmental delays, or even death.

The primary goal of neonatal screening is to identify affected infants early so that appropriate treatment and management can be initiated as soon as possible, thereby improving their overall prognosis and quality of life. Commonly screened conditions include phenylketonuria (PKU), congenital hypothyroidism, galactosemia, maple syrup urine disease, sickle cell disease, cystic fibrosis, and hearing loss, among others.

Neonatal screening typically involves collecting a small blood sample from the infant's heel (heel stick) or through a dried blood spot card, which is then analyzed using various biochemical, enzymatic, or genetic tests. In some cases, additional tests such as hearing screenings and pulse oximetry for critical congenital heart disease may also be performed.

It's important to note that neonatal screening is not a diagnostic tool but rather an initial step in identifying infants who may be at risk of certain conditions. Positive screening results should always be confirmed with additional diagnostic tests before any treatment decisions are made.

Long-chain-3-hydroxyacyl-coenzyme A dehydrogenase (LCHAD) is a mitochondrial enzyme that plays a crucial role in the beta-oxidation of fatty acids. Specifically, LCHAD catalyzes the third step of this process by oxidizing long-chain 3-hydroxyacyl-CoA molecules to 3-ketoacyl-CoAs, using NAD+ as an electron acceptor. This reaction is essential for generating energy in the form of ATP and reducing equivalents (NADH and FADH2) through the citric acid cycle.

Deficiencies in LCHAD can lead to a rare autosomal recessive disorder known as long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHADD). This condition impairs the body's ability to metabolize long-chain fatty acids, particularly during periods of fasting or increased energy demands. Symptoms can include hypoketotic hypoglycemia, muscle weakness, cardiomyopathy, and retinal damage, among others. Early diagnosis and management are crucial for improving outcomes in affected individuals.

3-Hydroxyacyl CoA Dehydrogenases (3-HADs) are a group of enzymes that play a crucial role in the beta-oxidation of fatty acids. These enzymes catalyze the third step of the beta-oxidation process, which involves the oxidation of 3-hydroxyacyl CoA to 3-ketoacyl CoA. This reaction is an essential part of the energy-generating process that occurs in the mitochondria of cells and allows for the breakdown of fatty acids into smaller molecules, which can then be used to produce ATP, the primary source of cellular energy.

There are several different isoforms of 3-HADs, each with specific substrate preferences and tissue distributions. The most well-known isoform is the mitochondrial 3-hydroxyacyl CoA dehydrogenase (M3HD), which is involved in the oxidation of medium and long-chain fatty acids. Other isoforms include the short-chain 3-hydroxyacyl CoA dehydrogenase (SCHAD) and the long-chain 3-hydroxyacyl CoA dehydrogenase (LCHAD), which are involved in the oxidation of shorter and longer chain fatty acids, respectively.

Deficiencies in 3-HADs can lead to serious metabolic disorders, such as 3-hydroxyacyl-CoA dehydrogenase deficiency (3-HAD deficiency), which is characterized by the accumulation of toxic levels of 3-hydroxyacyl CoAs in the body. Symptoms of this disorder can include hypoglycemia, muscle weakness, cardiomyopathy, and developmental delays. Early diagnosis and treatment of 3-HAD deficiency are essential to prevent serious complications and improve outcomes for affected individuals.

Carnitine is a naturally occurring substance in the body that plays a crucial role in energy production. It transports long-chain fatty acids into the mitochondria, where they can be broken down to produce energy. Carnitine is also available as a dietary supplement and is often used to treat or prevent carnitine deficiency.

The medical definition of Carnitine is:

"A quaternary ammonium compound that occurs naturally in animal tissues, especially in muscle, heart, brain, and liver. It is essential for the transport of long-chain fatty acids into the mitochondria, where they can be oxidized to produce energy. Carnitine also functions as an antioxidant and has been studied as a potential treatment for various conditions, including heart disease, diabetes, and kidney disease."

Carnitine is also known as L-carnitine or levocarnitine. It can be found in foods such as red meat, dairy products, fish, poultry, and tempeh. In the body, carnitine is synthesized from the amino acids lysine and methionine with the help of vitamin C and iron. Some people may have a deficiency in carnitine due to genetic factors, malnutrition, or certain medical conditions, such as kidney disease or liver disease. In these cases, supplementation may be necessary to prevent or treat symptoms of carnitine deficiency.

Inborn errors of amino acid metabolism refer to genetic disorders that affect the body's ability to properly break down and process individual amino acids, which are the building blocks of proteins. These disorders can result in an accumulation of toxic levels of certain amino acids or their byproducts in the body, leading to a variety of symptoms and health complications.

There are many different types of inborn errors of amino acid metabolism, each affecting a specific amino acid or group of amino acids. Some examples include:

* Phenylketonuria (PKU): This disorder affects the breakdown of the amino acid phenylalanine, leading to its accumulation in the body and causing brain damage if left untreated.
* Maple syrup urine disease: This disorder affects the breakdown of the branched-chain amino acids leucine, isoleucine, and valine, leading to their accumulation in the body and causing neurological problems.
* Homocystinuria: This disorder affects the breakdown of the amino acid methionine, leading to its accumulation in the body and causing a range of symptoms including developmental delay, intellectual disability, and cardiovascular problems.

Treatment for inborn errors of amino acid metabolism typically involves dietary restrictions or supplementation to manage the levels of affected amino acids in the body. In some cases, medication or other therapies may also be necessary. Early diagnosis and treatment can help prevent or minimize the severity of symptoms and health complications associated with these disorders.

Inborn errors of metabolism (IEM) refer to a group of genetic disorders caused by defects in enzymes or transporters that play a role in the body's metabolic processes. These disorders result in the accumulation or deficiency of specific chemicals within the body, which can lead to various clinical manifestations, such as developmental delay, intellectual disability, seizures, organ damage, and in some cases, death.

Examples of IEM include phenylketonuria (PKU), maple syrup urine disease (MSUD), galactosemia, and glycogen storage diseases, among many others. These disorders are typically inherited in an autosomal recessive manner, meaning that an affected individual has two copies of the mutated gene, one from each parent.

Early diagnosis and management of IEM are crucial to prevent or minimize complications and improve outcomes. Treatment options may include dietary modifications, supplementation with missing enzymes or cofactors, medication, and in some cases, stem cell transplantation or gene therapy.

Glutaryl-CoA Dehydrogenase (GCDH) is an enzyme that plays a crucial role in the catabolism of the amino acids lysine and hydroxylysine. It is located in the inner mitochondrial membrane and functions as a homotetramer, with each subunit containing one molecule of FAD as a cofactor.

GCDH catalyzes the oxidative decarboxylation of glutaryl-CoA to form succinyl-CoA, which is then further metabolized in the citric acid cycle. This reaction also involves the reduction of FAD to FADH2, which can subsequently be used in the electron transport chain to generate ATP.

Deficiency in GCDH function can lead to a rare inherited disorder called glutaric acidemia type I (GA-I), which is characterized by an accumulation of glutaryl-CoA and its metabolites, including glutaric acid and 3-hydroxyglutaric acid. These metabolites can cause neurological damage and intellectual disability if left untreated.

Butyryl-CoA dehydrogenase (BD) is an enzyme that plays a crucial role in the breakdown and metabolism of fatty acids, specifically those with medium chain length. It catalyzes the oxidation of butyryl-CoA to crotonyl-CoA, which is an important step in the beta-oxidation pathway.

The reaction catalyzed by BD can be summarized as follows:

butyryl-CoA + FAD → crotonyl-CoA + FADH2 + CO2

In this reaction, butyryl-CoA is oxidized to crotonyl-CoA, and FAD (flavin adenine dinucleotide) is reduced to FADH2. The release of CO2 is a byproduct of the reaction.

BD is an important enzyme in energy metabolism, as it helps to generate reducing equivalents that can be used in the electron transport chain to produce ATP, the primary source of cellular energy. Deficiencies in BD have been linked to various metabolic disorders, including a rare genetic disorder known as multiple acyl-CoA dehydrogenase deficiency (MADD), which is characterized by impaired fatty acid and amino acid metabolism.

L-Lactate Dehydrogenase (LDH) is an enzyme found in various tissues within the body, including the heart, liver, kidneys, muscles, and brain. It plays a crucial role in the process of energy production, particularly during anaerobic conditions when oxygen levels are low.

In the presence of the coenzyme NADH, LDH catalyzes the conversion of pyruvate to lactate, generating NAD+ as a byproduct. Conversely, in the presence of NAD+, LDH can convert lactate back to pyruvate using NADH. This reversible reaction is essential for maintaining the balance between lactate and pyruvate levels within cells.

Elevated blood levels of LDH may indicate tissue damage or injury, as this enzyme can be released into the circulation following cellular breakdown. As a result, LDH is often used as a nonspecific biomarker for various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and certain types of cancer. However, it's important to note that an isolated increase in LDH does not necessarily pinpoint the exact location or cause of tissue damage, and further diagnostic tests are usually required for confirmation.

I'm sorry for any confusion, but "Mediterranean Islands" is not a term that has a specific medical definition. The Mediterranean Sea is surrounded by many countries and islands, including Cyprus, Sicily, Sardinia, Corsica, Crete, and numerous Greek islands, among others. If you're looking for medical information related to these areas, I would need more specificity. However, if you're interested in general health statistics or demographic data related to these islands, I could try to provide some relevant information.

Hemolytic anemia is a type of anemia that occurs when red blood cells are destroyed (hemolysis) faster than they can be produced. Red blood cells are essential for carrying oxygen throughout the body. When they are destroyed, hemoglobin and other cellular components are released into the bloodstream, which can lead to complications such as kidney damage and gallstones.

Hemolytic anemia can be inherited or acquired. Inherited forms of the condition may result from genetic defects that affect the structure or function of red blood cells. Acquired forms of hemolytic anemia can be caused by various factors, including infections, medications, autoimmune disorders, and certain medical conditions such as cancer or blood disorders.

Symptoms of hemolytic anemia may include fatigue, weakness, shortness of breath, pale skin, jaundice (yellowing of the skin and eyes), dark urine, and a rapid heartbeat. Treatment for hemolytic anemia depends on the underlying cause and may include medications, blood transfusions, or surgery.

Alcohol dehydrogenase (ADH) is a group of enzymes responsible for catalyzing the oxidation of alcohols to aldehydes or ketones, and reducing equivalents such as NAD+ to NADH. In humans, ADH plays a crucial role in the metabolism of ethanol, converting it into acetaldehyde, which is then further metabolized by aldehyde dehydrogenase (ALDH) into acetate. This process helps to detoxify and eliminate ethanol from the body. Additionally, ADH enzymes are also involved in the metabolism of other alcohols, such as methanol and ethylene glycol, which can be toxic if allowed to accumulate in the body.

Electron-transferring flavoproteins (ETFs) are small protein molecules that play a crucial role in the electron transport chain in cells. They are responsible for accepting and donating electrons during various metabolic processes, particularly in the oxidation of fatty acids and amino acids.

ETFs contain a cofactor called flavin adenine dinucleotide (FAD), which can accept two electrons and two protons to form a reduced form of FAD (FADH2). When ETFs receive electrons from other molecules, they transfer these electrons to another protein called electron-transferring flavoprotein dehydrogenase (ETFDH), which then donates the electrons to the main electron transport chain.

Defects in ETFs or ETFDH can lead to serious metabolic disorders, such as multiple acyl-CoA dehydrogenase deficiency (MADD), also known as glutaric acidemia type II. This disorder affects the body's ability to break down certain fats and amino acids, leading to a buildup of toxic compounds in the body and potentially causing serious health problems.

Inborn errors of purine-pyrimidine metabolism refer to genetic disorders that result in dysfunctional enzymes involved in the metabolic pathways of purines and pyrimidines. These are essential components of nucleotides, which in turn are building blocks of DNA and RNA.

Inherited as autosomal recessive or X-linked recessive traits, these disorders can lead to an accumulation of toxic metabolites, a deficiency of necessary compounds, or both. Clinical features vary widely depending on the specific enzyme defect but may include neurologic symptoms, kidney problems, gout, and/or immunodeficiency.

Examples of such disorders include Lesch-Nyhan syndrome (deficiency of hypoxanthine-guanine phosphoribosyltransferase), adenosine deaminase deficiency (leading to severe combined immunodeficiency), and orotic aciduria (due to defects in pyrimidine metabolism). Early diagnosis and management are crucial to improve outcomes.

3-Hydroxysteroid dehydrogenases (3-HSDs) are a group of enzymes that play a crucial role in steroid hormone biosynthesis. These enzymes catalyze the conversion of 3-beta-hydroxy steroids to 3-keto steroids, which is an essential step in the production of various steroid hormones, including progesterone, cortisol, aldosterone, and sex hormones such as testosterone and estradiol.

There are several isoforms of 3-HSDs that are expressed in different tissues and have distinct substrate specificities. For instance, 3-HSD type I is primarily found in the ovary and adrenal gland, where it catalyzes the conversion of pregnenolone to progesterone and 17-hydroxyprogesterone to 17-hydroxycortisol. On the other hand, 3-HSD type II is mainly expressed in the testes, adrenal gland, and placenta, where it catalyzes the conversion of dehydroepiandrosterone (DHEA) to androstenedione and androstenedione to testosterone.

Defects in 3-HSDs can lead to various genetic disorders that affect steroid hormone production and metabolism, resulting in a range of clinical manifestations such as adrenal insufficiency, ambiguous genitalia, and sexual development disorders.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme that plays a crucial role in the metabolic pathway of glycolysis. Its primary function is to convert glyceraldehyde-3-phosphate (a triose sugar phosphate) into D-glycerate 1,3-bisphosphate, while also converting nicotinamide adenine dinucleotide (NAD+) into its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has also been implicated in various non-metabolic processes, including DNA replication, repair, and transcription regulation, due to its ability to interact with different proteins and nucleic acids.

Kernicterus is a severe form of brain damage caused by high levels of bilirubin, a yellow pigment that forms when red blood cells break down. It's most commonly seen in newborns, particularly those with a condition called ABO or Rh incompatibility, where the baby's blood type is different from the mother's. This can lead to an increased breakdown of the baby's red blood cells and a buildup of bilirubin.

In kernicterus, the bilirubin reaches such high levels that it becomes toxic and can damage the brain, particularly areas like the basal ganglia and brainstem. This can result in symptoms such as severe jaundice (a yellowing of the skin and eyes), lethargy, high-pitched crying, poor feeding, and eventually seizures, hearing loss, and developmental delays.

Kernicterus is preventable with timely treatment, which may include phototherapy (using light to break down bilirubin) or exchange transfusion (replacing the baby's blood with fresh donor blood). If you suspect your newborn has jaundice or if their skin appears yellow, it's important to seek medical attention immediately.

Phosphoglycerate Dehydrogenase (PGDH) is a critical enzyme in the metabolic pathway of glycolysis and serine synthesis. It catalyzes the first step in the serine synthesis pathway, where 3-phosphoglycerate is converted to 3-phosphohydroxypyruvate, while also reducing nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide hydride (NADH). This enzyme plays a significant role in cellular metabolism and has been linked to various diseases, including cancer, when its activity is dysregulated.

Primaquine is an antimalarial medication used to prevent and treat malaria caused by Plasmodium falciparum and P. vivax parasites. It is the only antimalarial drug effective against the liver stages (hypnozoites) of P. vivax and P. ovale, which can cause relapses if not treated.

Primaquine works by producing free radicals that damage the malaria parasite's DNA, leading to its death. It is a relatively inexpensive drug and is often used in mass drug administration programs for malaria elimination. However, primaquine can cause hemolysis (destruction of red blood cells) in people with glucose-6-phosphate dehydrogenase (G6PD) deficiency, so it is important to screen for this condition before prescribing the drug.

In addition to its antimalarial properties, primaquine has also been used off-label to treat certain types of cutaneous leishmaniasis, a parasitic disease caused by Leishmania species.

Aldehyde dehydrogenase (ALDH) is a class of enzymes that play a crucial role in the metabolism of alcohol and other aldehydes in the body. These enzymes catalyze the oxidation of aldehydes to carboxylic acids, using nicotinamide adenine dinucleotide (NAD+) as a cofactor.

There are several isoforms of ALDH found in different tissues throughout the body, with varying substrate specificities and kinetic properties. The most well-known function of ALDH is its role in alcohol metabolism, where it converts the toxic aldehyde intermediate acetaldehyde to acetate, which can then be further metabolized or excreted.

Deficiencies in ALDH activity have been linked to a number of clinical conditions, including alcohol flush reaction, alcohol-induced liver disease, and certain types of cancer. Additionally, increased ALDH activity has been associated with chemotherapy resistance in some cancer cells.

Glutamate Dehydrogenase (GLDH or GDH) is a mitochondrial enzyme that plays a crucial role in the metabolism of amino acids, particularly within liver and kidney tissues. It catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate, which links amino acid metabolism with the citric acid cycle and energy production. This enzyme is significant in clinical settings as its levels in blood serum can be used as a diagnostic marker for diseases that damage liver or kidney cells, since these cells release GLDH into the bloodstream upon damage.

Metabolic brain diseases refer to a group of conditions that are caused by disruptions in the body's metabolic processes, which affect the brain. These disorders can be inherited or acquired and can result from problems with the way the body produces, breaks down, or uses energy and nutrients.

Examples of metabolic brain diseases include:

1. Mitochondrial encephalomyopathies: These are a group of genetic disorders that affect the mitochondria, which are the energy-producing structures in cells. When the mitochondria don't function properly, it can lead to muscle weakness, neurological problems, and developmental delays.
2. Leukodystrophies: These are a group of genetic disorders that affect the white matter of the brain, which is made up of nerve fibers covered in myelin, a fatty substance that insulates the fibers and helps them transmit signals. When the myelin breaks down or is not produced properly, it can lead to cognitive decline, motor problems, and other neurological symptoms.
3. Lysosomal storage disorders: These are genetic disorders that affect the lysosomes, which are structures in cells that break down waste products and recycle cellular materials. When the lysosomes don't function properly, it can lead to the accumulation of waste products in cells, including brain cells, causing damage and neurological symptoms.
4. Maple syrup urine disease: This is a genetic disorder that affects the way the body breaks down certain amino acids, leading to a buildup of toxic levels of these substances in the blood and urine. If left untreated, it can cause brain damage, developmental delays, and other neurological problems.
5. Homocystinuria: This is a genetic disorder that affects the way the body processes an amino acid called methionine, leading to a buildup of homocysteine in the blood. High levels of homocysteine can cause damage to the blood vessels and lead to neurological problems, including seizures, developmental delays, and cognitive decline.

Treatment for metabolic brain diseases may involve dietary changes, supplements, medications, or other therapies aimed at managing symptoms and preventing further damage to the brain. In some cases, a stem cell transplant may be recommended as a treatment option.

Dimethylglycine dehydrogenase is an enzyme that plays a role in the metabolism of certain amino acids. The systematic name for this enzyme is N,N-dimethylglycine:electron transfer flavoprotein oxidoreductase. It catalyzes the following chemical reaction:

N,N-dimethylglycine + electron transfer flavoprotein → sarcosine + formaldehyde + reduced electron transfer flavoprotein

This enzyme is found in many organisms, including bacteria and humans. In humans, it is located in the mitochondria and is involved in the breakdown of the amino acid glycine. Mutations in the gene that encodes this enzyme can lead to a rare genetic disorder called dimethylglycine dehydrogenase deficiency, which is characterized by developmental delay, intellectual disability, and seizures.

Malate Dehydrogenase (MDH) is an enzyme that plays a crucial role in the Krebs cycle, also known as the citric acid cycle or tricarboxylic acid (TCA) cycle. It catalyzes the reversible oxidation of malate to oxaloacetate, while simultaneously reducing NAD+ to NADH. This reaction is essential for energy production in the form of ATP and NADH within the cell.

There are two main types of Malate Dehydrogenase:

1. NAD-dependent Malate Dehydrogenase (MDH1): Found primarily in the cytoplasm, this isoform plays a role in the malate-aspartate shuttle, which helps transfer reducing equivalents between the cytoplasm and mitochondria.
2. FAD-dependent Malate Dehydrogenase (MDH2): Located within the mitochondrial matrix, this isoform is involved in the Krebs cycle for energy production.

Abnormal levels of Malate Dehydrogenase enzyme can be indicative of certain medical conditions or diseases, such as myocardial infarction (heart attack), muscle damage, or various types of cancer. Therefore, MDH enzyme activity is often assessed in diagnostic tests to help identify and monitor these health issues.

Isocitrate Dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate to α-ketoglutarate in the presence of NAD+ or NADP+, producing NADH or NADPH respectively. This reaction occurs in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, which is a crucial metabolic pathway in the cell's energy production and biosynthesis of various molecules. There are three isoforms of IDH found in humans: IDH1 located in the cytosol, IDH2 in the mitochondrial matrix, and IDH3 within the mitochondria. Mutations in IDH1 and IDH2 have been associated with several types of cancer, such as gliomas and acute myeloid leukemia (AML), leading to abnormal accumulation of 2-hydroxyglutarate, which can contribute to tumorigenesis.

Reye Syndrome is a rare but serious condition that primarily affects children and teenagers, particularly those who have recently recovered from viral infections such as chickenpox or flu. It is characterized by rapidly progressive encephalopathy (brain dysfunction) and fatty degeneration of the liver.

The exact cause of Reye Syndrome remains unknown, but it has been linked to the use of aspirin and other salicylate-containing medications during viral illnesses. The American Academy of Pediatrics recommends avoiding the use of aspirin in children and teenagers with chickenpox or flu-like symptoms due to this association.

Early symptoms of Reye Syndrome include persistent vomiting, diarrhea, and listlessness. As the condition progresses, symptoms can worsen and may include disorientation, seizures, coma, and even death in severe cases. Diagnosis is typically based on clinical presentation, laboratory tests, and sometimes a liver biopsy.

Treatment for Reye Syndrome involves supportive care, such as fluid and electrolyte management, addressing metabolic abnormalities, controlling intracranial pressure, and providing ventilatory support if necessary. Early recognition and intervention are crucial to improving outcomes in affected individuals.

A newborn infant is a baby who is within the first 28 days of life. This period is also referred to as the neonatal period. Newborns require specialized care and attention due to their immature bodily systems and increased vulnerability to various health issues. They are closely monitored for signs of well-being, growth, and development during this critical time.

Methylphenazonium methosulfate is not a medication itself, but rather a reagent used in the production and pharmacological research of certain medications. It's commonly used as a redox mediator, which means it helps to facilitate electron transfer in chemical reactions. In medical contexts, it may be used in the laboratory synthesis or testing of some drugs.

It's important to note that methylphenazonium methosulfate is not intended for direct medical use in humans or animals. Always consult with a healthcare professional or trusted medical source for information regarding specific medications and their uses.

Neonatal jaundice is a medical condition characterized by the yellowing of a newborn baby's skin and eyes due to an excess of bilirubin in the blood. Bilirubin is a yellowish substance produced by the normal breakdown of red blood cells, which are then processed by the liver and excreted through the bile. In neonatal jaundice, the liver is not yet fully developed and cannot process bilirubin quickly enough, leading to its accumulation in the body.

Neonatal jaundice typically appears within the first 2-4 days of life and can range from mild to severe. Mild cases may resolve on their own without treatment, while more severe cases may require medical intervention such as phototherapy or a blood transfusion. Risk factors for neonatal jaundice include prematurity, bruising during birth, blood type incompatibility between mother and baby, and certain genetic disorders.

It is important to monitor newborns closely for signs of jaundice and seek medical attention if concerned, as untreated neonatal jaundice can lead to serious complications such as brain damage or hearing loss.

Alcohol oxidoreductases are a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones, while reducing nicotinamide adenine dinucleotide (NAD+) to NADH. These enzymes play an important role in the metabolism of alcohols and other organic compounds in living organisms.

The most well-known example of an alcohol oxidoreductase is alcohol dehydrogenase (ADH), which is responsible for the oxidation of ethanol to acetaldehyde in the liver during the metabolism of alcoholic beverages. Other examples include aldehyde dehydrogenases (ALDH) and sorbitol dehydrogenase (SDH).

These enzymes are important targets for the development of drugs used to treat alcohol use disorder, as inhibiting their activity can help to reduce the rate of ethanol metabolism and the severity of its effects on the body.

Gilbert's disease, also known as Gilbert's syndrome, is a common and mild condition characterized by **intermittent** elevations in bilirubin levels in the bloodstream without any evidence of liver damage or disease. Bilirubin is a yellowish pigment that forms when hemoglobin breaks down. Normally, it gets processed in the liver and excreted through bile.

In Gilbert's disease, there is an impaired ability to conjugate bilirubin due to a deficiency or dysfunction of the enzyme UDP-glucuronosyltransferase 1A1 (UGT1A1), which is responsible for the glucuronidation process. This results in mild unconjugated hyperbilirubinemia, where bilirubin levels may rise and cause mild jaundice, particularly during times of fasting, illness, stress, or dehydration.

Gilbert's disease is typically an incidental finding, as it usually does not cause any significant symptoms or complications. It is often discovered during routine blood tests when bilirubin levels are found to be slightly elevated. The condition is usually harmless and does not require specific treatment, but avoiding triggers like fasting or dehydration may help minimize the occurrence of jaundice.

Dihydrolipoamide dehydrogenase (DHLD) is an enzyme that plays a crucial role in several important metabolic pathways in the human body, including the citric acid cycle and the catabolism of certain amino acids. DHLD is a component of multi-enzyme complexes, such as the pyruvate dehydrogenase complex (PDC) and the alpha-ketoglutarate dehydrogenase complex (KGDC).

The primary function of DHLD is to catalyze the oxidation of dihydrolipoamide, a reduced form of lipoamide, back to its oxidized state (lipoamide) while simultaneously reducing NAD+ to NADH. This reaction is essential for the continued functioning of the PDC and KGDC, as dihydrolipoamide is a cofactor for these enzyme complexes.

Deficiencies in DHLD can lead to serious metabolic disorders, such as maple syrup urine disease (MSUD) and riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency (RR-MADD). These conditions can result in neurological symptoms, developmental delays, and metabolic acidosis, among other complications. Treatment typically involves dietary modifications, supplementation with specific nutrients, and, in some cases, enzyme replacement therapy.

Glycogen Storage Disease Type I (GSD I) is a rare inherited metabolic disorder caused by deficiency of the enzyme glucose-6-phosphatase, which is necessary for the liver to release glucose into the bloodstream. This leads to an accumulation of glycogen in the liver and abnormally low levels of glucose in the blood (hypoglycemia).

There are two main subtypes of GSD I: Type Ia and Type Ib. In Type Ia, there is a deficiency of both glucose-6-phosphatase enzyme activity in the liver, kidney, and intestine, leading to hepatomegaly (enlarged liver), hypoglycemia, lactic acidosis, hyperlipidemia, and growth retardation. Type Ib is characterized by a deficiency of glucose-6-phosphatase enzyme activity only in the neutrophils, leading to recurrent bacterial infections.

GSD I requires lifelong management with frequent feedings, high-carbohydrate diet, and avoidance of fasting to prevent hypoglycemia. In some cases, treatment with continuous cornstarch infusions or liver transplantation may be necessary.

Succinate dehydrogenase (SDH) is an enzyme complex that plays a crucial role in the process of cellular respiration, specifically in the citric acid cycle (also known as the Krebs cycle) and the electron transport chain. It is located in the inner mitochondrial membrane of eukaryotic cells.

SDH catalyzes the oxidation of succinate to fumarate, converting it into a molecule of fadaquate in the process. During this reaction, two electrons are transferred from succinate to the FAD cofactor within the SDH enzyme complex, reducing it to FADH2. These electrons are then passed on to ubiquinone (CoQ), which is a mobile electron carrier in the electron transport chain, leading to the generation of ATP, the main energy currency of the cell.

SDH is also known as mitochondrial complex II because it is the second complex in the electron transport chain. Mutations in the genes encoding SDH subunits or associated proteins have been linked to various human diseases, including hereditary paragangliomas, pheochromocytomas, gastrointestinal stromal tumors (GISTs), and some forms of neurodegenerative disorders.

Carbohydrate dehydrogenases are a group of enzymes that catalyze the oxidation of carbohydrates, including sugars and sugar alcohols. These enzymes play a crucial role in cellular metabolism by helping to convert these molecules into forms that can be used for energy or as building blocks for other biological compounds.

During the oxidation process, carbohydrate dehydrogenases remove hydrogen atoms from the carbohydrate substrate and transfer them to an electron acceptor, such as NAD+ or FAD. This results in the formation of a ketone or aldehyde group on the carbohydrate molecule and the reduction of the electron acceptor to NADH or FADH2.

Carbohydrate dehydrogenases are classified into several subgroups based on their substrate specificity, cofactor requirements, and other factors. Some examples include glucose dehydrogenase, galactose dehydrogenase, and sorbitol dehydrogenase.

These enzymes have important applications in various fields, including biotechnology, medicine, and industry. For example, they can be used to detect or quantify specific carbohydrates in biological samples, or to produce valuable chemical compounds through the oxidation of renewable resources such as plant-derived sugars.

L-Iditol 2-Dehydrogenase is an enzyme that catalyzes the chemical reaction between L-iditol and NAD+ to produce L-sorbose and NADH + H+. This enzyme plays a role in the metabolism of sugars, specifically in the conversion of L-iditol to L-sorbose in various organisms, including bacteria and fungi. The reaction catalyzed by this enzyme is part of the polyol pathway, which is involved in the regulation of osmotic pressure and other cellular processes.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Hemolysis is the destruction or breakdown of red blood cells, resulting in the release of hemoglobin into the surrounding fluid (plasma). This process can occur due to various reasons such as chemical agents, infections, autoimmune disorders, mechanical trauma, or genetic abnormalities. Hemolysis may lead to anemia and jaundice, among other complications. It is essential to monitor hemolysis levels in patients undergoing medical treatments that might cause this condition.

Hirsutism is a medical condition characterized by excessive hair growth in women in areas where hair growth is typically androgen-dependent, such as the face, chest, lower abdomen, and inner thighs. This hair growth is often thick, dark, and coarse, resembling male-pattern hair growth. Hirsutism can be caused by various factors, including hormonal imbalances, certain medications, and genetic conditions. It's essential to consult a healthcare professional if you experience excessive or unwanted hair growth to determine the underlying cause and develop an appropriate treatment plan.

Mitochondrial trifunctional protein (MTP) is a complex enzyme system located in the inner mitochondrial membrane of cells. It plays a crucial role in fatty acid oxidation, which is the process by which fatty acids are broken down to produce energy in the form of ATP.

MTP consists of three distinct enzymatic activities: long-chain enoyl-CoA hydratase, long-chain 3-hydroxyacyl-CoA dehydrogenase, and long-chain 3-ketoacyl-CoA thiolase. These enzymes work together to catalyze three consecutive reactions in the final steps of mitochondrial fatty acid oxidation, particularly for fatty acids with chain lengths greater than 12 carbons.

Deficiencies in MTP can lead to serious metabolic disorders known as mitochondrial trifunctional protein deficiency (MTPD). This rare genetic condition can cause a range of symptoms, including hypoketotic hypoglycemia, cardiomyopathy, skeletal muscle weakness, and neurological impairment. Early diagnosis and management of MTPD are essential to prevent severe complications and improve the patient's quality of life.

Oxidoreductases acting on CH-CH group donors are a class of enzymes within the larger group of oxidoreductases, which are responsible for catalyzing oxidation-reduction reactions. Specifically, this subclass of enzymes acts upon donors containing a carbon-carbon (CH-CH) bond, where one atom or group of atoms is oxidized and another is reduced during the reaction process. These enzymes play crucial roles in various metabolic pathways, including the breakdown and synthesis of carbohydrates, lipids, and amino acids.

The reactions catalyzed by these enzymes involve the transfer of electrons and hydrogen atoms between the donor and an acceptor molecule. This process often results in the formation or cleavage of carbon-carbon bonds, making them essential for numerous biological processes. The systematic name for this class of enzymes is typically structured as "donor:acceptor oxidoreductase," where donor and acceptor represent the molecules involved in the electron transfer process.

Examples of enzymes that fall under this category include:

1. Aldehyde dehydrogenases (EC 1.2.1.3): These enzymes catalyze the oxidation of aldehydes to carboxylic acids, using NAD+ as an electron acceptor.
2. Dihydrodiol dehydrogenase (EC 1.3.1.14): This enzyme is responsible for the oxidation of dihydrodiols to catechols in the biodegradation of aromatic compounds.
3. Succinate dehydrogenase (EC 1.3.5.1): A key enzyme in the citric acid cycle, succinate dehydrogenase catalyzes the oxidation of succinate to fumarate and reduces FAD to FADH2.
4. Xylose reductase (EC 1.1.1.307): This enzyme is involved in the metabolism of pentoses, where it reduces xylose to xylitol using NADPH as a cofactor.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Glycerol-3-phosphate dehydrogenase (GPD) is an enzyme that plays a crucial role in the metabolism of glucose and lipids. It catalyzes the conversion of dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate (G3P), which is a key intermediate in the synthesis of triglycerides, phospholipids, and other glycerophospholipids.

There are two main forms of GPD: a cytoplasmic form (GPD1) and a mitochondrial form (GPD2). The cytoplasmic form is involved in the production of NADH, which is used in various metabolic processes, while the mitochondrial form is involved in the production of ATP, the main energy currency of the cell.

Deficiencies or mutations in GPD can lead to a variety of metabolic disorders, including glycerol kinase deficiency and congenital muscular dystrophy. Elevated levels of GPD have been observed in certain types of cancer, suggesting that it may play a role in tumor growth and progression.

Neonatal hyperbilirubinemia is a condition characterized by an excessively high level of bilirubin in the blood of newborn infants. Bilirubin is a yellowish pigment produced by the normal breakdown of red blood cells. Normally, bilirubin is processed by the liver and excreted through the bile into the digestive system. However, in neonatal hyperbilirubinemia, the liver may be unable to process bilirubin quickly enough, leading to its accumulation in the bloodstream. This can cause the skin and eyes of the newborn to appear yellow, a condition known as jaundice.

Neonatal hyperbilirubinemia is relatively common and usually resolves on its own within a few days or weeks. However, if bilirubin levels become too high, they can cause brain damage (kernicterus) in severe cases. Treatment may include phototherapy to help break down bilirubin, exchange transfusions, or other interventions to support liver function and reduce bilirubin levels.

An exchange transfusion of whole blood is a medical procedure in which a patient's blood is gradually replaced with donor whole blood. This procedure is typically performed in newborns or infants who have severe jaundice caused by excessive levels of bilirubin, a yellowish pigment that forms when hemoglobin from red blood cells breaks down.

During an exchange transfusion, the baby's blood is removed through a vein or artery and replaced with donor whole blood through another vein or artery. The process is repeated several times until a significant portion of the baby's blood has been exchanged with donor blood. This helps to reduce the levels of bilirubin in the baby's blood, which can help prevent or treat brain damage caused by excessive bilirubin.

Exchange transfusions are typically performed in a neonatal intensive care unit (NICU) and require close monitoring by a team of healthcare professionals. The procedure carries some risks, including infection, bleeding, and changes in blood pressure or heart rate. However, it can be a lifesaving treatment for newborns with severe jaundice who are at risk of developing serious complications.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

17-alpha-Hydroxypregnenolone is a steroid hormone that is produced in the adrenal glands and, to a lesser extent, in the gonads (ovaries and testes). It is an intermediate in the biosynthesis of steroid hormones, including cortisol, aldosterone, and sex hormones such as testosterone and estrogen.

17-alpha-Hydroxypregnenolone is formed from pregnenolone through the action of the enzyme 17α-hydroxylase. It can then be converted to 17-hydroxyprogesterone, which is a precursor to both cortisol and androgens such as testosterone.

While 17-alpha-Hydroxypregnenolone itself does not have significant physiological activity, its role in the biosynthesis of other steroid hormones makes it an important intermediate in the endocrine system. Dysregulation of its production or metabolism can contribute to various medical conditions, such as congenital adrenal hyperplasia and certain forms of cancer.

Hydroxysteroid dehydrogenases (HSDs) are a group of enzymes that play a crucial role in steroid hormone metabolism. They catalyze the oxidation and reduction reactions of hydroxyl groups on the steroid molecule, which can lead to the activation or inactivation of steroid hormones. HSDs are involved in the conversion of various steroids, including sex steroids (e.g., androgens, estrogens) and corticosteroids (e.g., cortisol, cortisone). These enzymes can be found in different tissues throughout the body, and their activity is regulated by various factors, such as hormones, growth factors, and cytokines. Dysregulation of HSDs has been implicated in several diseases, including cancer, diabetes, and cardiovascular disease.

Hyperbilirubinemia is a medical condition characterized by an excessively high level of bilirubin in the bloodstream. Bilirubin is a yellowish pigment produced by the liver when it breaks down old red blood cells. Normally, bilirubin is conjugated (made water-soluble) in the liver and then excreted through the bile into the digestive system. However, if there is a problem with the liver's ability to process or excrete bilirubin, it can build up in the blood, leading to hyperbilirubinemia.

Hyperbilirubinemia can be classified as either unconjugated or conjugated, depending on whether the bilirubin is in its direct (conjugated) or indirect (unconjugated) form. Unconjugated hyperbilirubinemia can occur due to increased production of bilirubin (such as in hemolytic anemia), decreased uptake of bilirubin by the liver, or impaired conjugation of bilirubin in the liver. Conjugated hyperbilirubinemia, on the other hand, is usually caused by a problem with the excretion of conjugated bilirubin into the bile, such as in cholestatic liver diseases like hepatitis or cirrhosis.

Symptoms of hyperbilirubinemia can include jaundice (yellowing of the skin and eyes), dark urine, light-colored stools, itching, and fatigue. Treatment depends on the underlying cause of the condition and may involve medications, dietary changes, or surgery.

Glucose 1-Dehydrogenase (G1DH) is an enzyme that catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone and reduces the cofactor NAD+ into NADH. This reaction plays a role in various biological processes, including glucose sensing and detoxification of reactive carbonyl species. G1DH is found in many organisms, including humans, and has several isoforms with different properties and functions.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

The Ketoglutarate Dehydrogenase Complex (KGDC or α-KGDH) is a multi-enzyme complex that plays a crucial role in the Krebs cycle, also known as the citric acid cycle. It is located within the mitochondrial matrix of eukaryotic cells and functions to catalyze the oxidative decarboxylation of α-ketoglutarate into succinyl-CoA, thereby connecting the Krebs cycle to the electron transport chain for energy production.

The KGDC is composed of three distinct enzymes:

1. α-Ketoglutarate dehydrogenase (E1): This enzyme catalyzes the decarboxylation and oxidation of α-ketoglutarate to form a thioester intermediate with lipoamide, which is bound to the E2 component.
2. Dihydrolipoyl succinyltransferase (E2): This enzyme facilitates the transfer of the acetyl group from the lipoamide cofactor to CoA, forming succinyl-CoA and regenerating oxidized lipoamide.
3. Dihydrolipoyl dehydrogenase (E3): The final enzyme in the complex catalyzes the reoxidation of reduced lipoamide back to its disulfide form, using FAD as a cofactor and transferring electrons to NAD+, forming NADH.

The KGDC is subject to regulation by several mechanisms, including phosphorylation-dephosphorylation reactions that can inhibit or activate the complex, respectively. Dysfunction of this enzyme complex has been implicated in various diseases, such as neurodegenerative disorders and cancer.

Aldehyde oxidoreductases are a class of enzymes that catalyze the oxidation of aldehydes to carboxylic acids using NAD+ or FAD as cofactors. They play a crucial role in the detoxification of aldehydes generated from various metabolic processes, such as lipid peroxidation and alcohol metabolism. These enzymes are widely distributed in nature and have been identified in bacteria, yeast, plants, and animals.

The oxidation reaction catalyzed by aldehyde oxidoreductases involves the transfer of electrons from the aldehyde substrate to the cofactor, resulting in the formation of a carboxylic acid and reduced NAD+ or FAD. The enzymes are classified into several families based on their sequence similarity and cofactor specificity.

One of the most well-known members of this family is alcohol dehydrogenase (ADH), which catalyzes the oxidation of alcohols to aldehydes or ketones as part of the alcohol metabolism pathway. Another important member is aldehyde dehydrogenase (ALDH), which further oxidizes the aldehydes generated by ADH to carboxylic acids, thereby preventing the accumulation of toxic aldehydes in the body.

Deficiencies in ALDH enzymes have been linked to several human diseases, including alcoholism and certain types of cancer. Therefore, understanding the structure and function of aldehyde oxidoreductases is essential for developing new therapeutic strategies to treat these conditions.

Mitochondrial diseases are a group of disorders caused by dysfunctions in the mitochondria, which are the energy-producing structures in cells. These diseases can affect people of any age and can manifest in various ways, depending on which organs or systems are affected. Common symptoms include muscle weakness, neurological problems, cardiac disease, diabetes, and vision/hearing loss. Mitochondrial diseases can be inherited from either the mother's or father's side, or they can occur spontaneously due to genetic mutations. They can range from mild to severe and can even be life-threatening in some cases.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Sickle cell trait is a genetic condition where an individual inherits one abnormal gene for hemoglobin S (HbS) from one parent and one normal gene for hemoglobin A (HbA) from the other parent. Hemoglobin is a protein in red blood cells that carries oxygen throughout the body.

People with sickle cell trait do not have sickle cell disease, but they can pass the abnormal HbS gene on to their children. In certain situations, such as high altitude, low oxygen levels, or intense physical exertion, individuals with sickle cell trait may experience symptoms similar to those of sickle cell disease, such as fatigue, pain, and shortness of breath. However, these symptoms are typically milder and less frequent than in people with sickle cell disease.

It is important for individuals who know they have sickle cell trait to inform their healthcare providers, especially if they become pregnant or plan to engage in activities that may cause low oxygen levels, such as scuba diving or high-altitude climbing.

Peroxisomal multifunctional protein-2 (MFP2) is a key enzyme found within peroxisomes, which are membrane-bound organelles present in eukaryotic cells. MFP2 plays a crucial role in the breakdown of fatty acids and the detoxification of harmful substances within peroxisomes. It is involved in multiple steps of these processes, hence the term "multifunctional."

MFP2 catalyzes several reactions during the beta-oxidation of fatty acids, a process that breaks down long-chain fatty acids into shorter ones to generate energy for the cell. Specifically, MFP2 helps convert the breakdown products from earlier steps into forms that can enter subsequent steps of the beta-oxidation pathway.

Additionally, MFP2 is involved in the detoxification of molecules such as methanol and formaldehyde by facilitating their conversion to less harmful substances. This enzyme helps convert methanol into formic acid and then further metabolizes it, while formaldehyde is converted to formate.

Deficiencies in MFP2 or other peroxisomal proteins can lead to severe inherited metabolic disorders known as peroxisome biogenesis disorders (PBDs). These conditions can affect multiple organ systems and may cause neurological symptoms, developmental delays, vision loss, and hearing impairment.

Erythrocytes, also known as red blood cells (RBCs), are the most common type of blood cell in circulating blood in mammals. They are responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues to the lungs.

Erythrocytes are formed in the bone marrow and have a biconcave shape, which allows them to fold and bend easily as they pass through narrow blood vessels. They do not have a nucleus or mitochondria, which makes them more flexible but also limits their ability to reproduce or repair themselves.

In humans, erythrocytes are typically disc-shaped and measure about 7 micrometers in diameter. They contain the protein hemoglobin, which binds to oxygen and gives blood its red color. The lifespan of an erythrocyte is approximately 120 days, after which it is broken down in the liver and spleen.

Abnormalities in erythrocyte count or function can lead to various medical conditions, such as anemia, polycythemia, and sickle cell disease.

Phosphogluconate dehydrogenase (PGD) is an enzyme that plays a crucial role in the pentose phosphate pathway, which is a metabolic pathway that supplies reducing energy to cells by converting glucose into ribose-5-phosphate and NADPH.

PGD catalyzes the third step of this pathway, in which 6-phosphogluconate is converted into ribulose-5-phosphate, with the concurrent reduction of NADP+ to NADPH. This reaction is essential for the generation of NADPH, which serves as a reducing agent in various cellular processes, including fatty acid synthesis and antioxidant defense.

Deficiencies in PGD can lead to several metabolic disorders, such as congenital nonspherocytic hemolytic anemia, which is characterized by the premature destruction of red blood cells due to a defect in the pentose phosphate pathway.

Congenital Adrenal Hyperplasia (CAH) is a group of inherited genetic disorders that affect the adrenal glands, which are triangular-shaped glands located on top of the kidneys. The adrenal glands are responsible for producing several essential hormones, including cortisol, aldosterone, and androgens.

CAH is caused by mutations in genes that code for enzymes involved in the synthesis of these hormones. The most common form of CAH is 21-hydroxylase deficiency, which affects approximately 90% to 95% of all cases. Other less common forms of CAH include 11-beta-hydroxylase deficiency and 3-beta-hydroxysteroid dehydrogenase deficiency.

The severity of the disorder can vary widely, depending on the degree of enzyme deficiency. In severe cases, the lack of cortisol production can lead to life-threatening salt wasting and electrolyte imbalances in newborns. The excess androgens produced due to the enzyme deficiency can also cause virilization, or masculinization, of female fetuses, leading to ambiguous genitalia at birth.

In milder forms of CAH, symptoms may not appear until later in childhood or even adulthood. These may include early puberty, rapid growth followed by premature fusion of the growth plates and short stature, acne, excessive hair growth, irregular menstrual periods, and infertility.

Treatment for CAH typically involves replacing the missing hormones with medications such as hydrocortisone, fludrocortisone, and/or sex hormones. Regular monitoring of hormone levels and careful management of medication doses is essential to prevent complications such as adrenal crisis, growth suppression, and osteoporosis.

In severe cases of CAH, early diagnosis and treatment can help prevent or minimize the risk of serious health problems and improve quality of life. Genetic counseling may also be recommended for affected individuals and their families to discuss the risks of passing on the disorder to future generations.

Glucose dehydrogenases (GDHs) are a group of enzymes that catalyze the oxidation of glucose to generate gluconic acid or glucuronic acid. This reaction involves the transfer of electrons from glucose to an electron acceptor, most commonly nicotinamide adenine dinucleotide (NAD+) or phenazine methosulfate (PMS).

GDHs are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They play important roles in different biological processes, such as glucose metabolism, energy production, and detoxification of harmful substances. Based on their cofactor specificity, GDHs can be classified into two main types: NAD(P)-dependent GDHs and PQQ-dependent GDHs.

NAD(P)-dependent GDHs use NAD+ or NADP+ as a cofactor to oxidize glucose to glucono-1,5-lactone, which is then hydrolyzed to gluconic acid by an accompanying enzyme. These GDHs are involved in various metabolic pathways, such as the Entner-Doudoroff pathway and the oxidative pentose phosphate pathway.

PQQ-dependent GDHs, on the other hand, use pyrroloquinoline quinone (PQQ) as a cofactor to catalyze the oxidation of glucose to gluconic acid directly. These GDHs are typically found in bacteria and play a role in energy production and detoxification.

Overall, glucose dehydrogenases are essential enzymes that contribute to the maintenance of glucose homeostasis and energy balance in living organisms.

Sugar alcohol dehydrogenases (SADHs) are a group of enzymes that catalyze the interconversion between sugar alcohols and sugars, which involves the gain or loss of a pair of electrons, typically in the form of NAD(P)+/NAD(P)H. These enzymes play a crucial role in the metabolism of sugar alcohols, which are commonly found in various plants and some microorganisms.

Sugar alcohols, also known as polyols, are reduced forms of sugars that contain one or more hydroxyl groups instead of aldehyde or ketone groups. Examples of sugar alcohols include sorbitol, mannitol, xylitol, and erythritol. SADHs can interconvert these sugar alcohols to their corresponding sugars through a redox reaction that involves the transfer of hydrogen atoms.

The reaction catalyzed by SADHs is typically represented as follows:

R-CH(OH)-CH2OH + NAD(P)+ ↔ R-CO-CH2OH + NAD(P)H + H+

where R represents a carbon chain, and CH(OH)-CH2OH and CO-CH2OH represent the sugar alcohol and sugar forms, respectively.

SADHs are widely distributed in nature and have been found in various organisms, including bacteria, fungi, plants, and animals. These enzymes have attracted significant interest in biotechnology due to their potential applications in the production of sugar alcohols and other value-added products. Additionally, SADHs have been studied as targets for developing novel antimicrobial agents, as inhibiting these enzymes can disrupt the metabolism of certain pathogens that rely on sugar alcohols for growth and survival.

I'm sorry for any confusion, but "Jordan" is not a medical term or condition. It is most commonly known as the name of a country in the Middle East, as well as a personal name for both males and females. If you have any medical concerns or questions, I would be happy to try to help clarify or provide information based on appropriate medical terminology and concepts.

NADH dehydrogenase, also known as Complex I, is an enzyme complex in the electron transport chain located in the inner mitochondrial membrane. It catalyzes the oxidation of NADH to NAD+ and the reduction of coenzyme Q to ubiquinol, playing a crucial role in cellular respiration and energy production. The reaction involves the transfer of electrons from NADH to coenzyme Q, which contributes to the generation of a proton gradient across the membrane, ultimately leading to ATP synthesis. Defects in NADH dehydrogenase can result in various mitochondrial diseases and disorders.

Sudden Infant Death Syndrome (SIDS) is defined by the American Academy of Pediatrics as "the sudden unexpected death of an infant

Thalassemia is a group of inherited genetic disorders that affect the production of hemoglobin, a protein in red blood cells responsible for carrying oxygen throughout the body. The disorder results in less efficient or abnormal hemoglobin, which can lead to anemia, an insufficient supply of oxygen-rich red blood cells.

There are two main types of Thalassemia: alpha and beta. Alpha thalassemia occurs when there is a problem with the alpha globin chain production, while beta thalassemia results from issues in beta globin chain synthesis. These disorders can range from mild to severe, depending on the number of genes affected and their specific mutations.

Severe forms of Thalassemia may require regular blood transfusions, iron chelation therapy, or even a bone marrow transplant to manage symptoms and prevent complications.

A heterozygote is an individual who has inherited two different alleles (versions) of a particular gene, one from each parent. This means that the individual's genotype for that gene contains both a dominant and a recessive allele. The dominant allele will be expressed phenotypically (outwardly visible), while the recessive allele may or may not have any effect on the individual's observable traits, depending on the specific gene and its function. Heterozygotes are often represented as 'Aa', where 'A' is the dominant allele and 'a' is the recessive allele.

Inosine Monophosphate Dehydrogenase (IMDH or IMPDH) is an enzyme that is involved in the de novo biosynthesis of guanine nucleotides. It catalyzes the conversion of inosine monophosphate (IMP) to xanthosine monophosphate (XMP), which is the rate-limiting step in the synthesis of guanosine triphosphate (GTP).

There are two isoforms of IMPDH, type I and type II, which are encoded by separate genes. Type I IMPDH is expressed in most tissues, while type II IMPDH is primarily expressed in lymphocytes and other cells involved in the immune response. Inhibitors of IMPDH have been developed as immunosuppressive drugs to prevent rejection of transplanted organs. Defects in the gene encoding IMPDH type II have been associated with retinal degeneration and hearing loss.

Muscular diseases, also known as myopathies, refer to a group of conditions that affect the functionality and health of muscle tissue. These diseases can be inherited or acquired and may result from inflammation, infection, injury, or degenerative processes. They can cause symptoms such as weakness, stiffness, cramping, spasms, wasting, and loss of muscle function.

Examples of muscular diseases include:

1. Duchenne Muscular Dystrophy (DMD): A genetic disorder that results in progressive muscle weakness and degeneration due to a lack of dystrophin protein.
2. Myasthenia Gravis: An autoimmune disease that causes muscle weakness and fatigue, typically affecting the eyes and face, throat, and limbs.
3. Inclusion Body Myositis (IBM): A progressive muscle disorder characterized by muscle inflammation and wasting, typically affecting older adults.
4. Polymyositis: An inflammatory myopathy that causes muscle weakness and inflammation throughout the body.
5. Metabolic Myopathies: A group of inherited disorders that affect muscle metabolism, leading to exercise intolerance, muscle weakness, and other symptoms.
6. Muscular Dystonias: Involuntary muscle contractions and spasms that can cause abnormal postures or movements.

It is important to note that muscular diseases can have a significant impact on an individual's quality of life, mobility, and overall health. Proper diagnosis and treatment are crucial for managing symptoms and improving outcomes.

Lactate dehydrogenases (LDH) are a group of intracellular enzymes found in nearly all human cells, particularly in the heart, liver, kidneys, muscles, and brain. They play a crucial role in energy production during anaerobic metabolism, converting pyruvate to lactate while regenerating NAD+ from NADH. LDH exists as multiple isoenzymes (LDH-1 to LDH-5) in the body, each with distinct distributions and functions.

An elevated level of LDH in the blood may indicate tissue damage or injury, as these enzymes are released into the circulation following cellular destruction. Therefore, measuring LDH levels is a common diagnostic tool to assess various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and some types of cancer. However, an isolated increase in LDH may not be specific enough for a definitive diagnosis, and additional tests are usually required for confirmation.

17-Hydroxysteroid dehydrogenases (17-HSDs) are a group of enzymes that play a crucial role in steroid hormone biosynthesis. They are involved in the conversion of 17-ketosteroids to 17-hydroxy steroids or vice versa, by adding or removing a hydroxyl group (–OH) at the 17th carbon atom of the steroid molecule. This conversion is essential for the production of various steroid hormones, including cortisol, aldosterone, and sex hormones such as estrogen and testosterone.

There are several isoforms of 17-HSDs, each with distinct substrate specificities, tissue distributions, and functions:

1. 17-HSD type 1 (17-HSD1): This isoform primarily catalyzes the conversion of estrone (E1) to estradiol (E2), an active form of estrogen. It is mainly expressed in the ovary, breast, and adipose tissue.
2. 17-HSD type 2 (17-HSD2): This isoform catalyzes the reverse reaction, converting estradiol (E2) to estrone (E1). It is primarily expressed in the placenta, prostate, and breast tissue.
3. 17-HSD type 3 (17-HSD3): This isoform is responsible for the conversion of androstenedione to testosterone, an essential step in male sex hormone biosynthesis. It is predominantly expressed in the testis and adrenal gland.
4. 17-HSD type 4 (17-HSD4): This isoform catalyzes the conversion of dehydroepiandrosterone (DHEA) to androstenedione, an intermediate step in steroid hormone biosynthesis. It is primarily expressed in the placenta.
5. 17-HSD type 5 (17-HSD5): This isoform catalyzes the conversion of cortisone to cortisol, a critical step in glucocorticoid biosynthesis. It is predominantly expressed in the adrenal gland and liver.
6. 17-HSD type 6 (17-HSD6): This isoform catalyzes the conversion of androstenedione to testosterone, similar to 17-HSD3. However, it has a different substrate specificity and is primarily expressed in the ovary.
7. 17-HSD type 7 (17-HSD7): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the ovary.
8. 17-HSD type 8 (17-HSD8): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
9. 17-HSD type 9 (17-HSD9): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
10. 17-HSD type 10 (17-HSD10): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
11. 17-HSD type 11 (17-HSD11): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
12. 17-HSD type 12 (17-HSD12): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
13. 17-HSD type 13 (17-HSD13): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
14. 17-HSD type 14 (17-HSD14): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
15. 17-HSD type 15 (17-HSD15): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
16. 17-HSD type 16 (17-HSD16): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
17. 17-HSD type 17 (17-HSD17): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
18. 17-HSD type 18 (17-HSD18): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
19. 17-HSD type 19 (17-HSD19): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
20. 17-HSD type 20 (17-HSD20): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
21. 17-HSD type 21 (17-HSD21): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
22. 17-HSD type 22 (17-HSD22): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
23. 17-HSD type 23 (17-HSD23): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
24. 17-HSD type 24 (17-HSD24): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
25. 17-HSD type 25 (17-HSD25): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
26. 17-HSD type 26 (17-HSD26): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Formate dehydrogenases (FDH) are a group of enzymes that catalyze the oxidation of formic acid (formate) to carbon dioxide and hydrogen or to carbon dioxide and water, depending on the type of FDH. The reaction is as follows:

Formic acid + Coenzyme Q (or NAD+) -> Carbon dioxide + H2 (or H2O) + Reduced coenzyme Q (or NADH)

FDHs are widely distributed in nature and can be found in various organisms, including bacteria, archaea, and eukaryotes. They play a crucial role in the metabolism of many microorganisms that use formate as an electron donor for energy conservation or as a carbon source for growth. In addition to their biological significance, FDHs have attracted much interest as biocatalysts for various industrial applications, such as the production of hydrogen, reduction of CO2, and detoxification of formic acid in animal feed.

FDHs can be classified into two main types based on their cofactor specificity: NAD-dependent FDHs and quinone-dependent FDHs. NAD-dependent FDHs use nicotinamide adenine dinucleotide (NAD+) as a cofactor, while quinone-dependent FDHs use menaquinone or ubiquinone as a cofactor. Both types of FDHs have a similar reaction mechanism that involves the transfer of a hydride ion from formate to the cofactor and the release of carbon dioxide.

FDHs are composed of two subunits: a small subunit containing one or two [4Fe-4S] clusters and a large subunit containing a molybdenum cofactor (Moco) and one or two [2Fe-2S] clusters. Moco is a complex prosthetic group that consists of a pterin ring, a dithiolene group, and a molybdenum atom coordinated to three ligands: a sulfur atom from the dithiolene group, a terminal oxygen atom from a mononucleotide, and a serine residue. The molybdenum center can adopt different oxidation states (+4, +5, or +6) during the catalytic cycle, allowing for the transfer of electrons and the activation of formate.

FDHs have various applications in biotechnology and industry, such as the production of hydrogen gas, the removal of nitrate from wastewater, and the synthesis of fine chemicals. The high selectivity and efficiency of FDHs make them attractive catalysts for these processes, which require mild reaction conditions and low energy inputs. However, the stability and activity of FDHs are often limited by their sensitivity to oxygen and other inhibitors, which can affect their performance in industrial settings. Therefore, efforts have been made to improve the properties of FDHs through protein engineering, genetic modification, and immobilization techniques.

Xanthine dehydrogenase (XDH) is an enzyme involved in the metabolism of purines, which are nitrogen-containing compounds that form part of DNA and RNA. Specifically, XDH helps to break down xanthine and hypoxanthine into uric acid, a waste product that is excreted in the urine.

XDH can exist in two interconvertible forms: a dehydrogenase form (XDH) and an oxidase form (XO). In its dehydrogenase form, XDH uses NAD+ as an electron acceptor to convert xanthine into uric acid. However, when XDH is converted to its oxidase form (XO), it can use molecular oxygen as an electron acceptor instead, producing superoxide and hydrogen peroxide as byproducts. These reactive oxygen species can contribute to oxidative stress and tissue damage in the body.

Abnormal levels or activity of XDH have been implicated in various diseases, including gout, cardiovascular disease, and neurodegenerative disorders.

... cytochrome-c oxidase deficiency MeSH C16.320.565.390 - glucosephosphate dehydrogenase deficiency MeSH C16.320.565.437 - ... glucosephosphate dehydrogenase deficiency MeSH C16.320.070.480.370 - favism MeSH C16.320.070.490 - hemoglobin c disease MeSH ... pyruvate carboxylase deficiency disease MeSH C16.320.565.202.810.766 - pyruvate dehydrogenase complex deficiency disease MeSH ... pyruvate carboxylase deficiency disease MeSH C16.320.565.150.750 - pyruvate dehydrogenase complex deficiency disease MeSH ...
... glucosephosphate dehydrogenase deficiency MeSH C15.378.071.141.150.480.370 - favism MeSH C15.378.071.141.150.490 - hemoglobin c ... factor v deficiency MeSH C15.378.100.141.310 - factor vii deficiency MeSH C15.378.100.141.320 - factor x deficiency MeSH ... factor v deficiency MeSH C15.378.100.425.310 - factor vii deficiency MeSH C15.378.100.425.320 - factor x deficiency MeSH ... factor v deficiency MeSH C15.378.463.310 - factor vii deficiency MeSH C15.378.463.320 - factor x deficiency MeSH C15.378. ...
... cytochrome-c oxidase deficiency MeSH C18.452.648.390 - glucosephosphate dehydrogenase deficiency MeSH C18.452.648.437 - ... pyruvate carboxylase deficiency disease MeSH C18.452.648.202.810.766 - pyruvate dehydrogenase complex deficiency disease MeSH ... pyruvate carboxylase deficiency disease MeSH C18.452.660.710 - pyruvate dehydrogenase complex deficiency disease MeSH C18.452. ... pyruvate carboxylase deficiency disease MeSH C18.452.100.100.750 - pyruvate dehydrogenase complex deficiency disease MeSH ...
... glucose-6-phosphate dehydrogenase (G6PD) deficiency, congenital adrenal hyperplasia, methyl coenzyme dehydrogenase deficiency ... A study about sickle cell anemia in Arabs article about Birth defects Glucose phosphate isomerase deficiency responsible for ... Shalev O, Leibowitz G, Brok-Simoni F (June 1994). "[Glucose phosphate isomerase deficiency with congenital nonspherocytic ... Rosler A (August 2006). "17 beta-hydroxysteroid dehydrogenase 3 deficiency in the Mediterranean population". Pediatric ...
... phosphate dehydrogenase deficiency Glucose-6-phosphate translocase deficiency Glucose-galactose malabsorption Glucosephosphate ... II Glutaryl-CoA dehydrogenase deficiency Glutathione synthetase deficiency Glyceraldehyde-3-phosphate dehydrogenase deficiency ... isomerase deficiency Glucosidase acid-1,4-alpha deficiency Glut2 deficiency Glutamate decarboxylase deficiency Glutamate- ... constitutional Growth hormone deficiency Growth mental deficiency syndrome of Myhre Growth retardation alopecia pseudoanodontia ...
PC Pyruvate dehydrogenase deficiency; 312170; PDHA1 Pyruvate dehydrogenase E2 deficiency; 245348; DLAT Pyruvate dehydrogenase ... due to glucose phosphate isomerase deficiency; 613470; GPI Hemolytic uremic syndrome, atypical, susceptibility to, 1; 235400; ... SCARB2 Acyl-CoA dehydrogenase, long chain, deficiency of; 201460; ACADL Acyl-CoA dehydrogenase, medium chain, deficiency of; ... DCX Succinic semialdehyde dehydrogenase deficiency; 271980; ALDH5A1 Succinyl-CoA:3-oxoacid CoA transferase deficiency; 245050; ...
Cofactors: Mg2+ G6P is then rearranged into fructose 6-phosphate (F6P) by glucose phosphate isomerase. Fructose can also enter ... Glyceraldehyde-3-phosphate dehydrogenase NAD++ Pi NADH + H+ NAD++ Pi NADH + H+ 2 × 1,3-Bisphosphoglycerate 2 × Phosphoglycerate ... are seen with one notable example being pyruvate kinase deficiency, leading to chronic hemolytic anemia.[citation needed] ...
Results of search for su:{Glucosephosphate dehydrogenase deficiency.} Refine your search. *. Availability. * Limit to ... Reappraisal of G-6-PD deficiency and Falciparum malaria / by Dwip Kitayaporn. by Kitayaporn, Dwip , UNDP/World Bank/WHO Special ... by WHO Scientific Group on the Standardization of Procedures for the Study of Glucose-6-Phosphate Dehydrogenase , World Health ... by WHO Scientific Group on the Standardization of Procedures for the Study of Glucose-6-Phosphate Dehydrogenase , World Health ...
... deficiency and poorly controlled non-insulin-dependent diabetes mellitus, an episode of acute haemolysis occurred after the ... In a 61-year-old man with glucose-6-phosphate dehydrogenase (G6PD) ... Glucosephosphate Dehydrogenase Deficiency / complications* * Glyburide / adverse effects* * Humans * Hypoglycemic Agents / ... In a 61-year-old man with glucose-6-phosphate dehydrogenase (G6PD) deficiency and poorly controlled non-insulin-dependent ...
... cytochrome-c oxidase deficiency MeSH C16.320.565.390 - glucosephosphate dehydrogenase deficiency MeSH C16.320.565.437 - ... glucosephosphate dehydrogenase deficiency MeSH C16.320.070.480.370 - favism MeSH C16.320.070.490 - hemoglobin c disease MeSH ... pyruvate carboxylase deficiency disease MeSH C16.320.565.202.810.766 - pyruvate dehydrogenase complex deficiency disease MeSH ... pyruvate carboxylase deficiency disease MeSH C16.320.565.150.750 - pyruvate dehydrogenase complex deficiency disease MeSH ...
... hemolytic anemia in people who have glucose phosphate dehydrogenase deficiency (G6PD), and thrombocytopenia (very low platelets ...
keywords = "Adverse-drug-reactions, Dapsone, adverse reactions, Genetic-polymorphism, Glucosephosphate-dehydrogenase-deficiency ... Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common human enzyme defect and one of the most common genetic ... Medications and glucose-6-phosphate dehydrogenase deficiency: An evidence-based review. Ilan Youngster*, Lidia Arcavi, Renata ... Medications and glucose-6-phosphate dehydrogenase deficiency: An evidence-based review. Drug Safety. 2010;33(9):713-726. doi: ...
Glucosephosphate Dehydrogenase Deficiency 1 0 Goiter, Nodular 1 0 Glaucoma, Angle-Closure 1 0 ...
Glucose-6-phosphate dehydrogenase deficiency contributes to metabolic abnormality and pulmonary hypertension. Varghese, M. V., ... Glyceraldehyde-3-phosphate dehydrogenase binds to the AU-rich 3′ untranslated region of colony-stimulating factor-1 (CSF-1) ... Glucosephosphate Dehydrogenase Deficiency 100% * Pulmonary Hypertension 71% * Oxidative Stress 53% * Pentose Phosphate Pathway ...
Glucosephosphate Dehydrogenase Deficiency 28% * Glycogen Synthase Kinase 3 34% * Hemangiosarcoma 25% * Hemophagocytic ...
Glucose-6-phosphate dehydrogenase deficiency contributes to metabolic abnormality and pulmonary hypertension. Varghese, M. V., ... Glucosephosphate Dehydrogenase Deficiency 100% * Pulmonary Hypertension 71% * Oxidative Stress 53% * Pentose Phosphate Pathway ...
Glucose-6-phosphate Dehydrogenase Deficiency (51). *Glucose-galactose Malabsorption (13). *Glucosephosphate Dehydrogenase ...
Deficiency Diseases Medicine & Life Sciences 95% * Glucosephosphate Dehydrogenase Deficiency Medicine & Life Sciences 95% ... Glucose-6-phosphate dehydrogenase deficiency and haemolytic disease of the newborn in Israel. In: Archives of Disease in ... Glucose-6-phosphate dehydrogenase deficiency and haemolytic disease of the newborn in Israel. / Szeinberg, Arieh; Oliver, Moshe ... Szeinberg A, Oliver M, Schmidt R, Adam A, Sheba C. Glucose-6-phosphate dehydrogenase deficiency and haemolytic disease of the ...
Patients must be tested for glucosephosphate dehydrogenase deficiency. Intraclass correlation coefficients ICCs were used to ... Chrome deficiency is common in non-diabetic dependent diabetics, contributing to increased cholesterol and cholesterol. For ...
Glucosephosphate dehydrogenase deficiency, vitamin K, and ambiguity in medical textbooks. Map of Borrowash, Derbyshire, England ...
Hemolysis after acetaminophen overdose in a patient with glucosephosphate dehydrogenase deficiency. It is an i ndex relate d to ...
Some patients with glucose--phosphate dehydrogenase deficiency in red cells and are transported to the aptt in some patients, ... Affecting of hospitalized patients will admit to intensive care nurses, vitamin k deficiency is confirmed when all causes of ... agonist such as congenital deficiency of the portal blood flow is the preferred method of system calibration is to block ...
Haemolytic potential of three chemotherapeutic agents and aspirin in glucosephosphate dehydrogenase deficiency. Evergreen ...
Glucosephosphate Dehydrogenase. *Glucosephosphate Dehydrogenase Deficiency. *Polymers. *Semiconductors. *Synaptic Vesicles. * ...
Acute hemolytic anemia induced elitepvpers a pyrazolonic drug in a child with glucosephosphate dehydrogenase deficiency. Are ...
One male participant (1/174) had severe G6PD deficiency (,10% activity), five participants (5/174) had mild G6PD deficiency (10 ... The prevalence of G6PD deficiency was low. Main contribution to haemolysis in G6PD normal individuals was attributable to acute ... Adolescent, Adult, Aged, Antimalarials, Bangladesh, Child, Child, Preschool, Female, Glucosephosphate Dehydrogenase Deficiency ... One male participant (1/174) had severe G6PD deficiency (,10% activity), five participants (5/174) had mild G6PD deficiency (10 ...
Hemolytic anemia - hemolysis appears to be linked to a glucosephosphate dehydrogenase deficiency in the red blood cells of the ... glucose-6-phosphate dehydrogenase (G6PD) deficiency, vitamin B deficiency, any type of debilitating disease. This medication ... Do not take nitrofurantoin while breastfeeding if your baby has a rare condition called glucosephosphate dehydrogenase G6PD ... glucose-6-phosphate dehydrogenase deficiency, acute porphyria, pregnancy, in children under 12 years of age. Breastfeeding ...
glucosephosphate dehydrogenase deficiency. *favism. Entry Terms: *EC 1.1.1.49. *glucose 6-phosphate dehydrogenase (NADP) ...
... deficiency is a genetic disorder that is most common in males. Learn about symptoms, diagnosis and treatment. ... ClinicalTrials.gov: Glucosephosphate Dehydrogenase Deficiency (National Institutes of Health) Journal Articles References and ... G6PD Deficiency (Glucose-6-Phosphate Dehydrogenase) (For Parents) (Nemours Foundation) * G6PD Test (National Library of ... Glucose-6-phosphate dehydrogenase (G6PD) deficiency is a genetic disorder that is most common in males. About 1 in 10 African ...
Glucosephosphate Dehydrogenase Deficiency [C16.320.565.202.402] * Glycogen Storage Disease [C16.320.565.202.449] ... Pyruvate Carboxylase Deficiency Disease [C16.320.565.202.810.666] * Pyruvate Dehydrogenase Complex Deficiency Disease [C16.320. ... Pyruvate Carboxylase Deficiency Disease [C18.452.648.202.810.666] * Pyruvate Dehydrogenase Complex Deficiency Disease [C18.452. ... Multiple Carboxylase Deficiency [C16.320.565.202.720] * Pyruvate Metabolism, Inborn Errors [C16.320.565.202.810] * Leigh ...
Glucosephosphate Dehydrogenase Deficiency [C15.378.071.141.150.480] Glucosephosphate Dehydrogenase Deficiency * Hemoglobin C ...
Glucosephosphate Dehydrogenase Deficiency. *Glycogen Storage Disease. *Hyperoxaluria, Primary. *Lactose Intolerance. * ... "Mannosidase Deficiency Diseases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... This graph shows the total number of publications written about "Mannosidase Deficiency Diseases" by people in this website by ... Below are the most recent publications written about "Mannosidase Deficiency Diseases" by people in Profiles. ...
Glucosephosphate Dehydrogenase Deficiency. *Glycogen Storage Disease. *Hyperoxaluria, Primary. *Lactose Intolerance. * ... 6-diphosphatase deficiency. Essential fructosuria is a benign asymptomatic metabolic disorder caused by deficiency in ... hepatic fructokinase deficiency (essential fructosuria), hereditary fructose intolerance, and hereditary fructose-1, ...
Case Reports , Child , Glucosephosphate Dehydrogenase Deficiency , Hemoglobinuria , Malaria , Niger See more details. ... This study showed a deficiency in the control of critical control points that impacts the performance of the AST reported by ...
  • In a 61-year-old man with glucose-6-phosphate dehydrogenase (G6PD) deficiency and poorly controlled non-insulin-dependent diabetes mellitus, an episode of acute haemolysis occurred after the administration of glyburide (glibenclamide). (nih.gov)
  • Since autoimmune haemolysis was excluded on the basis of laboratory data, acute haemolysis was ascribed to G6PD deficiency. (nih.gov)
  • Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common human enzyme defect and one of the most common genetic disorders worldwide, with an estimated 400 million people worldwide carrying a mutation in the G6PD gene that causes deficiency of the enzyme. (tau.ac.il)
  • Although drug-induced haemolysis is considered the most common adverse clinical consequence of G6PD deficiency, significant confusion exists regarding which drugs can cause haemolytic anaemia in patients with G6PD deficiency. (tau.ac.il)
  • In the current review we aimed, by thorough search of the medical literature, to collect evidence on which to base decisions either to prohibit or allow the use of various medications in patients with G6PD deficiency. (tau.ac.il)
  • A literature search was conducted during May 2009 for studies and case reports on medication use and G6PD deficiency using the following sources: MEDLINE (1966May 2009), PubMed (1950May 2009), the Cochrane database of systematic reviews (2009), and major pharmacology, internal medicine, haematology and paediatric textbooks. (tau.ac.il)
  • Others were asymptomatic but belonged to a family with a history of G6PD deficiency. (hal.science)
  • The molecular analysis was performed by a combination of PCR-RFLP and DNA sequencing to characterize the mutations causing G6PD deficiency. (hal.science)
  • G6PD Deficiency and Antimalarial Efficacy for Uncomplicated Malaria in Bangladesh: A Prospective Observational Study. (ox.ac.uk)
  • 10% activity), five participants (5/174) had mild G6PD deficiency (10-60% activity). (ox.ac.uk)
  • The prevalence of G6PD deficiency was low. (ox.ac.uk)
  • Glucose-6-phosphate dehydrogenase (G6PD) deficiency is a genetic disorder that is most common in males. (medlineplus.gov)
  • G6PD deficiency mainly affects red blood cells , which carry oxygen from the lungs to tissues throughout the body. (medlineplus.gov)
  • If you have G6PD deficiency, you may not have symptoms. (medlineplus.gov)
  • Glucose-6-phosphate dehydrogenase deficiency is an erythrocyte enzyme disorder caused by mutations in the G6PD gene , which has an X-linked inheritance . (bvsalud.org)
  • Here we analyze the clinical and laboratory characteristics of 24 subjects with G6PD deficiency over 25 years. (bvsalud.org)
  • La deficiencia de glucosa-6-fosfato deshidrogenasa es la enzimopatía eritrocitaria causada por mutaciones en el gen G6PD , cuya herencia está ligada al cromosoma X . Se analizan las características clínicas y de laboratorio de 24 individuos con deficiencia de G6PD durante 25 años. (bvsalud.org)
  • Drug-induced acute hemolytic anemia led to the discovery of G6PD deficiency. (ashpublications.org)
  • 2.5 mg/kg once daily for 3 days), 95 G6PD-deficient hemizygous boys, 24 G6PD-deficient homozygous girls, and 200 girls heterozygous for G6PD deficiency received this agent. (ashpublications.org)
  • Therefore, contrary to current perception, in clinical terms the A− type of G6PD deficiency cannot be regarded as mild. (ashpublications.org)
  • Glucose 6-phosphate dehydrogenase (G6PD) deficiency is common in populations that have been exposed to malaria, either in the present or in the past. (ashpublications.org)
  • Estimation of risk of glucose 6-phosphate dehydrogenase deficient red cells to ozone and nitrogen dioxide : investigator's final report / by Marie A. Amoruso. (who.int)
  • The importance of glucose-6-phosphate dehydrogenase deficiency in the causation of severe neonatal jaundice in Israel was investigated. (openu.ac.il)
  • The overall results suggest that although a few such cases may occur in this country, glucose-6- phosphate dehydrogenase deficiency cannot be considered an important aetiological factor in the causation of severe haemolytic neonatal jaundice in Israel, in spite of the existence of population groups with a very high frequency of the enzyme deficiency. (openu.ac.il)
  • Some patients with glucose--phosphate dehydrogenase deficiency in red cells and are transported to the aptt in some patients, some improvement may occur with a propensity to cause harm to patients who received radiation therapy with antiviral agents. (elastizell.com)
  • Title : Glucose-6-Phosphate Dehydrogenase Deficiency In Project Head Start Children Personal Author(s) : Kelly, S.;Almy, R. (cdc.gov)
  • Phenotypic and genotypic characterization of glucose-6-phosphate dehydrogenase deficiency in Argentina. (bvsalud.org)
  • Communities with very high frequencies of enzyme deficiency and those in which it was very rare did not differ significantly in the frequency of severe neonatal jaundice not due to iso-immunization. (openu.ac.il)
  • However, in one investigated sample of Iraqi Jews the number of enzyme-deficient cases among the jaundiced infants was significantly higher than expected from the gene frequency, suggesting that some cases of haemolytic disease of newborn due to enzyme deficiency did occur in this group. (openu.ac.il)
  • A number of ventilator-free and shock-free days during the day.Thus diurnal enuresis is most often as needed saba, inhaled short-acting - agonist such as congenital deficiency of the portal blood flow is the preferred method of system calibration is to block cytokine-mediated inflam-mation. (elastizell.com)
  • Mannosidase Deficiency Diseases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ouhsc.edu)
  • It is available as a prescription only medicine and is commonly used for GTP-CH Deficiency, Neuroleptic Malignant Syndrome, Parkinson's Disease, Restless Legs Syndrome. (art-pasion.es)
  • Disorders in pyruvate metabolism appear to lead to deficiencies in neurotransmitter synthesis and, consequently, to nervous system disorders. (nih.gov)
  • Hemolysis and anemia persist after splenectomy, although some improvement may occur, particularly in patients with pyruvate kinase deficiency. (msdmanuals.com)
  • This graph shows the total number of publications written about "Mannosidase Deficiency Diseases" by people in this website by year, and whether "Mannosidase Deficiency Diseases" was a major or minor topic of these publications. (ouhsc.edu)
  • Below are the most recent publications written about "Mannosidase Deficiency Diseases" by people in Profiles. (ouhsc.edu)
  • Results of search for 'su:{Glucosephosphate dehydrogenase deficiency. (who.int)
  • Chrome deficiency is common in non-diabetic dependent diabetics, contributing to increased cholesterol and cholesterol. (alliedmortgage.ca)
  • Inherited abnormalities of fructose metabolism, which include three known autosomal recessive types: hepatic fructokinase deficiency (essential fructosuria), hereditary fructose intolerance, and hereditary fructose-1,6-diphosphatase deficiency. (sdsu.edu)
  • Overexpression of Dwarf promoted net photosynthetic rate ( P N ), whereas BR deficiency in d im led to a significant inhibition in P N as compared with WT. (biomedcentral.com)
  • A single patient with mutation (Asn126Asp) showed a 21% decrease in G6PD activity, two subjects showed G6PD deficiency without mutations, and one patient had a decreased level of G6PD mRNA and reduced enzyme levels. (nih.gov)
  • Estimation of risk of glucose 6-phosphate dehydrogenase deficient red cells to ozone and nitrogen dioxide : investigator's final report / by Marie A. Amoruso. (who.int)
  • 10. The relationship between the enzyme activity, lipid peroxidation and red blood cells deformability in hemizygous and heterozygous glucose-6-phosphate dehydrogenase deficient individuals. (nih.gov)
  • Glucosephosphate isomerase (GPI) deficiency in humans is an autosomal recessive disorder, which results in nonspherocytic hemolytic anemia of variable clinical expression. (nih.gov)
  • Glucose phosphate isomerase (GPI) deficiency is an inherited disorder that affects red blood cells, which carry oxygen to the body's tissues. (nih.gov)
  • Mohrenweiser and Neel identified thermolabile variants of lactate dehydrogenase B, can toothpaste affect blood sugar glucosephosphate isomerase, and glucose 6 phosphate dehydrogenase. (gsac.ge)
  • A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia. (nih.gov)
  • A 4-year-old female with severe congenital hemolytic anemia had low red cell GPI activity of 15.5 IU/g Hb (50% of normal mean) indicating GPI deficiency. (nih.gov)
  • 11. Molecular Analysis of Glucose-6-Phosphate Dehydrogenase Gene Mutations in Bangladeshi Individuals. (nih.gov)
  • Hemolysis and anemia persist after splenectomy, although some improvement may occur, particularly in patients with pyruvate kinase deficiency. (msdmanuals.com)
  • We assessed the prevalence of three common hereditary blood disorders [‎sickle-cell and beta-thalassaemia traits and glucose 6-phosphate dehydrogenase deficiency]‎ among the Omani population. (who.int)
  • About 27% of Omani males had inherited glucose-6-phosphate dehydrogenase deficiency [‎compared with 11% of females]‎ while countrywide prevalence rates for the sickle-cell and beta-thalassaemia traits were estimated to be 5.8% and 2.2% respectively and showed no significant gender differences. (who.int)
  • Deficiencia enzimática que produce una enfermedad con muchas variantes, algunas de las cuales causa déficit de la actividad enzimática en los eritrocitos, que genera una anemia hemolítica. (bvsalud.org)
  • 19. [Clinical evaluation of a melting curve analysis-based PCR assay for glucose phosphate dehydrogenase gene mutation detection]. (nih.gov)
  • While the biochemical defect has been quantified, the genetic basis of the deficiency is unknown. (nih.gov)
  • Under nitrogen deficiency situation, Nannochloropsis spp. (biomedcentral.com)
  • Mechanisms of this process from the perspective of transcriptome and metabolome have been obtained previously, yet proteome analysis is still sparse which hinders the analysis of dynamic adaption to nitrogen deficiency. (biomedcentral.com)
  • PMID- 5097531 TI - Subunit interaction of a temperature-sensitive alcohol dehydrogenase mutant in maize. (nih.gov)