Coenzymes
Transferases
Glutathione Transferase
Alkyl and Aryl Transferases
Coenzyme A-Transferases
Ubiquinone
Acetyl Coenzyme A
Transferases (Other Substituted Phosphate Groups)
DNA Nucleotidylexotransferase
Hydroxymethylglutaryl CoA Reductases
Molecular Sequence Data
Mesna
Acyltransferases
Substrate Specificity
NAD
Peptidyl Transferases
Amino Acid Sequence
N-Acetylglucosaminyltransferases
Pantothenic Acid
ADP Ribose Transferases
Farnesyltranstransferase
Escherichia coli
Liver
Pantetheine
Base Sequence
Euryarchaeota
Catalysis
Propanediol Dehydratase
Binding Sites
Protein Prenylation
Cloning, Molecular
Dinitrochlorobenzene
NADP
Hydroxymethylglutaryl-CoA Reductase Inhibitors
Methanosarcina barkeri
Galactosyltransferases
N-Acetylgalactosaminyltransferases
Palmitoyl Coenzyme A
Alcohol Oxidoreductases
Lovastatin
Acetate-CoA Ligase
Riboflavin
Methyltransferases
Isoenzymes
Malonyl Coenzyme A
Sequence Homology, Amino Acid
Oxidoreductases
gamma-Glutamyltransferase
Mutation
Methanobacterium
Glycosyltransferases
Oxidation-Reduction
Acetyltransferases
DNA Nucleotidyltransferases
Models, Molecular
Pentosyltransferases
Protein Binding
Hydrogen-Ion Concentration
Acetates
Chromatography, High Pressure Liquid
UTP-Hexose-1-Phosphate Uridylyltransferase
Pyridoxal Phosphate
Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent
Methylmalonyl-CoA Mutase
Glutathione
Simvastatin
Methane
Microsomes, Liver
Electrophoresis, Polyacrylamide Gel
Vitamin B 12
Sequence Alignment
Mutagenesis, Site-Directed
Catalytic Domain
Acetyl-CoA C-Acetyltransferase
Glucuronosyltransferase
Sterol O-Acyltransferase
Protein Conformation
Glucosyltransferases
Phosphate Acetyltransferase
Structure-Activity Relationship
Genetic Complementation Test
Aspartate Aminotransferases
Flavin-Adenine Dinucleotide
Crystallography, X-Ray
Gene Expression Regulation, Enzymologic
Fatty Acids
Glutamate Dehydrogenase
RNA, Messenger
Alcohol Dehydrogenase
Carbohydrate Sequence
Intramolecular Transferases
Enzyme Stability
Glycosylation
UDPglucose-Hexose-1-Phosphate Uridylyltransferase
Molecular Structure
Clostridium
Cholesterol
Acyl Carrier Protein
Oxo-Acid-Lyases
Sparsomycin
Hydroxymethylglutaryl-CoA Synthase
Apoenzymes
Saccharomyces cerevisiae
Hypoxanthine Phosphoribosyltransferase
Spectrophotometry, Ultraviolet
Mannosyltransferases
Enzyme Inhibitors
Phosphotransferases
Ethanolamine Ammonia-Lyase
Protein Structure, Tertiary
Mitochondria
Carboxy-Lyases
Ethanolaminephosphotransferase
Cytosol
Chromatography, Gel
DNA Primers
Methanosarcina
Adipates
Acetyl-CoA C-Acyltransferase
Carboxyl and Carbamoyl Transferases
Isomerases
Dimethylallyltranstransferase
Models, Chemical
Microsomes
Succinates
Plasmids
Succinate-CoA Ligases
Uridine Diphosphate N-Acetylglucosamine
Rats, Inbred Strains
Coumaric Acids
Amino Acids
Uridine Diphosphate N-Acetylgalactosamine
Multienzyme Complexes
Enzyme Induction
Biocatalysis
Crotonates
Enzyme Activation
Propylene Glycol
Cells, Cultured
Chromatography, Ion Exchange
Transcription, Genetic
Xanthobacter
Cattle
Multigene Family
Ribosomes
In Situ Nick-End Labeling
Temperature
Galactosemias
Propionates
Acetyl-CoA Carboxylase
Chloroflexus
Adenosine Triphosphate
Spectrophotometry
Methanobacteriaceae
Gene Expression Regulation, Bacterial
Fatty Acid Synthases
Flavin Mononucleotide
Transaminases
DNA
Apoptosis
Hydroxymethyl and Formyl Transferases
Stereoisomerism
NADH, NADPH Oxidoreductases
Sterols
Cricetinae
Hydro-Lyases
Peptide Synthases
Sequence Analysis, DNA
Chromatography, Affinity
Protein Processing, Post-Translational
Species Specificity
A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1. (1/146)
The bacterium Sphingomonas sp. strain RW1 is able to use dibenzo-p-dioxin, dibenzofuran, and several hydroxylated derivatives as sole sources of carbon and energy. We have determined and analyzed the nucleic acid sequence of a 9,997-bp HindIII fragment downstream of cistrons dxnA1A2, which encode the dioxygenase component of the initial dioxygenase system of the corresponding catabolic pathways. This fragment contains 10 colinear open reading frames (ORFs), apparently organized in one compact operon. The enzymatic activities of some proteins encoded by these genes were analyzed in the strain RW1 and, after hyperexpression, in Escherichia coli. The first three ORFs of the locus, designated dxnC, ORF2, and fdx3, specify a protein with a low homology to bacterial siderophore receptors, a polypeptide representing no significant homology to known proteins, and a putative ferredoxin, respectively. dxnD encodes a 69-kDa phenol monooxygenase-like protein with activity for the turnover of 4-hydroxysalicylate, and dxnE codes for a 37-kDa protein whose sequence and activity are similar to those of known maleylacetate reductases. The following gene, dxnF, encodes a 33-kDa intradiol dioxygenase which efficiently cleaves hydroxyquinol, yielding maleylacetate, the ketoform of 3-hydroxy-cis,cis-muconate. The heteromeric protein encoded by dxnGH is a 3-oxoadipate succinyl coenzyme A (succinyl-CoA) transferase, whereas dxnI specifies a protein exhibiting marked homology to acetyl-CoA acetyltransferases (thiolases). The last ORF of the sequenced fragment codes for a putative transposase. DxnD, DxnF, DxnE, DxnGH, and DxnI (the activities of most of them have also been detected in strain RW1) thus form a complete 4-hydroxysalicylate/hydroxyquinol degradative pathway. A route for the mineralization of the growth substrates 3-hydroxydibenzofuran and 2-hydroxydibenzo-p-dioxin in Sphingomonas sp. strain RW1 thus suggests itself. (+info)Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis. (2/146)
The exchange of oxygen atoms between acetate, glutaryl-CoA, and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans was analyzed using [(18)O(2)]acetate together with matrix-assisted laser desorption/ionization time of flight mass spectrometry of an appropriate undecapeptide. The exchange reaction was shown to be site-specific, reversible, and required both glutaryl-CoA and [(18)O(2)]acetate. The observed exchange is in agreement with the formation of a mixed anhydride intermediate between the enzyme and acetate. In contrast, with a mutant enzyme, which was converted to a thiol ester hydrolyase by replacement of the catalytic glutamate residue by aspartate, no (18)O uptake from H(2)(18)O into the carboxylate was detectable. This result is in accord with a mechanism in which the carboxylate of aspartate acts as a general base in activating a water molecule for hydrolysis of the thiol ester intermediate. This mechanism is further supported by the finding of a significant hydrolyase activity of the wild-type enzyme using acetyl-CoA as substrate, whereas glutaryl-CoA is not hydrolyzed. The small acetate molecule in the substrate binding pocket may activate a water molecule for hydrolysis of the nearby enzyme-CoA thiol ester. (+info)Regulation and adaptation of glucose metabolism of the parasitic protist Leishmania donovani at the enzyme and mRNA levels. (3/146)
Adaptation of the glucose metabolism of Leishmania donovani promastigotes (insect stage) was investigated by simultaneously measuring metabolic rates, enzyme activities, message levels, and cellular parameters under various conditions. Chemostats were used to adapt cells to different growth rates with growth rate-limiting or excess glucose concentrations. L. donovani catabolized glucose to CO(2), succinate, acetate, and pyruvate in ratios that depended on growth rate and glucose availability. Rates of glucose consumption were a linear function of growth rate and were twice as high in excess glucose-grown cells as in glucose-limited organisms. The major end product was CO(2), but organic end products were also formed in ratios that varied strongly with growth conditions. The specific activities of the 14 metabolic enzymes measured varied by factors of 3 to 17. Two groups of enzymes adapted specific activities in parallel, but there was no correlation between the groups. The activities of only one group correlated with specific rates of glucose metabolism. Total RNA content per cellular protein varied by a factor of 6 and showed a linear relationship with the rate of glucose consumption. There was no correlation between steady-state message levels and activities of the corresponding enzymes, suggesting regulation at the posttranscriptional level. A comparison of the adaptation of energy metabolism in L. donovani and other species suggests that the energy metabolism of L. donovani is inefficient but is well suited to the environmental challenges that it encounters during residence in the sandfly, its insect vector. (+info)Protection of mice against brucellosis by vaccination with Brucella melitensis WR201(16MDeltapurEK). (4/146)
Human brucellosis can be acquired from infected animal tissues by ingestion, inhalation, or contamination of the conjunctiva or traumatized skin by infected animal products. A vaccine to protect humans from occupational exposure or from zoonotic infection in areas where the disease is endemic would reduce an important cause of morbidity worldwide. Vaccines currently used in animals are unsuitable for human use. We tested a live, attenuated, purine-auxotrophic mutant strain of Brucella melitensis, WR201, for its ability to elicit cellular and humoral immune responses and to protect mice against intranasal challenge with B. melitensis 16M. Mice inoculated intraperitoneally with WR201 made serum antibody to lipopolysaccharide and non-O-polysaccharide antigens. Splenocytes from immunized animals released interleukin-2 (IL-2), gamma interferon, and IL-10 when cultured with Brucella antigens. Immunization led to protection from disseminated infection but had only a slight effect on clearance of the challenge inoculum from the lungs. These studies suggest that WR201 should be further investigated as a vaccine to prevent human brucellosis. (+info)Isolation and characterization of a haploid germ cell-specific novel complementary deoxyribonucleic acid; testis-specific homologue of succinyl CoA:3-Oxo acid CoA transferase. (5/146)
We have isolated a cDNA clone encoding a mouse haploid germ cell-specific protein from a subtracted cDNA library. Sequence analysis of the cDNA revealed high homology with pig and human heart succinyl CoA:3-oxo acid CoA transferase (EC 2.8.3.5), which is a key enzyme for energy metabolism of ketone bodies. The deduced protein consists of 520 amino acid residues, including glutamate 344, known to be the catalytic residue in the active site of pig heart CoA transferase and the expected mitochondrial targeting sequence enriched with Arg, Leu, and Ser in the N-terminal region. Thus, we termed this gene scot-t (testis-specific succinyl CoA:3-oxo acid CoA transferase). Northern blot analysis, in situ hybridization, and Western blot analysis demonstrated a unique expression pattern of the mRNA with rapid translation exclusively in late spermatids. The scot-t protein was detected first in elongated spermatids at step 8 or 9 as faint signals and gradually accumulated during spermiogenesis. It was also detected in the midpiece of spermatozoa by immunohistochemistry. The results suggest that the scot-t protein plays important roles in the energy metabolism of spermatozoa. (+info)Nitration of succinyl-CoA:3-oxoacid CoA-transferase in rats after endotoxin administration. (6/146)
The tyrosine nitration of proteins has been observed in diverse inflammatory conditions and has been linked to the presence of reactive nitrogen species. From many in vitro experiments, it is apparent that tyrosine nitration may alter the function of proteins. A limited number of experiments under in vivo conditions also demonstrate that protein nitration is associated with altered cellular processes. To understand the association of protein nitration with the pathogenic mechanism of the disease, it is essential to identify specific protein targets of nitration with in vivo or intact tissue models. Using anti-nitrotyrosine antibodies, we demonstrated the accumulation of nitrotyrosine in a 52-kDa protein in rat kidney after lipopolysaccharide treatment. The 52-kDa protein was purified and identified with partial sequence as succinyl-CoA:3-oxoacid CoA-transferase (SCOT; EC ). Western blot analysis revealed that the nitration of this mitochondrial enzyme increased in the kidneys and hearts of lipopolysaccharide-treated rats, whereas its catalytic activity decreased. These data suggest that tyrosine nitration may be a mechanism for the inhibition of SCOT activity in inflammatory conditions. SCOT is a key enzyme for ketone body utilization. Thus, tyrosine nitration of the enzyme with sepsis or inflammation may explain the altered metabolism of ketone bodies present in these disorders. (+info)Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: an enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria. (7/146)
Anaerobic microbial toluene catabolism is initiated by addition of fumarate to the methyl group of toluene, yielding (R)-benzylsuccinate as first intermediate, which is further metabolized via beta-oxidation to benzoyl-coenzyme A (CoA) and succinyl-CoA. A specific succinyl-CoA:(R)-benzylsuccinate CoA-transferase activating (R)-benzylsuccinate to the CoA-thioester was purified and characterized from Thauera aromatica. The enzyme is fully reversible and forms exclusively the 2-(R)-benzylsuccinyl-CoA isomer. Only some close chemical analogs of the substrates are accepted by the enzyme: succinate was partially replaced by maleate or methylsuccinate, and (R)-benzylsuccinate was replaced by methylsuccinate, benzylmalonate, or phenylsuccinate. In contrast to all other known CoA-transferases, the enzyme consists of two subunits of similar amino acid sequences and similar sizes (44 and 45 kDa) in an alpha(2)beta(2) conformation. Identity of the subunits with the products of the previously identified toluene-induced bbsEF genes was confirmed by determination of the exact masses via electrospray-mass spectrometry. The deduced amino acid sequences resemble those of only two other characterized CoA-transferases, oxalyl-CoA:formate CoA-transferase and (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase, which represent a new family of CoA-transferases. As suggested by kinetic analysis, the reaction mechanism of enzymes of this family apparently involves formation of a ternary complex between the enzyme and the two substrates. (+info)Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA-transferase. (8/146)
High levels of reactive species of nitrogen and oxygen in diabetes may cause modifications of proteins. Recently, an increase in protein tyrosine nitration was found in several diabetic tissues. To understand whether protein tyrosine nitration is the cause or the result of the associated diabetic complications, it is essential to identify specific proteins vulnerable to nitration with in vivo models of diabetes. In the present study, we have demonstrated that succinyl-CoA:3-oxoacid CoA-transferase (SCOT; EC 2.8.3.5) is susceptible to tyrosine nitration in hearts from streptozotocin-treated rats. After 4 and 8 wk of streptozotocin administration and diabetes progression, SCOT from rat hearts had a 24% and 39% decrease in catalytic activity, respectively. The decrease in SCOT catalytic activity is accompanied by an accumulation of nitrotyrosine in SCOT protein. SCOT is a mitochondrial matrix protein responsible for ketone body utilization. Ketone bodies provide an alternative source of energy during periods of glucose deficiency. Because diabetes results in profound derangements in myocardial substrate utilization, we suggest that SCOT tyrosine nitration is a contributing factor to this impairment in the diabetic heart. (+info)There are two main types of galactosemia:
1. Classical galactosemia: This is the most severe form of the disorder, and it is characterized by a complete lack of the enzyme galactose-1-phosphate uridylyltransferase (GALT). Without GALT, galactose builds up in the blood and tissues, leading to serious health problems.
2. Dialectical galactosemia: This form of the disorder is less severe than classical galactosemia, and it is characterized by a partial deficiency of GALT. People with dialectical galactosemia may experience some symptoms, but they are typically milder than those experienced by people with classical galactosemia.
Symptoms of galactosemia can include:
* Diarrhea
* Vomiting
* Jaundice (yellowing of the skin and eyes)
* Fatigue
* Poor feeding in infants
* Developmental delays
If left untreated, galactosemia can lead to a range of complications, including:
* Liver disease
* Kidney disease
* Increased risk of infections
* Delayed growth and development
The diagnosis of galactosemia is typically made through a combination of physical examination, medical history, and laboratory tests. Treatment for the disorder typically involves a strict diet that limits or eliminates galactose-containing foods, such as milk and other dairy products. In some cases, medication may also be prescribed to help manage symptoms.
Overall, early diagnosis and treatment of galactosemia are important for preventing or minimizing the risk of complications associated with this condition.
Term: Lesch-Nyhan Syndrome
Definition: A rare X-linked recessive genetic disorder caused by mutations in the HPRT1 gene, resulting in an impaired ability to metabolize uric acid and leading to symptoms such as gout, kidney stones, and other complications.
Etymology: Named after the physicians who first described the condition, Lesch and Nyhan.
Incidence: Approximately 1 in 165,000 male births.
Prevalence: Estimated to affect approximately 1 in 23,000 males worldwide.
Causes: Mutations in the HPRT1 gene, which codes for the enzyme hypoxanthine-guanine phosphoribosyltransferase (HPRT). This enzyme is involved in the metabolism of uric acid.
Symptoms: Gout attacks, kidney stones, joint pain and swelling, urate nephropathy (kidney damage), and other complications.
Diagnosis: Diagnosed through a combination of clinical evaluation, laboratory tests such as blood and urine analysis, and genetic testing to identify HPRT1 gene mutations.
Treatment: Medications to reduce uric acid levels, such as allopurinol or rasburicase, and management of symptoms such as pain and inflammation with nonsteroidal anti-inflammatory drugs (NSAIDs) or colchicine.
Prognosis: The condition is usually diagnosed in childhood, and patients often have a normal life expectancy if properly managed. However, untreated or poorly managed hyperuricemia can lead to complications such as kidney damage and cardiovascular disease.
Inheritance pattern: Autosomal recessive inheritance pattern, meaning that the individual must inherit two copies of the mutated HPRT1 gene (one from each parent) in order to develop the condition.
Other names: Hyperuricemia, gout, Lesch-Nyhan syndrome.
The two main types of lymphoid leukemia are:
1. Acute Lymphoblastic Leukemia (ALL): This type of leukemia is most commonly seen in children, but it can also occur in adults. It is characterized by a rapid increase in the number of immature white blood cells in the blood and bone marrow.
2. Chronic Lymphocytic Leukemia (CLL): This type of leukemia usually affects older adults and is characterized by the gradual buildup of abnormal white blood cells in the blood, bone marrow, and lymph nodes.
Symptoms of lymphoid leukemia include fatigue, fever, night sweats, weight loss, and swollen lymph nodes. Treatment options for lymphoid leukemia can vary depending on the type of cancer and the severity of symptoms, but may include chemotherapy, radiation therapy, or bone marrow transplantation.
There are several methods for diagnosing myringosclerosis, including:
1. Otoscopy: an examination of the outer ear and eardrum using a specialized instrument called an otoscope.
2. Tympanometry: a test that measures the movement of the eardrum and the reflexes of the middle ear muscles.
3. Acoustic reflectometry: a test that uses sound waves to measure the stiffness of the eardrum.
4. Auditory brainstem response (ABR) testing: a test that measures the electrical activity of the hearing nerve in response to sound.
There is no cure for myringosclerosis, but there are several treatment options available, including:
1. Hearing aids: devices that amplify sound and can help improve hearing.
2. Cochlear implants: devices that bypass the damaged part of the ear and directly stimulate the auditory nerve.
3. Surgery: in some cases, surgery may be necessary to remove the affected portion of the eardrum.
4. Medications: certain medications, such as corticosteroids, may be prescribed to help reduce inflammation and improve hearing.
It is important to seek medical attention if you experience any symptoms of myringosclerosis, as early diagnosis and treatment can help improve outcomes.
PKAN typically presents in children during the first few years of life, and is characterized by progressive loss of motor skills, cognitive decline, and vision loss. Affected individuals may also experience seizures, difficulty with speech and communication, and changes in behavior. The disorder is often diagnosed based on a combination of clinical features, genetic testing, and imaging studies such as magnetic resonance imaging (MRI) or positron emission tomography (PET).
The underlying pathology of PKAN involves the accumulation of a toxic protein called aggregated pantothenate kinase, which disrupts normal cellular function and leads to progressive degeneration of brain cells. There is currently no cure for PKAN, and treatment is focused on managing symptoms and slowing disease progression. This may include medications to control seizures and muscle spasticity, physical therapy to maintain mobility and strength, and supportive care to address cognitive and behavioral changes.
PKAN is a rare disorder, and the prevalence is not well-defined. However, it is estimated to affect approximately 1 in 200,000 individuals worldwide. The progression of PKAN can be variable, with some individuals experiencing a rapid decline in cognitive and motor functions, while others may have a more gradual course.
In summary, pantothenate kinase-associated neurodegeneration (PKAN) is a rare genetic disorder that affects the brain and spinal cord, causing progressive loss of motor skills, cognitive decline, and vision loss. There is currently no cure for PKAN, and treatment is focused on managing symptoms and slowing disease progression.
Examples of experimental liver neoplasms include:
1. Hepatocellular carcinoma (HCC): This is the most common type of primary liver cancer and can be induced experimentally by injecting carcinogens such as diethylnitrosamine (DEN) or dimethylbenz(a)anthracene (DMBA) into the liver tissue of animals.
2. Cholangiocarcinoma: This type of cancer originates in the bile ducts within the liver and can be induced experimentally by injecting chemical carcinogens such as DEN or DMBA into the bile ducts of animals.
3. Hepatoblastoma: This is a rare type of liver cancer that primarily affects children and can be induced experimentally by administering chemotherapy drugs to newborn mice or rats.
4. Metastatic tumors: These are tumors that originate in other parts of the body and spread to the liver through the bloodstream or lymphatic system. Experimental models of metastatic tumors can be studied by injecting cancer cells into the liver tissue of animals.
The study of experimental liver neoplasms is important for understanding the underlying mechanisms of liver cancer development and progression, as well as identifying potential therapeutic targets for the treatment of this disease. Animal models can be used to test the efficacy of new drugs or therapies before they are tested in humans, which can help to accelerate the development of new treatments for liver cancer.
1) They share similarities with humans: Many animal species share similar biological and physiological characteristics with humans, making them useful for studying human diseases. For example, mice and rats are often used to study diseases such as diabetes, heart disease, and cancer because they have similar metabolic and cardiovascular systems to humans.
2) They can be genetically manipulated: Animal disease models can be genetically engineered to develop specific diseases or to model human genetic disorders. This allows researchers to study the progression of the disease and test potential treatments in a controlled environment.
3) They can be used to test drugs and therapies: Before new drugs or therapies are tested in humans, they are often first tested in animal models of disease. This allows researchers to assess the safety and efficacy of the treatment before moving on to human clinical trials.
4) They can provide insights into disease mechanisms: Studying disease models in animals can provide valuable insights into the underlying mechanisms of a particular disease. This information can then be used to develop new treatments or improve existing ones.
5) Reduces the need for human testing: Using animal disease models reduces the need for human testing, which can be time-consuming, expensive, and ethically challenging. However, it is important to note that animal models are not perfect substitutes for human subjects, and results obtained from animal studies may not always translate to humans.
6) They can be used to study infectious diseases: Animal disease models can be used to study infectious diseases such as HIV, TB, and malaria. These models allow researchers to understand how the disease is transmitted, how it progresses, and how it responds to treatment.
7) They can be used to study complex diseases: Animal disease models can be used to study complex diseases such as cancer, diabetes, and heart disease. These models allow researchers to understand the underlying mechanisms of the disease and test potential treatments.
8) They are cost-effective: Animal disease models are often less expensive than human clinical trials, making them a cost-effective way to conduct research.
9) They can be used to study drug delivery: Animal disease models can be used to study drug delivery and pharmacokinetics, which is important for developing new drugs and drug delivery systems.
10) They can be used to study aging: Animal disease models can be used to study the aging process and age-related diseases such as Alzheimer's and Parkinson's. This allows researchers to understand how aging contributes to disease and develop potential treatments.
Examples of inborn errors of metabolism include:
1. Phenylketonuria (PKU): A disorder that affects the body's ability to break down the amino acid phenylalanine, leading to a buildup of this substance in the blood and brain.
2. Hypothyroidism: A condition in which the thyroid gland does not produce enough thyroid hormones, leading to developmental delays, intellectual disability, and other health problems.
3. Maple syrup urine disease (MSUD): A disorder that affects the body's ability to break down certain amino acids, leading to a buildup of these substances in the blood and urine.
4. Glycogen storage diseases: A group of disorders that affect the body's ability to store and use glycogen, a form of carbohydrate energy.
5. Mucopolysaccharidoses (MPS): A group of disorders that affect the body's ability to produce and break down certain sugars, leading to a buildup of these substances in the body.
6. Citrullinemia: A disorder that affects the body's ability to break down the amino acid citrulline, leading to a buildup of this substance in the blood and urine.
7. Homocystinuria: A disorder that affects the body's ability to break down certain amino acids, leading to a buildup of these substances in the blood and urine.
8. Tyrosinemia: A disorder that affects the body's ability to break down the amino acid tyrosine, leading to a buildup of this substance in the blood and liver.
Inborn errors of metabolism can be diagnosed through a combination of physical examination, medical history, and laboratory tests such as blood and urine tests. Treatment for these disorders varies depending on the specific condition and may include dietary changes, medication, and other therapies. Early detection and treatment can help manage symptoms and prevent complications.
Diagnosis of monieziasis typically involves a combination of physical examination, medical history, and laboratory tests such as fecal examination or endoscopy. Treatment typically involves the use of anthelmintic medications to kill the parasites, and supportive care to manage symptoms such as pain and diarrhea. In severe cases, hospitalization may be necessary to monitor and treat complications.
Prevention of monieziasis primarily involves good hygiene practices such as washing hands before eating or preparing food, avoiding close contact with individuals who have the infection, and avoiding consumption of undercooked or raw meat. In areas where the parasite is common, regular deworming programs can also help to reduce the risk of infection.
The prognosis for monieziasis is generally good if treatment is prompt and effective. However, complications such as intestinal obstruction, perforation, or abscesses can occur if left untreated, and can be life-threatening. It is important to seek medical attention if symptoms persist or worsen over time.
Overall, monieziasis is a rare but potentially serious condition that requires prompt diagnosis and treatment to prevent complications and ensure a good outcome.
There are several types of inborn errors of amino acid metabolism, including:
1. Phenylketonuria (PKU): This is the most common inborn error of amino acid metabolism and is caused by a deficiency of the enzyme phenylalanine hydroxylase. This enzyme is needed to break down the amino acid phenylalanine, which is found in many protein-containing foods. If phenylalanine is not properly broken down, it can build up in the blood and brain and cause serious health problems.
2. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
3. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
4. Arginase deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid arginine. Arginine is important for the body's production of nitric oxide, a compound that helps to relax blood vessels and improve blood flow.
5. Citrullinemia: This is a rare genetic disorder that affects the breakdown of the amino acid citrulline. Citrulline is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
6. Tyrosinemia: This is a rare genetic disorder that affects the breakdown of the amino acid tyrosine. Tyrosine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
7. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
8. PKU (phenylketonuria): This is a rare genetic disorder that affects the breakdown of the amino acid phenylalanine. Phenylalanine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
9. Methionine adenosyltransferase (MAT) deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
10. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid homocysteine. Homocysteine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
It is important to note that these disorders are rare and affect a small percentage of the population. However, they can be serious and potentially life-threatening, so it is important to be aware of them and seek medical attention if symptoms persist or worsen over time.
A vitamin B6 deficiency happens when the body does not get enough of this essential nutrient. Vitamin B6 is needed for many bodily functions, such as making new blood cells, keeping the nervous system healthy, and helping to convert food into energy.
The symptoms of a vitamin B6 deficiency can range from mild to severe and may include:
1. Fatigue or weakness: A lack of vitamin B6 can cause tiredness, weakness, and a general feeling of being unwell.
2. Irritability or depression: Vitamin B6 plays a role in the production of neurotransmitters, such as serotonin and dopamine, which are important for mood regulation. A deficiency can lead to feelings of irritability, anxiety, and depression.
3. Nausea and vomiting: Vitamin B6 helps with the absorption of nutrients from food, so a deficiency can cause nausea and vomiting.
4. Skin problems: Vitamin B6 is important for the health of the skin, and a deficiency can lead to conditions such as acne, eczema, and dermatitis.
5. Weight loss: A vitamin B6 deficiency can make it harder to gain weight or maintain weight loss.
Causes of Vitamin B6 Deficiency:
1. Poor diet: A diet that is low in vitamin B6 can lead to a deficiency. Foods rich in vitamin B6 include meat, fish, poultry, whole grains, and leafy green vegetables.
2. Malabsorption: Certain medical conditions, such as celiac disease or inflammatory bowel disease, can make it harder for the body to absorb vitamin B6 from food.
3. Pregnancy and breastfeeding: Women who are pregnant or breastfeeding have a higher need for vitamin B6 and may be more likely to develop a deficiency if they do not consume enough of this nutrient.
4. Alcoholism: Heavy alcohol consumption can interfere with the absorption of vitamin B6, leading to a deficiency.
5. Certain medications: Some medications, such as antidepressants and anti-inflammatory drugs, can interfere with the absorption of vitamin B6.
Signs and Symptoms of Vitamin B6 Deficiency:
1. Depression or anxiety
2. Fatigue or weakness
3. Irritability or mood swings
4. Skin problems, such as acne or eczema
5. Nausea and vomiting
6. Weight loss or difficulty gaining weight
7. Difficulty walking or maintaining balance
8. Headaches or migraines
9. Muscle weakness or cramps
10. Seizures or convulsions (in severe cases)
Treatment of Vitamin B6 Deficiency:
1. Dietary changes: Increasing the intake of vitamin B6-rich foods, such as lean meats, whole grains, and vegetables, can help treat a deficiency.
2. Supplements: Taking a vitamin B6 supplement can help treat a deficiency. The recommended daily dose is 1.3-2.0 mg per day for adults.
3. Addressing underlying causes: If the deficiency is caused by an underlying medical condition, such as celiac disease or alcoholism, treating the condition can help resolve the deficiency.
4. Vitamin B complex supplements: Taking a vitamin B complex supplement that contains all eight B vitamins can help ensure that the body is getting enough of this essential nutrient.
In conclusion, vitamin B6 is an essential nutrient that plays a crucial role in many bodily functions. Deficiency in this vitamin can lead to a range of health problems, from mild discomforts like fatigue and nausea to more severe conditions like seizures and convulsions. Treatment of a deficiency typically involves dietary changes, supplements, and addressing any underlying medical conditions. It is important to seek medical advice if symptoms persist or worsen over time.
There are several types of hypercholesterolemia, including:
1. Familial hypercholesterolemia: This is an inherited condition that causes high levels of low-density lipoprotein (LDL) cholesterol, also known as "bad" cholesterol, in the blood.
2. Non-familial hypercholesterolemia: This type of hypercholesterolemia is not inherited and can be caused by a variety of factors, such as a high-fat diet, lack of exercise, obesity, and certain medical conditions, such as hypothyroidism or polycystic ovary syndrome (PCOS).
3. Mixed hypercholesterolemia: This type of hypercholesterolemia is characterized by high levels of both LDL and high-density lipoprotein (HDL) cholesterol in the blood.
The diagnosis of hypercholesterolemia is typically made based on a physical examination, medical history, and laboratory tests, such as a lipid profile, which measures the levels of different types of cholesterol and triglycerides in the blood. Treatment for hypercholesterolemia usually involves lifestyle changes, such as a healthy diet and regular exercise, and may also include medication, such as statins, to lower cholesterol levels.
Crigler-Najjar syndrome is a rare genetic disorder that affects the liver and causes it to be unable to break down bilirubin, a yellow pigment found in the blood. This results in a buildup of bilirubin in the blood and can lead to jaundice, which is characterized by a yellowish tint to the skin and whites of the eyes.
There are two types of Crigler-Najjar syndrome: type 1 and type 2. Type 1 is caused by a deficiency of the enzyme glucuronyltransferase, which is necessary for the breakdown of bilirubin. Type 2 is caused by a deficiency of the enzyme UDP-glucuronosyltransferase. Both types can be inherited from one's parents or can be acquired through mutations that occur spontaneously.
Symptoms of Crigler-Najjar syndrome include jaundice, yellowing of the skin and whites of the eyes, dark urine, itching all over the body, and a higher risk of liver disease. Treatment for Crigler-Najjar syndrome typically involves managing the symptoms and preventing complications. This may include phototherapy to help break down bilirubin, medications to reduce jaundice, and careful monitoring of the liver function. In severe cases, a liver transplant may be necessary.
Overall, Crigler-Najjar syndrome is a rare and potentially serious genetic disorder that affects the liver's ability to break down bilirubin. With proper management and care, individuals with this condition can lead relatively normal lives.
Body weight is an important health indicator, as it can affect an individual's risk for certain medical conditions, such as obesity, diabetes, and cardiovascular disease. Maintaining a healthy body weight is essential for overall health and well-being, and there are many ways to do so, including a balanced diet, regular exercise, and other lifestyle changes.
There are several ways to measure body weight, including:
1. Scale: This is the most common method of measuring body weight, and it involves standing on a scale that displays the individual's weight in kg or lb.
2. Body fat calipers: These are used to measure body fat percentage by pinching the skin at specific points on the body.
3. Skinfold measurements: This method involves measuring the thickness of the skin folds at specific points on the body to estimate body fat percentage.
4. Bioelectrical impedance analysis (BIA): This is a non-invasive method that uses electrical impulses to measure body fat percentage.
5. Dual-energy X-ray absorptiometry (DXA): This is a more accurate method of measuring body composition, including bone density and body fat percentage.
It's important to note that body weight can fluctuate throughout the day due to factors such as water retention, so it's best to measure body weight at the same time each day for the most accurate results. Additionally, it's important to use a reliable scale or measuring tool to ensure accurate measurements.
Mitochondrial encephalomyopathies can be classified into several types based on the specific symptoms and the location of the mutations in the mitochondrial DNA. Some of the most common forms of these disorders include:
1. MELAS syndrome (mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes): This is a rare condition that affects the brain, muscles, and other organs. It is characterized by recurrent stroke-like episodes, seizures, and muscle weakness.
2. Kearns-Sayre syndrome: This is a rare genetic disorder that affects the nervous system and the muscles. It is characterized by progressive weakness and paralysis of the muscles, as well as vision loss and cognitive impairment.
3. Chronic progressive external ophthalmoplegia (CPEO): This is a rare disorder that affects the muscles of the eyes and the extraocular system. It is characterized by progressive weakness of the eye muscles, which can lead to droopy eyelids, double vision, and other vision problems.
4. Mitochondrial DNA depletion syndrome: This is a group of disorders that are caused by a decrease in the amount of mitochondrial DNA. These disorders can affect various parts of the body, including the brain, muscles, and other organs. They can cause a wide range of symptoms, including muscle weakness, seizures, and vision loss.
5. Myoclonic dystonia: This is a rare genetic disorder that affects the muscles and the nervous system. It is characterized by muscle stiffness, spasms, and myoclonus (involuntary jerky movements).
6. Neuronal ceroid lipofuscinoses (NCL): These are a group of rare genetic disorders that affect the brain and the nervous system. They can cause progressive loss of cognitive and motor functions, as well as vision loss and seizures.
7. Spinocerebellar ataxia: This is a group of rare genetic disorders that affect the cerebellum and the spinal cord. They can cause progressive weakness, coordination problems, and other movement disorders.
8. Friedreich's ataxia: This is a rare genetic disorder that affects the nervous system and the muscles. It is characterized by progressive loss of coordination and balance, as well as muscle weakness and wasting.
9. Charcot-Marie-Tooth disease: This is a group of rare genetic disorders that affect the peripheral nerves. They can cause muscle weakness, numbness or tingling in the hands and feet, and other problems with movement and sensation.
10. Progressive supranuclear palsy: This is a rare genetic disorder that affects the brain and the nervous system. It is characterized by progressive loss of movement control, as well as dementia and behavioral changes.
It is important to note that this list is not exhaustive and there may be other rare movement disorders that are not included here. If you suspect that you or a loved one may have a rare movement disorder, it is important to consult with a healthcare professional for proper diagnosis and treatment.
Mitochondrial diseases can affect anyone, regardless of age or gender, and they can be caused by mutations in either the mitochondrial DNA (mtDNA) or the nuclear DNA (nDNA). These mutations can be inherited from one's parents or acquired during embryonic development.
Some of the most common symptoms of mitochondrial diseases include:
1. Muscle weakness and wasting
2. Seizures
3. Cognitive impairment
4. Vision loss
5. Hearing loss
6. Heart problems
7. Neurological disorders
8. Gastrointestinal issues
9. Liver and kidney dysfunction
Some examples of mitochondrial diseases include:
1. MELAS syndrome (Mitochondrial Myopathy, Encephalopathy, Lactic Acidosis, and Stroke-like episodes)
2. Kearns-Sayre syndrome (a rare progressive disorder that affects the nervous system and other organs)
3. Chronic progressive external ophthalmoplegia (CPEO), which is characterized by weakness of the extraocular muscles and vision loss
4. Mitochondrial DNA depletion syndrome, which can cause a wide range of symptoms including seizures, developmental delays, and muscle weakness.
5. Mitochondrial myopathy, encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS)
6. Leigh syndrome, which is a rare genetic disorder that affects the brain and spinal cord.
7. LHON (Leber's Hereditary Optic Neuropathy), which is a rare form of vision loss that can lead to blindness in one or both eyes.
8. Mitochondrial DNA mutation, which can cause a wide range of symptoms including seizures, developmental delays, and muscle weakness.
9. Mitochondrial myopathy, encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS)
10. Kearns-Sayre syndrome, which is a rare progressive disorder that affects the nervous system and other organs.
It's important to note that this is not an exhaustive list and there are many more mitochondrial diseases and disorders that can affect individuals. Additionally, while these diseases are rare, they can have a significant impact on the quality of life of those affected and their families.
Causes and risk factors:
1. Poor diet: A diet that is deficient in riboflavin can lead to a deficiency. Common culprits include a lack of dairy products, eggs, and leafy green vegetables.
2. Malabsorption: Certain medical conditions, such as celiac disease, Crohn's disease, and pancreatic insufficiency, can lead to malabsorption of riboflavin and other nutrients.
3. Alcoholism: Alcohol can interfere with the absorption of riboflavin and other B vitamins.
4. Pregnancy and lactation: Pregnant and breastfeeding women have a higher demand for riboflavin, and may be at risk for deficiency if their diet does not provide enough.
5. Genetic disorders: Certain genetic disorders, such as fibroblastosis, can lead to riboflavin deficiency.
Symptoms of riboflavin deficiency can include:
1. Cracks in the corners of the mouth (cheilosis)
2. Redness and swelling of the tongue
3. Dry, itchy skin
4. Fatigue
5. Headaches
6. Dizziness
7. Muscle weakness
8. Seizures (in severe cases)
Diagnosis of riboflavin deficiency is typically made based on a combination of symptoms, physical examination findings, and laboratory tests. Treatment involves supplementation with riboflavin, which can help to resolve symptoms and prevent complications.
In summary, riboflavin deficiency is a condition where the body does not have enough riboflavin, leading to a range of symptoms and potential health complications. It is important for individuals at risk for deficiency to be aware of the signs and symptoms, and to seek medical attention if they suspect they may have a deficiency.
1. Muscular dystrophy: A group of genetic disorders characterized by progressive muscle weakness and degeneration.
2. Myopathy: A condition where the muscles become damaged or diseased, leading to muscle weakness and wasting.
3. Fibromyalgia: A chronic condition characterized by widespread pain, fatigue, and muscle stiffness.
4. Rhabdomyolysis: A condition where the muscle tissue is damaged, leading to the release of myoglobin into the bloodstream and potentially causing kidney damage.
5. Polymyositis/dermatomyositis: Inflammatory conditions that affect the muscles and skin.
6. Muscle strain: A common injury caused by overstretching or tearing of muscle fibers.
7. Cervical dystonia: A movement disorder characterized by involuntary contractions of the neck muscles.
8. Myasthenia gravis: An autoimmune disorder that affects the nerve-muscle connection, leading to muscle weakness and fatigue.
9. Oculopharyngeal myopathy: A condition characterized by weakness of the muscles used for swallowing and eye movements.
10. Inclusion body myositis: An inflammatory condition that affects the muscles, leading to progressive muscle weakness and wasting.
These are just a few examples of the many different types of muscular diseases that can affect individuals. Each condition has its unique set of symptoms, causes, and treatment options. It's important for individuals experiencing muscle weakness or wasting to seek medical attention to receive an accurate diagnosis and appropriate care.
Liver neoplasms, also known as liver tumors or hepatic tumors, are abnormal growths of tissue in the liver. These growths can be benign (non-cancerous) or malignant (cancerous). Malignant liver tumors can be primary, meaning they originate in the liver, or metastatic, meaning they spread to the liver from another part of the body.
There are several types of liver neoplasms, including:
1. Hepatocellular carcinoma (HCC): This is the most common type of primary liver cancer and arises from the main cells of the liver (hepatocytes). HCC is often associated with cirrhosis and can be caused by viral hepatitis or alcohol abuse.
2. Cholangiocarcinoma: This type of cancer arises from the cells lining the bile ducts within the liver (cholangiocytes). Cholangiocarcinoma is rare and often diagnosed at an advanced stage.
3. Hemangiosarcoma: This is a rare type of cancer that originates in the blood vessels of the liver. It is most commonly seen in dogs but can also occur in humans.
4. Fibromas: These are benign tumors that arise from the connective tissue of the liver (fibrocytes). Fibromas are usually small and do not spread to other parts of the body.
5. Adenomas: These are benign tumors that arise from the glandular cells of the liver (hepatocytes). Adenomas are usually small and do not spread to other parts of the body.
The symptoms of liver neoplasms vary depending on their size, location, and whether they are benign or malignant. Common symptoms include abdominal pain, fatigue, weight loss, and jaundice (yellowing of the skin and eyes). Diagnosis is typically made through a combination of imaging tests such as CT scans, MRI scans, and ultrasound, and a biopsy to confirm the presence of cancer cells.
Treatment options for liver neoplasms depend on the type, size, location, and stage of the tumor, as well as the patient's overall health. Surgery may be an option for some patients with small, localized tumors, while others may require chemotherapy or radiation therapy to shrink the tumor before surgery can be performed. In some cases, liver transplantation may be necessary.
Prognosis for liver neoplasms varies depending on the type and stage of the cancer. In general, early detection and treatment improve the prognosis, while advanced-stage disease is associated with a poorer prognosis.
There are several different types of leukemia, including:
1. Acute Lymphoblastic Leukemia (ALL): This is the most common type of leukemia in children, but it can also occur in adults. It is characterized by an overproduction of immature white blood cells called lymphoblasts.
2. Acute Myeloid Leukemia (AML): This type of leukemia affects the bone marrow's ability to produce red blood cells, platelets, and other white blood cells. It can occur at any age but is most common in adults.
3. Chronic Lymphocytic Leukemia (CLL): This type of leukemia affects older adults and is characterized by the slow growth of abnormal white blood cells called lymphocytes.
4. Chronic Myeloid Leukemia (CML): This type of leukemia is caused by a genetic mutation in a gene called BCR-ABL. It can occur at any age but is most common in adults.
5. Hairy Cell Leukemia: This is a rare type of leukemia that affects older adults and is characterized by the presence of abnormal white blood cells called hairy cells.
6. Myelodysplastic Syndrome (MDS): This is a group of disorders that occur when the bone marrow is unable to produce healthy blood cells. It can lead to leukemia if left untreated.
Treatment for leukemia depends on the type and severity of the disease, but may include chemotherapy, radiation therapy, targeted therapy, or stem cell transplantation.
Coenzyme A transferases
3-oxoacid CoA-transferase
Transferase
Coenzyme Q5, methyltransferase
Malonate CoA-transferase
Propionate CoA-transferase
Formyl-CoA transferase
Oxalyl-CoA decarboxylase
OXCT1
Acetate CoA-transferase
Coenzyme-B sulfoethylthiotransferase
Quinate O-hydroxycinnamoyltransferase
COQ2
Coenzyme A
5-hydroxypentanoate CoA-transferase
Isobutyryl-CoA mutase
Oxalate CoA-transferase
3-oxoadipate CoA-transferase
Tartronate O-hydroxycinnamoyltransferase
Succinate-hydroxymethylglutarate CoA-transferase
Cinnamoyl-CoA:phenyllactate CoA-transferase
Succinyl-CoA:3-oxoacid CoA transferase deficiency
2-acylglycerol O-acyltransferase
Isopenicillin N N-acyltransferase
Butyrate-acetoacetate CoA-transferase
Diacylglycerol ethanolaminephosphotransferase
2-hydroxypropyl-CoM lyase
Glutaconyl-CoA
Flavonol-3-O-triglucoside O-coumaroyltransferase
Serine dehydratase
Methanogenesis
Metabolism
List of diseases (C)
Enzyme inhibitor
Polysialic-acid O-acetyltransferase
Glutathione synthetase
D-ornithine 4,5-aminomutase
Dephospho-CoA kinase
Chromosome 6
Dephospho-(reductase kinase) kinase
Sterol O-acyltransferase
Fatty acid oxidation inhibitors
RNA world
Melatonin
Oxalate degrading enzyme
Ribonucleotide
Cinnamoyl-CoA
Uridine diphosphate N-acetylglucosamine
Precorrin-6A synthase (deacetylating)
MMACHC
List of OMIM disorder codes
N-acetylneuraminate 7-O(or 9-O)-acetyltransferase
List of EC numbers (EC 6)
Butyric acid
Palmitoyl-CoA
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About Us
Protein2
- System kinetics were influenced by domain dissections, and the FAS phosphopantetheinyl transferase (PPT) monodomain exhibited coenzyme A selectivity for the post-translational activation of the FAS acyl carrier protein (ACP). (nih.gov)
- This gene encodes the bifunctional protein coenzyme A synthase (CoAsy) which carries out the last two steps in the biosynthesis of CoA from pantothenic acid (vitamin B5). (nih.gov)
Acetyl2
- Enzymes which transfer coenzyme A moieties from acyl- or acetyl-CoA to various carboxylic acceptors forming a thiol ester. (nih.gov)
- Coenzyme A (CoA) functions as a carrier of acetyl and acyl groups in cells and thus plays an important role in numerous synthetic and degradative metabolic pathways in all organisms. (nih.gov)
Cholesterol2
- Role of acyl-coenzyme A: cholesterol transferase 1 (ACAT1) in retinal neovascularization. (bvsalud.org)
- We have investigated the efficacy of a new strategy to limit pathological retinal neovascularization (RNV) during ischemic retinopathy by targeting the cholesterol metabolizing enzyme acyl- coenzyme A cholesterol transferase 1 (ACAT1). (bvsalud.org)
Encodes1
- in two siblings with the infantile form of CoQ10 deficiency, we identified a homozygous missense mutation in the COQ2 gene which encodes para-hydroxybenzoate-polyprenyl transferase, the enzyme responsible for the condensation of the isoprenoid side chains to the benzoquinone ring. (nih.gov)
Reactions1
- It catalyzes 2 types of reactions, which involve either rearrangements (conversion of l methylmalonyl coenzyme A [CoA] to succinyl CoA) or methylation (synthesis of methionine). (medscape.com)
Acid2
- An acyl-CoA that results from the formal condensation of the thiol group of coenzyme A with the carboxy group of propionic acid. (mcw.edu)
- The former is required for conversion of L- methylmalonic acid to succinyl coenzyme A (CoA), and the latter acts as a methyltransferase for conversion of homocysteine to methionine. (medscape.com)
Active1
- The cobalt atom is reduced in a nicotinamide adenine dinucleotide (NADH)-dependent reaction to yield the active coenzyme. (medscape.com)
Cells1
- Aim 4: In collaboration with Professor Placido Navas, University of Sevilla, Spain, we will characterize CoQ10 biosynthetic genes and mutations in yeast.Narrative Coenzyme Q10 (CoQ10) is a vital molecule required for cells to generate energy and to prevent damage from toxic oxygen radicals. (nih.gov)
Primary coenzyme Q10 deficiency3
- However, the COQ2 gene variations associated with an increased risk of this disorder are thought to affect coenzyme Q10 levels less severely than the COQ2 gene mutations that cause primary coenzyme Q10 deficiency (described below). (nih.gov)
- At least nine mutations in the COQ2 gene have been found to cause a disorder known as primary coenzyme Q10 deficiency. (nih.gov)
- These changes can cause cells throughout the body to malfunction, which may help explain the variety of organs and tissues that can be affected by primary coenzyme Q10 deficiency. (nih.gov)
Enzymes1
- Enzymes which transfer coenzyme A moieties from acyl- or acetyl-CoA to various carboxylic acceptors forming a thiol ester. (nih.gov)
Deficiency5
- In two siblings of consanguineous parents with the infantile form of CoQ(10) deficiency, we identified a homozygous missense mutation in the COQ2 gene, which encodes para-hydroxybenzoate-polyprenyl transferase. (nih.gov)
- in two siblings with the infantile form of CoQ10 deficiency, we identified a homozygous missense mutation in the COQ2 gene which encodes para-hydroxybenzoate-polyprenyl transferase, the enzyme responsible for the condensation of the isoprenoid side chains to the benzoquinone ring. (nih.gov)
- Studies suggest that a shortage (deficiency) of coenzyme Q10 impairs oxidative phosphorylation and increases the vulnerability of cells to damage from free radicals. (nih.gov)
- A deficiency of coenzyme Q10 may also disrupt the production of pyrimidines. (nih.gov)
- Desbats MA, Lunardi G, Doimo M, Trevisson E, Salviati L. Genetic bases and clinical manifestations of coenzyme Q10 (CoQ 10) deficiency. (nih.gov)
Molecule3
- Abstract: Coenzyme Q10 (CoQ10) is a small lipophillic molecule composed of a benzoquinone ring and a hydrophobic isoprenoid tail and is present in virtually all cell membranes. (nih.gov)
- Aim 4: In collaboration with Professor Placido Navas, University of Sevilla, Spain, we will characterize CoQ10 biosynthetic genes and mutations in yeast.Narrative Coenzyme Q10 (CoQ10) is a vital molecule required for cells to generate energy and to prevent damage from toxic oxygen radicals. (nih.gov)
- The COQ2 gene provides instructions for making an enzyme that carries out one step in the production of a molecule called coenzyme Q10, which has several critical functions in cells throughout the body. (nih.gov)
Mutations1
- The COQ2 gene mutations associated with this disorder greatly reduce or eliminate the production of the COQ2 enzyme, which prevents the normal production of coenzyme Q10. (nih.gov)
COQ21
- Researchers speculate that changes in the COQ2 gene could impair the activity of the COQ2 enzyme, which would affect the production of coenzyme Q10. (nih.gov)