A hydro-lyase that catalyzes the dehydration of 2-phosphoglycerate to form PHOSPHOENOLPYRUVATE. Several different isoforms of this enzyme exist, each with its own tissue specificity.
An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonyl-CoA. EC 4.2.1.17.
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
Pyruvates, in the context of medical and biochemistry definitions, are molecules that result from the final step of glycolysis, containing a carboxylic acid group and an aldehyde group, playing a crucial role in cellular metabolism, including being converted into Acetyl-CoA to enter the Krebs cycle or lactate under anaerobic conditions.
A compound composed of a two CYCLIC PEPTIDES attached to a phenoxazine that is derived from STREPTOMYCES parvullus. It binds to DNA and inhibits RNA synthesis (transcription), with chain elongation more sensitive than initiation, termination, or release. As a result of impaired mRNA production, protein synthesis also declines after dactinomycin therapy. (From AMA Drug Evaluations Annual, 1993, p2015)
An enzyme that catalyzes the reversible hydration of fumaric acid to yield L-malic acid. It is one of the citric acid cycle enzymes. EC 4.2.1.2.
Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.
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.
The state of having multiple leiomyomas throughout the body. (Stedman, 25th ed)
A monomeric protein found in liver peroxisomes that contains two enzymatically active domains; an enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase domain, and an (S)-3-hydroxyacyl-CoA dehydrogenase domain. The enzyme is stereospecific with regards to how cis and trans double bonds are metabolized. It is complemented by PEROXISOMAL MULTIFUNCTIONAL PROTEIN-2, which has the opposite stereospecificity.
A bacterial genus of the order ACTINOMYCETALES.
A carbon-carbon double bond isomerase that catalyzes the movement double bond from C3 to C2 of an unsaturated acyl-CoA. The enzyme plays a key role in allowing acyl-CoA substrates to re-enter the beta-oxidation pathway.
Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to another within the same molecule. EC 5.3.3.
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.
A PEROXISOME-specific enzyme that catalyzes the hydration step of the beta-oxidation pathway.
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
Enzymes that catalyze inversion of the configuration around an asymmetric carbon in a substrate having one (racemase) or more (epimerase) center(s) of asymmetry. (Dorland, 28th ed) EC 5.1.
Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.
S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.
Tungsten. A metallic element with the atomic symbol W, atomic number 74, and atomic weight 183.85. It is used in many manufacturing applications, including increasing the hardness, toughness, and tensile strength of steel; manufacture of filaments for incandescent light bulbs; and in contact points for automotive and electrical apparatus.
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.
Derivatives of BUTYRIC ACID that include a double bond between carbon 2 and 3 of the aliphatic structure. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include the aminobutryrate structure.
An enzyme that catalyzes the reversible hydration of cis-aconitate to yield citrate or isocitrate. It is one of the citric acid cycle enzymes. EC 4.2.1.3.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
A highly poisonous compound used widely in the manufacture of plastics, adhesives and synthetic rubber.
A genus of gram-negative, rod-shaped bacteria able to anaerobically oxidize and degrade toluene.
Enzymes that catalyze reversibly the formation of an epoxide or arene oxide from a glycol or aromatic diol, respectively.
Fatty acid biopolymers that are biosynthesized by microbial polyhydroxyalkanoate synthase enzymes. They are being investigated for use as biodegradable polyesters.
The condition of a pattern of malignancies within a family, but not every individual's necessarily having the same neoplasm. Characteristically the tumor tends to occur at an earlier than average age, individuals may have more than one primary tumor, the tumors may be multicentric, usually more than 25 percent of the individuals in direct lineal descent from the proband are affected, and the cancer predisposition in these families behaves as an autosomal dominant trait with about 60 percent penetrance.
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.
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.
A gram-positive organism found in dairy products, fresh and salt water, marine organisms, insects, and decaying organic matter.
A cytosolic carbonic anhydrase isoenzyme primarily expressed in ERYTHROCYTES, vascular endothelial cells, and the gastrointestinal mucosa. EC 4.2.1.-
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Aconitic Acid is a weak organic acid, naturally found in some fruits and vegetables, that metabolizes to citric acid in the body and has been used in traditional medicine but can be toxic in high concentrations.
Isocitrate is a chemical compound, an isomer of citric acid, which is a key intermediate in the tricarboxylic acid cycle (Krebs cycle) and is involved in energy production through cellular respiration in living organisms.
A group of PROTEOBACTERIA represented by morphologically diverse, anaerobic sulfidogens. Some members of this group are considered bacterial predators, having bacteriolytic properties.
Microbodies which occur in animal and plant cells and in certain fungi and protozoa. They contain peroxidase, catalase, and allied enzymes. (From Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2nd ed)
Compounds that either share the structure of fibric acid in their molecular arrangement or are considered variants of the fibric acid structure.
A flavoring agent. It is the intermediate product in the two-step bioconversion of ferulic acid to vanillin. (J Biotechnol 1996;50(2-3):107-13).
Compounds based on fumaric acid.
A trace element that is a component of vitamin B12. It has the atomic symbol Co, atomic number 27, and atomic weight 58.93. It is used in nuclear weapons, alloys, and pigments. Deficiency in animals leads to anemia; its excess in humans can lead to erythrocytosis.
An enzyme that catalyzes the first and rate-determining steps of peroxisomal beta-oxidation of fatty acids. It acts on COENZYME A derivatives of fatty acids with chain lengths from 8 to 18, using FLAVIN-ADENINE DINUCLEOTIDE as a cofactor.
The alpha subunit of mitochondrial trifunctional protein. It contains both enoyl-CoA hydratase activity (EC 4.2.1.17) and long-chain-3-hydroxyacyl-CoA dehydrogenase activity (EC 1.1.1.211). There are four of these alpha subunits in each mitochondrial trifunctional protein molecule.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Coenzyme A is an essential coenzyme that plays a crucial role in various metabolic processes, particularly in the transfer and activation of acetyl groups in important biochemical reactions such as fatty acid synthesis and oxidation, and the citric acid cycle.
A species of gram-negative, aerobic bacteria isolated from soil and water as well as clinical specimens. Occasionally it is an opportunistic pathogen.
An organization of cells into an organ-like structure. Organoids can be generated in culture. They are also found in certain neoplasms.
Tumors or cancer of the UTERUS.
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).
A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A cyanide compound which has been used as a fertilizer, defoliant and in many manufacturing processes. It often occurs as the calcium salt, sometimes also referred to as cyanamide. The citrated calcium salt is used in the treatment of alcoholism.
A species of MITOSPORIC FUNGI that is a major cause of SEPTICEMIA and disseminated CANDIDIASIS, especially in patients with LYMPHOMA; LEUKEMIA; and DIABETES MELLITUS. It is also found as part of the normal human mucocutaneous flora.
Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)
An antilipemic agent that is the biologically active metabolite of CLOFIBRATE.
An enzyme that catalyzes the conversion of 4,5-dihydro-4-oxo-5-imidazolepropanoate to urocanate and water. EC 4.2.1.49.
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.
Complex of iron atoms chelated with carbonyl ions.
A heterogeneous group of inherited metabolic disorders marked by absent or dysfunctional PEROXISOMES. Peroxisomal enzymatic abnormalities may be single or multiple. Biosynthetic peroxisomal pathways are compromised, including the ability to synthesize ether lipids and to oxidize long-chain fatty acid precursors. Diseases in this category include ZELLWEGER SYNDROME; INFANTILE REFSUM DISEASE; rhizomelic chondrodysplasia (CHONDRODYSPLASIA PUNCTATA, RHIZOMELIC); hyperpipecolic acidemia; neonatal adrenoleukodystrophy; and ADRENOLEUKODYSTROPHY (X-linked). Neurologic dysfunction is a prominent feature of most peroxisomal disorders.
"Citrates, in a medical context, are compounds containing citric acid, often used in medical solutions for their chelating properties and as a part of certain types of nutritional support."
Benzaldehydes are aromatic organic compounds consisting of a benzene ring connected to a formyl group (-CHO), which is the simplest and most representative compound being benzaldehyde (C6H5CHO).

Adult subventricular zone neuronal precursors continue to proliferate and migrate in the absence of the olfactory bulb. (1/1229)

Neurons continue to be born in the subventricular zone (SVZ) of the lateral ventricles of adult mice. These cells migrate as a network of chains through the SVZ and the rostral migratory stream (RMS) into the olfactory bulb (OB), where they differentiate into mature neurons. The OB is the only known target for these neuronal precursors. Here, we show that, after elimination of the OB, the SVZ and RMS persist and become dramatically larger. The proportion of dividing [bromodeoxyuridine (BrdU)-labeled] or dying (pyknotic or terminal deoxynucleotidyl transferase-mediated biotinylated UTP nick end-labeled) cells in the RMS was not significantly affected at 3 d or 3 weeks after bulbectomy (OBX). However, by 3 months after OBX, the percentage of BrdU-labeled cells in the RMS decreased by half and that of dying cells doubled. Surprisingly, the rostral migration of precursors continued along the RMS after OBX. This was demonstrated by focal microinjections of BrdU and grafts of SVZ cells carrying LacZ under the control of a neuron-specific promoter gene. Results indicate that the OB is not essential for proliferation and the directional migration of SVZ precursors.  (+info)

Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation. (2/1229)

We initially identified c-myc promoter binding protein 1 (MBP-1), which negatively regulates c-myc promoter activity, from a human cervical carcinoma cell expression library. Subsequent studies on the biological role of MBP-1 demonstrated induction of cell death in fibroblasts and loss of anchorage-independent growth, reduced invasive ability, and tumorigenicity of human breast carcinoma cells. To investigate the potential role of MBP-1 as a transcriptional regulator, a chimeric protein containing MBP-1 fused to the DNA binding domain of the yeast transactivator factor GAL4 was constructed. This fusion protein exhibited repressor activity on the herpes simplex virus thymidine kinase promoter via upstream GAL4 DNA binding sites. Structure-function analysis of mutant MBP-1 in the context of the GAL4 DNA binding domain revealed that MBP-1 transcriptional repressor domains are located in the N terminus (amino acids 1 to 47) and C terminus (amino acids 232 to 338), whereas the activation domain lies in the middle (amino acids 140 to 244). The N-terminal domain exhibited stronger transcriptional repressor activity than the C-terminal region. When the N-terminal repressor domain was transferred to a potent activator, transcription was strongly inhibited. Both of the repressor domains contained hydrophobic regions and had an LXVXL motif in common. Site-directed mutagenesis in the repressor domains indicated that the leucine residues in the LXVXL motif are required for transcriptional repression. Mutation of the leucine residues in the common motif of MBP-1 also abrogated the repressor activity on the c-myc promoter. In addition, the leucine mutant forms of MBP-1 failed to suppress cell growth in fibroblasts like wild-type MBP-1. Taken together, our results indicate that MBP-1 is a complex cellular factor containing multiple transcriptional regulatory domains that play an important role in cell growth regulation.  (+info)

Maturation of the myogenic program is induced by postmitotic expression of insulin-like growth factor I. (3/1229)

The molecular mechanisms underlying myogenic induction by insulin-like growth factor I (IGF-I) are distinct from its proliferative effects on myoblasts. To determine the postmitotic role of IGF-I on muscle cell differentiation, we derived L6E9 muscle cell lines carrying a stably transfected rat IGF-I gene under the control of a myosin light chain (MLC) promoter-enhancer cassette. Expression of MLC-IGF-I exclusively in differentiated L6E9 myotubes, which express the embryonic form of myosin heavy chain (MyHC) and no endogenous IGF-I, resulted in pronounced myotube hypertrophy, accompanied by activation of the neonatal MyHC isoform. The hypertrophic myotubes dramatically increased expression of myogenin, muscle creatine kinase, beta-enolase, and IGF binding protein 5 and activated the myocyte enhancer factor 2C gene which is normally silent in this cell line. MLC-IGF-I induction in differentiated L6E9 cells also increased the expression of a transiently transfected LacZ reporter driven by the myogenin promoter, demonstrating activation of the differentiation program at the transcriptional level. Nuclear reorganization, accumulation of skeletal actin protein, and an increased expression of beta1D integrin were also observed. Inhibition of the phosphatidyl inositol (PI) 3-kinase intermediate in IGF-I-mediated signal transduction confirmed that the PI 3-kinase pathway is required only at early stages for IGF-I-mediated hypertrophy and neonatal MyHC induction in these cells. Expression of IGF-I in postmitotic muscle may therefore play an important role in the maturation of the myogenic program.  (+info)

Neuronal and glial cell type-specific promoters within adenovirus recombinants restrict the expression of the apoptosis-inducing molecule Fas ligand to predetermined brain cell types, and abolish peripheral liver toxicity. (4/1229)

Gene therapy using Fas ligand (FasL) for treatment of tumours and protection of transplant rejection is hampered because of the systemic toxicity of FasL. In the present study, recombinant replication-defective adenovirus vectors (RAds) encoding FasL under the control of either the neuronal-specific neuronal-specific enolase (NSE) promoter or the astrocyte-specific glial fibrillary acidic protein (GFAP) promoter have been constructed. The cell type-specific expression of FasL in both neurons and glial cells in primary cultures, and in neuronal and glial cell lines is demonstrated. Furthermore, transgene expression driven by the neuronal and glial promoter was not detected in fibroblastic or epithelial cell lines. Expression of FasL driven by a major immediate early human cytomegalovirus promoter (MIEhCMV) was, however, achieved in all cells tested. As a final test of the stringency of transgene-specific expression, the RAds were injected directly into the bloodstream of mice. The RAds encoding FasL under the control of the non-cell type-specific MIEhCMV promoter induced acute generalized liver haemorrhage with hepatocyte apoptosis, while the RAds containing the NSE or GFAP promoter sequences were completely non-toxic. This demonstrates the specificity of transgene expression, enhanced safety during systemic administration, and tightly regulated control of transgene expression of highly cytotoxic gene products, encoded within transcriptionally targeted RAds.  (+info)

Structural and functional analysis of pCI65st, a 6.5 kb plasmid from Streptococcus thermophilus NDI-6. (5/1229)

The 6.5 kb cryptic plasmid pCI65st from Streptococcus thermophilus NDI-6, a strain isolated from the Indian fermented milk dahi, was subcloned and sequenced. Five putative ORFs were identified. ORF1 could encode a 315 aa polypeptide almost identical to the RepA protein of previously sequenced S. thermophilus plasmids, indicating that pCI65st is one of the pC194 group of small gram-positive rolling-circle plasmids. ORFs 2 and 4 were virtually identical and could specify proteins of approximately 150 aa with significant similarity to the small heat-shock proteins described from a variety of gram-positive bacteria. ORF3 could encode a 415 aa protein similar to enolase, an enzyme involved in glycolysis and gluconeogenesis. ORF5 could encode a 412 aa protein which had high similarity to the HsdS (specificity) proteins of type I restriction-modification systems. Variants of strain NDI-6 which lacked pCI65st were readily isolated after subculture of the parent strain at 32 degrees C. The plasmid-bearing parent culture was significantly more resistant to a temperature shift from 42 degrees C to 62 degrees C than its plasmid-free variant and expressed proteins which corresponded with the predicted translation products from ORF2 and ORF4. In addition, plasmid-free mutants were lysed in broth by bacteriophages to which the parent culture was resistant.  (+info)

Early neurobehavioral outcome after stroke is related to release of neurobiochemical markers of brain damage. (6/1229)

BACKGROUND AND PURPOSE: The study aimed to investigate the predictive value of neurobiochemical markers of brain damage (protein S-100B and neuron-specific enolase [NSE]) with respect to early neurobehavioral outcome after stroke. METHODS: We investigated 58 patients with completed stroke who were admitted to the stroke unit of the Department of Neurology at Magdeburg University. Serial venous blood samples were taken after admission and during the first 4 days, and protein S-100B and NSE were analyzed by the use of immunoluminometric assays. In all patients, lesion topography and vascular supply were analyzed and volume of infarcted brain areas was calculated. The neurological status was evaluated by a standardized neurological examination and the National Institutes of Health Stroke Scale (NIHSS) on admission, at days 1 and 4 on the stroke unit, at day 10, and at discharge from the hospital. Comprehensive neuropsychological examinations were performed in all patients with first-ever stroke event and supratentorial brain infarctions. Functional outcome was measured with the Barthel score at discharge from the hospital. RESULTS: NSE and protein S-100B concentrations were significantly correlated with both volume of infarcted brain areas and NIHSS scores. Patients with an adverse neurological outcome had a significantly higher and significantly longer release of both markers. Neuropsychological impairment was associated with higher protein S-100B release, but this did not reach statistical significance. CONCLUSIONS: Serum concentrations and kinetics of protein S-100B and NSE have a high predictive value for early neurobehavioral outcome after acute stroke. Protein S-100B concentrations at days 2 to 4 after acute stroke may provide valuable information for both neurological status and functional impairment at discharge from the acute care hospital.  (+info)

Time course of neurone-specific enolase and S-100 protein release during and after coronary artery bypass grafting. (7/1229)

Serum neurone-specific enolase (NSE) and S-100 protein are well established as markers of cerebral injury, and have been used as markers of neuronal and glial cell damage, respectively, after cardiac surgery with cardiopulmonary bypass (CPB), but the speed of their increase during CPB has not been studied. Therefore, we have investigated the time course of NSE and S-100 release during and after CPB. We studied 18 adult patients undergoing elective coronary artery bypass grafting (CABG). Standard hypothermic (32 degrees C) pulsatile bypass with membrane oxygenation was used. Blood samples were obtained at induction, before bypass, before rewarming, at the end of rewarming, 10 min, 1 h and 8 h after bypass and 1, 2 and 3 days after surgery. NSE and S-100 were assayed using immunoradiometric assay kits (Sangtec Medical). NSE and S-100 release followed similar time courses. Both increased sharply during bypass, reached peak concentrations at the end of rewarming (mean 25.55 (SEM 2.79) and 1.65 (0.23) microgram litre-1, respectively), had decreased significantly by the end of operation and returned to pre-bypass concentrations by the second day after surgery. No patient developed a major neurological deficit. When using NSE and S-100 assays to study cerebral dysfunction in relation to CPB, postoperative samples miss peak (end-bypass) concentrations, and studies should be designed to include intraoperative samples.  (+info)

Quinupristin/dalfopristin attenuates the inflammatory response and reduces the concentration of neuron-specific enolase in the cerebrospinal fluid of rabbits with experimental Streptococcus pneumoniae meningitis. (8/1229)

The inflammatory response following initiation of antibiotic therapy and parameters of neuronal damage were compared during intravenous treatment with quinupristin/dalfopristin (100 mg/kg as either a short or a continuous infusion) and ceftriaxone (10 mg/kg/h) in a rabbit model of Streptococcus pneumoniae meningitis. With both modes of administration, quinupristin/dalfopristin was less bactericidal than ceftriaxone. However, the concentration of proinflammatory cell wall components (lipoteichoic acid (LTA) and teichoic acid (TA)) and the activity of tumour necrosis factor (TNF) in cerebrospinal fluid (CSF) were significantly lower in the two quinupristin/dalfopristin groups than in ceftriaxone-treated rabbits. The median LTA/TA concentrations (25th/75th percentiles) were as follows: (i) 14 h after infection: 133 (72/155) ng/mL for continuous infusion of quinupristin/dalfopristin and 193 (91/308) ng/mL for short duration infusion, compared with 455 (274/2042) ng/mL for ceftriaxone (P = 0.002 and 0.02 respectively); (ii) 17 h after infection: 116 (60/368) ng/mL for continuous infusion of quinupristin/dalfopristin and 117 (41/247) ng/mL for short duration infusion, compared with 694 (156/2173) ng/mL for ceftriaxone (P = 0.04 and 0.03 respectively). Fourteen hours after infection the median TNF activity (25th/75th percentiles) was 0.2 (0.1/1.9) U/mL for continuous infusion of quinupristin/dalfopristin and 0.1 (0.01/3.5) U/mL for short duration infusion, compared with 30 (4.6/180) U/mL for ceftriaxone (P = 0.02 for each comparison); 17 h after infection the TNF activity was 2.8 (0.2/11) U/mL (continuous infusion of quinupristin/dalfopristin) and 0.1 (0.04/6.1) U/mL (short duration infusion), compared with 48.6 (18/169) U/mL for ceftriaxone (P = 0.002 and 0.001). The concentration of neuron-specific enolase (NSE) 24 h after infection was significantly lower in animals treated with quinupristin/dalfopristin: 4.6 (3.3/5.7) microg/L (continuous infusion) and 3.6 (2.9/4.7) microg/L (short duration infusion) than in those treated with ceftriaxone (17.7 (8.8/78.2) microg/L) (P = 0.03 and 0.009 respectively). In conclusion, antibiotic treatment with quinupristin/dalfopristin attenuated the inflammatory response within the subarachnoid space after initiation of antibiotic therapy. The concentration of NSE in the CSF, taken as a measure of neuronal damage, was lower in quinupristin/dalfopristin-treated rabbits than in ceftriaxone-treated rabbits.  (+info)

Phosphopyruvate Hydratase is an enzyme also known as Enolase. It plays a crucial role in the glycolytic pathway, which is a series of reactions that occur in the cell to break down glucose into pyruvate, producing ATP and NADH as energy-rich intermediates.

Specifically, Phosphopyruvate Hydratase catalyzes the conversion of 2-phospho-D-glycerate (2-PG) to phosphoenolpyruvate (PEP), which is the second to last step in the glycolytic pathway. This reaction includes the removal of a water molecule from 2-PG, resulting in the formation of PEP and the release of a molecule of water.

The enzyme requires magnesium ions as a cofactor for its activity, and it is inhibited by fluoride ions. Deficiency or dysfunction of Phosphopyruvate Hydratase can lead to various metabolic disorders, including some forms of muscular dystrophy and neurodegenerative diseases.

Enoyl-CoA hydratase is an enzyme that catalyzes the second step in the fatty acid oxidation process, also known as the beta-oxidation pathway. The systematic name for this reaction is (3R)-3-hydroxyacyl-CoA dehydratase.

The function of Enoyl-CoA hydratase is to convert trans-2-enoyl-CoA into 3-hydroxyacyl-CoA by adding a molecule of water (hydration) across the double bond in the substrate. This reaction forms a chiral center, resulting in the production of an (R)-stereoisomer of 3-hydroxyacyl-CoA.

The gene that encodes for Enoyl-CoA hydratase is called ECHS1, and mutations in this gene can lead to a rare genetic disorder known as Enoyl-CoA Hydratase Deficiency or ECHS1 Deficiency. This condition affects the breakdown of fatty acids in the body and can cause neurological symptoms such as developmental delay, seizures, and movement disorders.

Carboxy-lyases are a class of enzymes that catalyze the removal of a carboxyl group from a substrate, often releasing carbon dioxide in the process. These enzymes play important roles in various metabolic pathways, such as the biosynthesis and degradation of amino acids, sugars, and other organic compounds.

Carboxy-lyases are classified under EC number 4.2 in the Enzyme Commission (EC) system. They can be further divided into several subclasses based on their specific mechanisms and substrates. For example, some carboxy-lyases require a cofactor such as biotin or thiamine pyrophosphate to facilitate the decarboxylation reaction, while others do not.

Examples of carboxy-lyases include:

1. Pyruvate decarboxylase: This enzyme catalyzes the conversion of pyruvate to acetaldehyde and carbon dioxide during fermentation in yeast and other organisms.
2. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO): This enzyme is essential for photosynthesis in plants and some bacteria, as it catalyzes the fixation of carbon dioxide into an organic molecule during the Calvin cycle.
3. Phosphoenolpyruvate carboxylase: Found in plants, algae, and some bacteria, this enzyme plays a role in anaplerotic reactions that replenish intermediates in the citric acid cycle. It catalyzes the conversion of phosphoenolpyruvate to oxaloacetate and inorganic phosphate.
4. Aspartate transcarbamylase: This enzyme is involved in the biosynthesis of pyrimidines, a class of nucleotides. It catalyzes the transfer of a carboxyl group from carbamoyl aspartate to carbamoyl phosphate, forming cytidine triphosphate (CTP) and fumarate.
5. Urocanase: Found in animals, this enzyme is involved in histidine catabolism. It catalyzes the conversion of urocanate to formiminoglutamate and ammonia.

Pyruvate is a negatively charged ion or group of atoms, called anion, with the chemical formula C3H3O3-. It is formed from the decomposition of glucose and other sugars in the process of cellular respiration. Pyruvate plays a crucial role in the metabolic pathways that generate energy for cells.

In the cytoplasm, pyruvate is produced through glycolysis, where one molecule of glucose is broken down into two molecules of pyruvate, releasing energy and producing ATP (adenosine triphosphate) and NADH (reduced nicotinamide adenine dinucleotide).

In the mitochondria, pyruvate can be further metabolized through the citric acid cycle (also known as the Krebs cycle) to produce more ATP. The process involves the conversion of pyruvate into acetyl-CoA, which then enters the citric acid cycle and undergoes a series of reactions that generate energy in the form of ATP, NADH, and FADH2 (reduced flavin adenine dinucleotide).

Overall, pyruvate is an important intermediate in cellular respiration and plays a central role in the production of energy for cells.

Dactinomycin is an antineoplastic antibiotic, which means it is used to treat cancer. It is specifically used to treat certain types of testicular cancer, Wilms' tumor (a type of kidney cancer that occurs in children), and some gestational trophoblastic tumors (a type of tumor that can develop in the uterus after pregnancy). Dactinomycin works by interfering with the DNA in cancer cells, which prevents them from dividing and growing. It is often used in combination with other chemotherapy drugs as part of a treatment regimen.

Dactinomycin is administered intravenously (through an IV) and its use is usually limited to hospitals or specialized cancer treatment centers due to the need for careful monitoring during administration. Common side effects include nausea, vomiting, and hair loss. More serious side effects can include bone marrow suppression, which can lead to an increased risk of infection, and tissue damage at the site where the drug is injected. Dactinomycin can also cause severe allergic reactions in some people.

It's important to note that dactinomycin should only be used under the supervision of a qualified healthcare professional, as its use requires careful monitoring and management of potential side effects.

Fumarate hydratase (FH) is an enzyme that plays a crucial role in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle. The citric acid cycle is a series of chemical reactions used by all living cells to generate energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins into adenosine triphosphate (ATP), carbon dioxide, and water.

Fumarate hydratase is specifically responsible for catalyzing the conversion of fumarate to malate in this cycle. A deficiency or dysfunction of this enzyme can lead to various metabolic disorders and hereditary diseases, such as fumarate hydratase deficiency, which may manifest as neurological issues, hemolytic anemia, and an increased risk of developing renal cell carcinoma.

I'm sorry for any confusion, but "Hydro-Lyases" is not a recognized medical term or category in biochemistry. It seems like there might be a misunderstanding or a typo in the term.

In biochemistry, "lyases" are enzymes that catalyze the removal of groups from substrates by means other than hydrolysis or oxidation, often forming a double bond or a ring-forming reaction. They are classified and named based on the type of bond they break.

If you meant to ask about a specific enzyme or reaction, could you please provide more context or clarify the term? I'd be happy to help further with accurate information.

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.

Leiomyomatosis is a medical term that refers to the benign growth (non-cancerous) of smooth muscle cells, which form tumors known as leiomyomas or fibroids. These growths can occur in various parts of the body, including the skin, uterus, gastrointestinal tract, and other organs.

The term "leiomyomatosis" is often used to describe a condition where multiple smooth muscle tumors develop in a single organ or throughout the body. For example:

1. Cutaneous leiomyomatosis - Multiple benign tumors of the smooth muscle in the skin.
2. Uterine leiomyomatosis - Multiple fibroids in the uterus, also known as uterine fibroids or myomas.
3. Gastrointestinal stromal tumor (GIST) leiomyomatosis - Multiple benign smooth muscle tumors in the gastrointestinal tract.
4. Disseminated peritoneal leiomyomatosis - Multiple benign smooth muscle tumors spread across the peritoneum, the lining of the abdominal cavity.

These conditions are usually not cancerous but can cause various symptoms depending on their location and size. Treatment options may include surveillance, medication, or surgical removal of the tumors.

A peroxisomal bifunctional enzyme is not a specific medical term, but it refers to a type of enzyme that has two distinct functional domains and is located within peroxisomes. Peroxisomes are small membrane-bound organelles found in the cells of many organisms, including humans, where they play a crucial role in various metabolic processes, such as fatty acid oxidation and detoxification of harmful substances.

The term "bifunctional" indicates that this enzyme possesses two distinct catalytic activities or functions within the same polypeptide chain. In the context of peroxisomal enzymes, bifunctional enzymes often participate in the breakdown of specific fatty acids, particularly very-long-chain fatty acids (VLCFAs) and branched-chain fatty acids (BCFAs).

An example of a peroxisomal bifunctional enzyme is the D-bifunctional protein (DBP), which has two catalytic domains: one for the oxidation of long-chain 2-enoyl-CoA intermediates and another for the hydratase/dehydrogenase activity. DBP plays a critical role in peroxisomal fatty acid beta-oxidation, particularly for VLCFAs and BCFAs, which cannot be efficiently metabolized by mitochondria.

Defects in peroxisomal bifunctional enzymes can lead to various genetic disorders, such as peroxisome biogenesis disorders (PBDs) or peroxisomal fatty acid oxidation disorders, which may result in severe neurological symptoms and developmental delays.

Rhodococcus is a genus of gram-positive, aerobic, actinomycete bacteria that are widely distributed in the environment, including soil and water. Some species of Rhodococcus can cause opportunistic infections in humans and animals, particularly in individuals with weakened immune systems. These infections can affect various organs and tissues, such as the lungs, skin, and brain, and can range from mild to severe.

Rhodococcus species are known for their ability to degrade a wide variety of organic compounds, including hydrocarbons, making them important players in bioremediation processes. They also have complex cell walls that make them resistant to many antibiotics and disinfectants, which can complicate treatment of Rhodococcus infections.

Dodecenoyl-CoA isomerase is an enzyme that catalyzes the conversion of dodecenoyl-CoA to trans-2-dodecenoyl-CoA in the beta-oxidation pathway of fatty acid metabolism. This enzyme plays a crucial role in the breakdown and energy production from long-chain fatty acids in the body. The isomerization reaction facilitated by this enzyme helps to introduce a double bond at a specific position during the degradation process, allowing for further oxidation and energy release.

Carbon-carbon double bond isomerases are a class of enzymes that catalyze the conversion of one geometric or positional isomer of a molecule containing a carbon-carbon double bond into another. These enzymes play an important role in the metabolism and biosynthesis of various biological compounds, including fatty acids, steroids, and carotenoids.

There are several types of carbon-carbon double bond isomerases, each with their own specific mechanisms and substrate preferences. Some examples include:

1. Ene/Yne Isomerases: These enzymes catalyze the conversion of a carbon-carbon double bond that is conjugated to an alkene or alkyne group into a new double bond location through a series of [1,5]-sigmatropic shifts.

2. Cis-Trans Isomerases: These enzymes catalyze the interconversion of cis and trans geometric isomers of carbon-carbon double bonds. They are often involved in the biosynthesis of complex lipids and other biological molecules where specific stereochemistry is required for proper function.

3. Peroxisomal Isomerases: These enzymes are involved in the metabolism of fatty acids with very long chains (VLCFA) in peroxisomes. They catalyze the conversion of cis-delta(3)-double bonds to trans-delta(2)-double bonds, which is a necessary step for further processing and degradation of VLCFAs.

4. Retinal Isomerases: These enzymes are involved in the visual cycle and catalyze the conversion of 11-cis-retinal into all-trans-retinal during the process of vision.

5. Carotenoid Isomerases: These enzymes are involved in the biosynthesis of carotenoids, which are pigments found in plants and microorganisms. They catalyze the conversion of cis-configured carotenoids into trans-configured forms, which have higher stability and bioactivity.

In general, carbon-carbon double bond isomerases function by lowering the energy barrier for a specific isomerization reaction, allowing it to occur under physiological conditions. They often require cofactors or other proteins to facilitate their activity, and their regulation is critical for maintaining proper metabolism and homeostasis in cells.

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.

Enoyl-CoA hydratase 2 is an enzyme that is encoded by the ECHS2 gene in humans. This enzyme plays a crucial role in the mitochondrial beta-oxidation of fatty acids, which is a process that breaks down fatty acids to generate energy in the form of ATP.

More specifically, enoyl-CoA hydratase 2 catalyzes the second step of this process, which involves the addition of water (hydration) to a double bond in an enoyl-CoA molecule, resulting in the formation of a 3-hydroxyacyl-CoA molecule. This reaction is essential for the continued breakdown and eventual conversion of fatty acids into acetyl-CoA molecules, which can then enter the citric acid cycle to generate ATP.

Defects in the ECHS2 gene have been associated with a rare genetic disorder known as multiple acyl-CoA dehydrogenase deficiency (MADD), also called glutaric acidemia type II. This condition is characterized by impaired mitochondrial fatty acid oxidation and can lead to a range of symptoms, including metabolic acidosis, hypoglycemia, cardiomyopathy, and neurological problems.

Isomerases are a class of enzymes that catalyze the interconversion of isomers of a single molecule. They do this by rearranging atoms within a molecule to form a new structural arrangement or isomer. Isomerases can act on various types of chemical bonds, including carbon-carbon and carbon-oxygen bonds.

There are several subclasses of isomerases, including:

1. Racemases and epimerases: These enzymes interconvert stereoisomers, which are molecules that have the same molecular formula but different spatial arrangements of their atoms in three-dimensional space.
2. Cis-trans isomerases: These enzymes interconvert cis and trans isomers, which differ in the arrangement of groups on opposite sides of a double bond.
3. Intramolecular oxidoreductases: These enzymes catalyze the transfer of electrons within a single molecule, resulting in the formation of different isomers.
4. Mutases: These enzymes catalyze the transfer of functional groups within a molecule, resulting in the formation of different isomers.
5. Tautomeres: These enzymes catalyze the interconversion of tautomers, which are isomeric forms of a molecule that differ in the location of a movable hydrogen atom and a double bond.

Isomerases play important roles in various biological processes, including metabolism, signaling, and regulation.

Racemases and epimerases are two types of enzymes that are involved in the modification of the stereochemistry of molecules, particularly amino acids and sugars. Here is a brief definition for each:

1. Racemases: These are enzymes that catalyze the interconversion of D- and L-stereoisomers of amino acids or other chiral compounds. They do this by promoting the conversion of one stereoisomer to its mirror image, resulting in a racemic mixture (a 1:1 mixture of two enantiomers). Racemases are important in various biological processes, such as the biosynthesis of some amino acids and the degradation of certain carbohydrates.

Example: Alanine racemase is an enzyme that catalyzes the conversion of L-alanine to D-alanine, which is essential for bacterial cell wall biosynthesis.

2. Epimerases: These are enzymes that convert one stereoisomer (epimer) of a chiral compound into another stereoisomer by changing the configuration at a single asymmetric carbon atom while keeping the rest of the molecule unchanged. Unlike racemases, epimerases do not produce racemic mixtures but rather create specific stereoisomers.

Example: Glucose-1-phosphate epimerase is an enzyme that converts glucose-1-phosphate to galactose-1-phosphate during the Leloir pathway, which is the primary metabolic route for lactose digestion in mammals.

Both racemases and epimerases play crucial roles in various biochemical processes, including the synthesis and degradation of essential molecules like amino acids and carbohydrates.

Microbodies are small, membrane-bound organelles found in the cells of eukaryotic organisms. They typically measure between 0.2 to 0.5 micrometers in diameter and play a crucial role in various metabolic processes, particularly in the detoxification of harmful substances and the synthesis of lipids.

There are several types of microbodies, including:

1. Peroxisomes: These are the most common type of microbody. They contain enzymes that help break down fatty acids and amino acids, producing hydrogen peroxide as a byproduct. Another set of enzymes within peroxisomes then converts the harmful hydrogen peroxide into water and oxygen, thus detoxifying the cell.
2. Glyoxysomes: These microbodies are primarily found in plants and some fungi. They contain enzymes involved in the glyoxylate cycle, a metabolic pathway that helps convert stored fats into carbohydrates during germination.
3. Microbody-like particles (MLPs): These are smaller organelles found in certain protists and algae. Their functions are not well understood but are believed to be involved in lipid metabolism.

It is important to note that microbodies do not have a uniform structure or function across all eukaryotic cells, and their specific roles can vary depending on the organism and cell type.

Acyl Coenzyme A (often abbreviated as Acetyl-CoA or Acyl-CoA) is a crucial molecule in metabolism, particularly in the breakdown and oxidation of fats and carbohydrates to produce energy. It is a thioester compound that consists of a fatty acid or an acetate group linked to coenzyme A through a sulfur atom.

Acyl CoA plays a central role in several metabolic pathways, including:

1. The citric acid cycle (Krebs cycle): In the mitochondria, Acyl-CoA is formed from the oxidation of fatty acids or the breakdown of certain amino acids. This Acyl-CoA then enters the citric acid cycle to produce high-energy electrons, which are used in the electron transport chain to generate ATP (adenosine triphosphate), the main energy currency of the cell.
2. Beta-oxidation: The breakdown of fatty acids occurs in the mitochondria through a process called beta-oxidation, where Acyl-CoA is sequentially broken down into smaller units, releasing acetyl-CoA, which then enters the citric acid cycle.
3. Ketogenesis: In times of low carbohydrate availability or during prolonged fasting, the liver can produce ketone bodies from acetyl-CoA to supply energy to other organs, such as the brain and heart.
4. Protein synthesis: Acyl-CoA is also involved in the modification of proteins by attaching fatty acid chains to them (a process called acetylation), which can influence protein function and stability.

In summary, Acyl Coenzyme A is a vital molecule in metabolism that connects various pathways related to energy production, fatty acid breakdown, and protein modification.

I'm sorry for any confusion, but 'Tungsten' is not a medical term. It is a chemical element with the symbol W and atomic number 74. Tungsten is a rare metal found naturally on Earth, and it has many industrial uses due to its hardness, high density, and high melting point.

In the context of medicine or healthcare, tungsten may be encountered in certain medical devices, such as X-ray tubes and electrodes, where its properties are utilized for their durability and heat resistance. However, it is not a term that would typically have a formal medical definition.

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.

Crotonates are a group of organic compounds that contain a carboxylic acid functional group (-COOH) attached to a crotyl group, which is a type of alkyl group with the structure -CH=CH-CH\_{2}-. Crotyl groups are derived from crotonic acid or its derivatives.

Crotonates can be found in various natural and synthetic compounds, including some pharmaceuticals, agrochemicals, and other industrial chemicals. They can exist as salts, esters, or other derivatives of crotonic acid.

In medical contexts, crotonates may refer to certain medications or chemical compounds used for research purposes. For example, sodium crotylate is a salt of crotonic acid that has been studied for its potential anti-inflammatory and analgesic effects. However, it is not widely used in clinical practice.

It's worth noting that the term "crotonates" may not have a specific medical definition on its own, as it refers to a broad class of compounds with varying properties and uses.

Aconitate hydratase is an enzyme that catalyzes the reversible conversion of citrate to isocitrate in the Krebs cycle (also known as the tricarboxylic acid cycle or TCA cycle), which is a central metabolic pathway in the cell. This enzyme is also called aconitase or aconitate dehydratase.

The reaction catalyzed by aconitate hydratase involves two steps: first, the removal of a water molecule from citrate to form cis-aconitate; and second, the addition of a water molecule to cis-aconitate to form isocitrate. The enzyme binds to the substrate in such a way that it stabilizes the transition state between citrate and cis-aconitate, making the reaction more favorable.

Aconitate hydratase plays an important role in energy metabolism, as it helps generate NADH and FADH2, which are used to produce ATP through oxidative phosphorylation. Additionally, aconitate hydratase has been implicated in various diseases, including neurodegenerative disorders, cancer, and bacterial infections.

Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.

Acrylonitrile is a colorless, flammable liquid with an unpleasant odor. It is used in the manufacture of plastics, resins, and synthetic fibers. In terms of medical toxicology, acrylonitrile is classified as a volatile organic compound (VOC) and can cause irritation to the eyes, skin, and respiratory tract. Exposure to high levels of acrylonitrile can lead to symptoms such as headache, dizziness, nausea, and vomiting. Chronic exposure has been associated with an increased risk of certain types of cancer, including lung, laryngeal, and esophageal cancer. However, it's important to note that occupational exposure limits are in place to minimize the risks associated with acrylonitrile exposure.

"Thauera" is a genus of bacteria that belongs to the family of Comamonadaceae. These bacteria are commonly found in various environments such as soil, water, and wastewater treatment systems. They have the ability to degrade various organic compounds, including aromatic hydrocarbons and ammonia, making them important players in bioremediation processes.

The name "Thauera" is derived from the Greek word "thauema," which means "wonder" or "marvel." This name reflects the remarkable abilities of these bacteria to break down complex organic compounds.

It's worth noting that "Thauera" is a taxonomic category, and individual species within this genus may have additional characteristics or properties that are not shared by all members of the group.

Epoxide hydrolases are a group of enzymes that catalyze the hydrolysis of epoxides, which are molecules containing a three-membered ring consisting of two carbon atoms and one oxygen atom. This reaction results in the formation of diols, which are molecules containing two hydroxyl groups (-OH).

Epoxide hydrolases play an important role in the detoxification of xenobiotics (foreign substances) and the metabolism of endogenous compounds. They help to convert toxic epoxides into less harmful products, which can then be excreted from the body.

There are two main types of epoxide hydrolases: microsomal epoxide hydrolase (mEH) and soluble epoxide hydrolase (sEH). mEH is primarily responsible for metabolizing xenobiotics, while sEH plays a role in the metabolism of endogenous compounds such as arachidonic acid.

Impaired function or inhibition of epoxide hydrolases has been linked to various diseases, including cancer, cardiovascular disease, and neurological disorders. Therefore, these enzymes are considered important targets for the development of drugs and therapies aimed at treating these conditions.

Polyhydroxyalkanoates (PHAs) are naturally occurring, biodegradable polyesters accumulated by some bacteria as intracellular granules under conditions of limiting nutrients, typically carbon source excess and nutrient deficiency. They serve as a form of energy reserve and can be produced from renewable resources such as sugars, lipids, or organic acids. PHAs have potential applications in various fields including packaging, agriculture, pharmaceuticals, and medicine due to their biodegradability and biocompatibility.

Hereditary neoplastic syndromes refer to genetic disorders that predispose affected individuals to develop tumors or cancers. These syndromes are caused by inherited mutations in specific genes that regulate cell growth and division. As a result, cells may divide and grow uncontrollably, leading to the formation of benign or malignant tumors.

Examples of hereditary neoplastic syndromes include:

1. Hereditary breast and ovarian cancer syndrome (HBOC): This syndrome is caused by mutations in the BRCA1 or BRCA2 genes, which increase the risk of developing breast, ovarian, and other cancers.
2. Lynch syndrome: Also known as hereditary non-polyposis colorectal cancer (HNPCC), this syndrome is caused by mutations in DNA mismatch repair genes, leading to an increased risk of colon, endometrial, and other cancers.
3. Li-Fraumeni syndrome: This syndrome is caused by mutations in the TP53 gene, which increases the risk of developing a wide range of cancers, including breast, brain, and soft tissue sarcomas.
4. Familial adenomatous polyposis (FAP): This syndrome is caused by mutations in the APC gene, leading to the development of numerous colon polyps that can become cancerous if not removed.
5. Neurofibromatosis type 1 (NF1): This syndrome is caused by mutations in the NF1 gene and is characterized by the development of benign tumors called neurofibromas on the nerves and skin.
6. Von Hippel-Lindau disease (VHL): This syndrome is caused by mutations in the VHL gene, leading to an increased risk of developing various types of tumors, including kidney, pancreas, and adrenal gland tumors.

Individuals with hereditary neoplastic syndromes often have a higher risk of developing cancer than the general population, and they may require more frequent screening and surveillance to detect cancers at an early stage when they are more treatable.

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

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.

Brevibacterium is a genus of Gram-positive, rod-shaped bacteria that are commonly found in nature, particularly in soil, water, and various types of decaying organic matter. Some species of Brevibacterium can also be found on the skin of animals and humans, where they play a role in the production of body odor.

Brevibacterium species are known for their ability to produce a variety of enzymes that allow them to break down complex organic compounds into simpler molecules. This makes them useful in a number of industrial applications, such as the production of cheese and other fermented foods, as well as in the bioremediation of contaminated environments.

In medical contexts, Brevibacterium species are rarely associated with human disease. However, there have been occasional reports of infections caused by these bacteria, particularly in individuals with weakened immune systems or who have undergone surgical procedures. These infections can include bacteremia (bloodstream infections), endocarditis (inflammation of the heart valves), and soft tissue infections. Treatment typically involves the use of antibiotics that are effective against Gram-positive bacteria, such as vancomycin or teicoplanin.

Carbonic anhydrase I is a specific type of carbonic anhydrase, which is an enzyme that catalyzes the reversible reaction between carbon dioxide and water to form carbonic acid. This enzyme is primarily found in red blood cells and plays a crucial role in maintaining pH balance and regulating respiration.

Carbonic anhydrase I, also known as CA I or CA-I, is responsible for hydrating carbon dioxide to form bicarbonate ions and protons, which helps maintain the acid-base balance in the body. It has a relatively slower reaction rate compared to other carbonic anhydrase isoforms.

Defects or mutations in the CA I gene can lead to reduced enzymatic activity and may contribute to certain medical conditions, such as distal renal tubular acidosis (dRTA), a disorder characterized by impaired kidney function and acid-base imbalances. However, other carbonic anhydrase isoforms can compensate for the loss of CA I activity in most cases, so its deficiency rarely causes severe symptoms on its own.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Aconitic acid is a type of organic acid that is found naturally in some plants, including Aconitum napellus (monkshood or wolf's bane). It is a white crystalline powder with a sour taste and is soluble in water. In the human body, aconitic acid is produced as a byproduct of energy metabolism and can be found in small amounts in various tissues.

Aconitic acid has three carboxylic acid groups, making it a triprotic acid, which means that it can donate three protons (hydrogen ions) in solution. It is a strong acid and is often used as a laboratory reagent for various chemical reactions. In the food industry, aconitic acid may be used as a food additive or preservative.

It's important to note that some species of Aconitum plants contain highly toxic compounds called aconitines, which can cause serious harm or even death if ingested. Therefore, these plants should not be consumed or handled without proper knowledge and precautions.

I believe there may be a slight spelling error in your question. If you are referring to "isocitrate," I can provide a medical definition for that. Isocitrate is a chemical compound that is naturally found in the body and plays a crucial role in energy production within cells. It is a key intermediate in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, which is a series of chemical reactions used by all living cells to generate energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins into adenosine triphosphate (ATP).

Isocitrate is an important molecule in this cycle as it undergoes oxidative decarboxylation, catalyzed by the enzyme isocitrate dehydrogenase, to form alpha-ketoglutarate. This reaction also produces nicotinamide adenine dinucleotide (NADH), which serves as an essential electron carrier in the generation of ATP during oxidative phosphorylation.

If you meant something else or need more information, please let me know, and I will be happy to help.

Deltaproteobacteria is a class of proteobacteria, which are a group of gram-negative bacteria. Deltaproteobacteria are characterized by their unique arrangement of flagella and their ability to perform anaerobic respiration, which means they can grow without oxygen. They play important roles in various environments such as soil, freshwater, and marine ecosystems, where they are involved in processes like sulfur cycling and denitrification. Some members of this class are also known to cause diseases in humans, such as the genera Myxococcus, Bdellovibrio, and Desulfovibrio.

Peroxisomes are membrane-bound subcellular organelles found in the cytoplasm of eukaryotic cells. They play a crucial role in various cellular processes, including the breakdown of fatty acids and the detoxification of harmful substances such as hydrogen peroxide (H2O2). Peroxisomes contain numerous enzymes, including catalase, which converts H2O2 into water and oxygen, thus preventing oxidative damage to cellular components. They also participate in the biosynthesis of ether phospholipids, a type of lipid essential for the structure and function of cell membranes. Additionally, peroxisomes are involved in the metabolism of reactive oxygen species (ROS) and contribute to the regulation of intracellular redox homeostasis. Dysfunction or impairment of peroxisome function has been linked to several diseases, including neurological disorders, developmental abnormalities, and metabolic conditions.

Fibric acids, also known as fibric acid derivatives, are a class of medications that are primarily used to lower elevated levels of triglycerides (a type of fat) in the blood. They work by increasing the breakdown and removal of triglycerides from the bloodstream, and reducing the production of very-low-density lipoprotein (VLDL), a type of particle that carries triglycerides in the blood.

Examples of fibric acids include gemfibrozil, fenofibrate, and clofibrate. These medications are often prescribed for people with high triglyceride levels who are at risk for pancreatitis (inflammation of the pancreas) or other complications related to high triglycerides.

Fibric acids may also have a modest effect on raising levels of high-density lipoprotein (HDL), or "good" cholesterol, and lowering levels of low-density lipoprotein (LDL), or "bad" cholesterol, in some people. However, they are generally not as effective at lowering LDL cholesterol as statins, another class of cholesterol-lowering medications.

It's important to note that fibric acids can interact with other medications and may cause side effects such as stomach upset, muscle pain, and an increased risk of gallstones. As with any medication, it's important to use fibric acids under the guidance of a healthcare provider.

Vanillic Acid is not a medical term, but it is a chemical compound with the name 4-hydroxy-3-methoxybenzoic acid. It is a type of phenolic acid that occurs naturally in some foods and plants, including vanilla beans, pineapples, and certain types of mushrooms.

Vanillic Acid has been studied for its potential antioxidant, anti-inflammatory, and neuroprotective properties. However, it is not considered a medication or a medical treatment and does not have a specific medical definition.

Fumarates are the salts or esters of fumaric acid, a naturally occurring organic compound with the formula HO2C-CH=CH-CO2H. In the context of medical therapy, fumarates are used as medications for the treatment of psoriasis and multiple sclerosis.

One such medication is dimethyl fumarate (DMF), which is a stable salt of fumaric acid. DMF has anti-inflammatory and immunomodulatory properties, and it's used to treat relapsing forms of multiple sclerosis (MS) and moderate-to-severe plaque psoriasis.

The exact mechanism of action of fumarates in these conditions is not fully understood, but they are thought to modulate the immune system and have antioxidant effects. Common side effects of fumarate therapy include gastrointestinal symptoms such as diarrhea, nausea, and abdominal pain, as well as flushing and skin reactions.

Cobalt is a chemical element with the symbol Co and atomic number 27. It is a hard, silver-white, lustrous, and brittle metal that is found naturally only in chemically combined form, except for small amounts found in meteorites. Cobalt is used primarily in the production of magnetic, wear-resistant, and high-strength alloys, as well as in the manufacture of batteries, magnets, and pigments.

In a medical context, cobalt is sometimes used in the form of cobalt-60, a radioactive isotope, for cancer treatment through radiation therapy. Cobalt-60 emits gamma rays that can be directed at tumors to destroy cancer cells. Additionally, small amounts of cobalt are present in some vitamin B12 supplements and fortified foods, as cobalt is an essential component of vitamin B12. However, exposure to high levels of cobalt can be harmful and may cause health effects such as allergic reactions, lung damage, heart problems, and neurological issues.

Acyl-CoA oxidase is an enzyme that plays a crucial role in the breakdown of fatty acids within the body. It is located in the peroxisomes, which are small organelles found in the cells of living organisms. The primary function of acyl-CoA oxidase is to catalyze the initial step in the beta-oxidation of fatty acids, a process that involves the sequential removal of two-carbon units from fatty acid molecules in the form of acetyl-CoA.

The reaction catalyzed by acyl-CoA oxidase is as follows:

acyl-CoA + FAD → trans-2,3-dehydroacyl-CoA + FADH2 + H+

In this reaction, the enzyme removes a hydrogen atom from the fatty acyl-CoA molecule and transfers it to its cofactor, flavin adenine dinucleotide (FAD). This results in the formation of trans-2,3-dehydroacyl-CoA, FADH2, and a proton. The FADH2 produced during this reaction can then be used to generate ATP through the electron transport chain, while the trans-2,3-dehydroacyl-CoA undergoes further reactions in the beta-oxidation pathway.

There are two main isoforms of acyl-CoA oxidase found in humans: ACOX1 and ACOX2. ACOX1 is primarily responsible for oxidizing straight-chain fatty acids, while ACOX2 specializes in the breakdown of branched-chain fatty acids. Mutations in the genes encoding these enzymes can lead to various metabolic disorders, such as peroxisomal biogenesis disorders and Refsum disease.

The Mitochondrial Trifunctional Protein (MTP) is a complex located within the inner mitochondrial membrane and is responsible for the last three steps in the beta-oxidation of long-chain fatty acids. The alpha subunit, also known as HADHA (Hydroxyacyl-CoA Dehydrogenase/3-Ketoacyl-CoA Thiolase/Enoyl-CoA Hydratase), is a key component of this complex. It has three enzymatic activities:

1. Long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD): This enzyme catalyzes the oxidation of L-3-hydroxyacyl-CoAs to 3-ketoacyl-CoAs, using electron transfer flavoprotein (ETF) as an electron acceptor.
2. Long-chain enoyl-CoA hydratase: This enzyme catalyzes the hydration of trans-2-enoyl-CoAs to L-3-hydroxyacyl-CoAs in the beta-oxidation cycle.
3. 3-ketoacyl-CoA thiolase (KAT): This enzyme catalyzes the final step of beta-oxidation, cleaving 3-ketoacyl-CoAs into acetyl-CoA and a new CoA thioester that is two carbons shorter than the original fatty acid.

Mutations in the HADHA gene can lead to various severe mitochondrial disorders, such as long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHADD) and mitochondrial trifunctional protein deficiency (MTPD). These genetic defects impair the ability of the cell to oxidize long-chain fatty acids, resulting in metabolic crisis, especially under conditions of increased energy demand or during fasting. Symptoms can include hypoketotic hypoglycemia, muscle weakness, cardiomyopathy, and neurological impairment.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Coenzyme A, often abbreviated as CoA or sometimes holo-CoA, is a coenzyme that plays a crucial role in several important chemical reactions in the body, particularly in the metabolism of carbohydrates, fatty acids, and amino acids. It is composed of a pantothenic acid (vitamin B5) derivative called pantothenate, an adenosine diphosphate (ADP) molecule, and a terminal phosphate group.

Coenzyme A functions as a carrier molecule for acetyl groups, which are formed during the breakdown of carbohydrates, fatty acids, and some amino acids. The acetyl group is attached to the sulfur atom in CoA, forming acetyl-CoA, which can then be used as a building block for various biochemical pathways, such as the citric acid cycle (Krebs cycle) and fatty acid synthesis.

In summary, Coenzyme A is a vital coenzyme that helps facilitate essential metabolic processes by carrying and transferring acetyl groups in the body.

"Pseudomonas putida" is a species of gram-negative, rod-shaped bacteria that is commonly found in soil and water environments. It is a non-pathogenic, opportunistic microorganism that is known for its versatile metabolism and ability to degrade various organic compounds. This bacterium has been widely studied for its potential applications in bioremediation and industrial biotechnology due to its ability to break down pollutants such as toluene, xylene, and other aromatic hydrocarbons. It is also known for its resistance to heavy metals and antibiotics, making it a valuable tool in the study of bacterial survival mechanisms and potential applications in bioremediation and waste treatment.

Organoids are 3D tissue cultures grown from stem cells that mimic the structure and function of specific organs. They are used in research to study development, disease, and potential treatments. The term "organoid" refers to the fact that these cultures can organize themselves into structures that resemble rudimentary organs, with differentiated cell types arranged in a pattern similar to their counterparts in the body. Organoids can be derived from various sources, including embryonic stem cells, induced pluripotent stem cells (iPSCs), or adult stem cells, and they provide a valuable tool for studying complex biological processes in a controlled laboratory setting.

Uterine neoplasms refer to abnormal growths in the uterus, which can be benign (non-cancerous) or malignant (cancerous). These growths can originate from different types of cells within the uterus, leading to various types of uterine neoplasms. The two main categories of uterine neoplasms are endometrial neoplasms and uterine sarcomas.

Endometrial neoplasms develop from the endometrium, which is the inner lining of the uterus. Most endometrial neoplasms are classified as endometrioid adenocarcinomas, arising from glandular cells in the endometrium. Other types include serous carcinoma, clear cell carcinoma, and mucinous carcinoma.

Uterine sarcomas, on the other hand, are less common and originate from the connective tissue (stroma) or muscle (myometrium) of the uterus. Uterine sarcomas can be further divided into several subtypes, such as leiomyosarcoma, endometrial stromal sarcoma, and undifferentiated uterine sarcoma.

Uterine neoplasms can cause various symptoms, including abnormal vaginal bleeding or discharge, pelvic pain, and difficulty urinating or having bowel movements. The diagnosis typically involves a combination of imaging tests (such as ultrasound, CT, or MRI scans) and tissue biopsies to determine the type and extent of the neoplasm. Treatment options depend on the type, stage, and patient's overall health but may include surgery, radiation therapy, chemotherapy, or hormone therapy.

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.

"Pseudomonas" is a genus of Gram-negative, rod-shaped bacteria that are widely found in soil, water, and plants. Some species of Pseudomonas can cause disease in animals and humans, with P. aeruginosa being the most clinically relevant as it's an opportunistic pathogen capable of causing various types of infections, particularly in individuals with weakened immune systems.

P. aeruginosa is known for its remarkable ability to resist many antibiotics and disinfectants, making infections caused by this bacterium difficult to treat. It can cause a range of healthcare-associated infections, such as pneumonia, bloodstream infections, urinary tract infections, and surgical site infections. In addition, it can also cause external ear infections and eye infections.

Prompt identification and appropriate antimicrobial therapy are crucial for managing Pseudomonas infections, although the increasing antibiotic resistance poses a significant challenge in treatment.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Cyanamide is a chemical compound with the formula NH2CN. It is a colorless, crystalline solid that is highly soluble in water and has an ammonia-like odor. Cyanamide is used as a reagent in organic synthesis and as a fertilizer.

In a medical context, cyanamide may be used as a drug to treat certain conditions. For example, it has been used as a muscle relaxant and to reduce muscle spasms in people with multiple sclerosis. It is also being studied as a potential treatment for alcohol dependence, as it may help to reduce cravings and withdrawal symptoms.

It is important to note that cyanamide can be toxic in high doses, and it should only be used under the supervision of a healthcare professional.

'Candida tropicalis' is a species of yeast that can be found normally in certain environments, including the human body (such as the skin, mouth, and digestive system). However, it can also cause infections in people with weakened immune systems or underlying medical conditions. These infections can occur in various parts of the body, including the bloodstream, urinary tract, and skin.

Like other Candida species, C. tropicalis is a type of fungus that reproduces by budding, forming oval-shaped cells. It is often resistant to certain antifungal medications, which can make infections more difficult to treat. Proper diagnosis and treatment, usually with antifungal drugs, are essential for managing C. tropicalis infections.

Fatty acids are carboxylic acids with a long aliphatic chain, which are important components of lipids and are widely distributed in living organisms. They can be classified based on the length of their carbon chain, saturation level (presence or absence of double bonds), and other structural features.

The two main types of fatty acids are:

1. Saturated fatty acids: These have no double bonds in their carbon chain and are typically solid at room temperature. Examples include palmitic acid (C16:0) and stearic acid (C18:0).
2. Unsaturated fatty acids: These contain one or more double bonds in their carbon chain and can be further classified into monounsaturated (one double bond) and polyunsaturated (two or more double bonds) fatty acids. Examples of unsaturated fatty acids include oleic acid (C18:1, monounsaturated), linoleic acid (C18:2, polyunsaturated), and alpha-linolenic acid (C18:3, polyunsaturated).

Fatty acids play crucial roles in various biological processes, such as energy storage, membrane structure, and cell signaling. Some essential fatty acids cannot be synthesized by the human body and must be obtained through dietary sources.

Clofibric acid is the main metabolic product of clofibrate, a medication that belongs to the class of drugs called fibrates. It works by lowering levels of total and LDL (low-density lipoprotein) cholesterol and triglycerides in the blood, while increasing HDL (high-density lipoprotein) cholesterol levels. Clofibric acid is an antihyperlipidemic agent that is used primarily for the treatment of hypertriglyceridemia and mixed dyslipidemia. It may also be used to prevent pancreatitis caused by high triglyceride levels.

Clofibric acid is detectable in the urine and can be used as a biomarker for clofibrate exposure or use. However, it's important to note that clofibrate has largely been replaced by newer fibrates and statins due to its adverse effects profile and lower efficacy compared to these newer agents.

Urocanate hydratase is an enzyme that is involved in the metabolism of the amino acid histidine. The gene for this enzyme is located on chromosome 7q31-q32. Urocanate hydratase catalyzes the conversion of urocanate to imidazoleacetic acid, which is an important step in the degradation of histidine. Defects in this enzyme can lead to a rare genetic disorder called histidinemia, which is characterized by elevated levels of histidine and its metabolites in the blood and urine. However, it's important to note that histidinemia is generally considered a benign condition, and affected individuals usually do not experience any symptoms or complications.

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.

Iron carbonyl compounds are a group of chemical compounds that contain iron and carbon monoxide (CO) molecules. The most common iron carbonyl compound is Iron pentacarbonyl (Fe(CO)5), which is a colorless liquid with a faint, sweet odor. It is used as a reducing agent and a catalyst in various chemical reactions. Other iron carbonyl compounds include diiron decacarbonyl (Fe2(CO)10), triiron dodecacarbonyl (Fe3(CO)12), and tetracarbonylferrate(II) ion [Fe(CO)4]2-. These compounds are typically prepared by the direct reaction of iron with carbon monoxide under high pressure. They are sensitive to oxygen, moisture, and light, and must be handled carefully to prevent degradation.

Peroxisomal disorders are a group of inherited metabolic diseases caused by defects in the function or structure of peroxisomes, which are specialized subcellular organelles found in the cells of animals, plants, and humans. These disorders can affect various aspects of metabolism, including fatty acid oxidation, bile acid synthesis, and plasma cholesterol levels.

Peroxisomal disorders can be classified into two main categories: single peroxisomal enzyme deficiencies and peroxisome biogenesis disorders (PBDs). Single peroxisomal enzyme deficiencies are characterized by a defect in a specific enzyme found within the peroxisome, while PBDs are caused by problems with the formation or assembly of the peroxisome itself.

Examples of single peroxisomal enzyme deficiencies include X-linked adrenoleukodystrophy (X-ALD), Refsum disease, and acyl-CoA oxidase deficiency. PBDs include Zellweger spectrum disorders, such as Zellweger syndrome, neonatal adrenoleukodystrophy, and infantile Refsum disease.

Symptoms of peroxisomal disorders can vary widely depending on the specific disorder and the severity of the enzyme or biogenesis defect. They may include neurological problems, vision and hearing loss, developmental delays, liver dysfunction, and skeletal abnormalities. Treatment typically focuses on managing symptoms and addressing any underlying metabolic imbalances.

Citrates are the salts or esters of citric acid, a weak organic acid that is naturally found in many fruits and vegetables. In a medical context, citrates are often used as a buffering agent in intravenous fluids to help maintain the pH balance of blood and other bodily fluids. They are also used in various medical tests and treatments, such as in urine alkalinization and as an anticoagulant in kidney dialysis solutions. Additionally, citrate is a component of some dietary supplements and medications.

Benzaldehyde is an organic compound with the formula C6H5CHO. It is the simplest aromatic aldehyde, and it consists of a benzene ring attached to a formyl group. Benzaldehyde is a colorless liquid with a characteristic almond-like odor.

Benzaldehyde occurs naturally in various plants, including bitter almonds, cherries, peaches, and apricots. It is used in many industrial applications, such as in the production of perfumes, flavorings, and dyes. In addition, benzaldehyde has been used in medical research for its potential therapeutic effects, such as its anti-inflammatory and antimicrobial properties.

However, it is important to note that benzaldehyde can be toxic in high concentrations and may cause irritation to the skin, eyes, and respiratory system. Therefore, it should be handled with care and used in accordance with appropriate safety guidelines.

Gamma-enolase is a phosphopyruvate hydratase. Gamma-enolase is one of the three enolase isoenzymes found in mammals. This ...
Phosphopyruvate hydratase, usually known as enolase, is a metalloenzyme (EC 4.2.1.11) that catalyses the conversion of 2- ... H2O Phosphopyruvate hydratase belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds ...
... phosphopyruvate hydratase, RNA-associated protein, threonine synthase, aspartate aminotransferase, precorrin-8x methylmutase, ...
Phosphopyruvate hydratase (enolase) H2O H2O 2 × Phosphoenolpyruvate 2 × Pyruvate kinase ADP ATP 2 × Pyruvate 2 × The first five ...
... enoyl-coa hydratase MeSH D08.811.520.241.300.300 - fumarate hydratase MeSH D08.811.520.241.300.500 - phosphopyruvate hydratase ... aconitate hydratase MeSH D08.811.520.241.300.050.500 - iron regulatory protein 1 MeSH D08.811.520.241.300.050.750 - iron ... urocanate hydratase MeSH D08.811.520.241.300.950 - uroporphyrinogen iii synthetase MeSH D08.811.520.241.700 - polysaccharide- ...
... phosphopyruvate hydratase (enolase) EC 4.2.1.12: phosphogluconate dehydratase EC 4.2.1.13: Now EC 4.3.1.17, L-serine ammonia- ... 2-hydratase EC 4.2.1.132: 2-hydroxyhexa-2,4-dienoate hydratase EC 4.2.1.133: copal-8-ol diphosphate hydratase EC 4.2.1.134: ... 4-oxalmesaconate hydratase EC 4.2.1.84: nitrile hydratase EC 4.2.1.85: dimethylmaleate hydratase EC 4.2.1.86: identical to EC ... 2-methylfumaryl-CoA hydratase * EC 4.2.1.149: crotonobetainyl-CoA hydratase * EC 4.2.1.150: short-chain-enoyl-CoA hydratase * ...
Gamma-enolase is a phosphopyruvate hydratase. Gamma-enolase is one of the three enolase isoenzymes found in mammals. This ...
Phosphopyruvate hydratase. Insoluble. +. ND. Burkholderia pseudomallei. ABA48070.1. Bp 90-510. Sensor histidine kinase. ...
Phosphopyruvate Hydratase / analysis * Phosphopyruvate Hydratase / metabolism * Post-Concussion Syndrome / metabolism* * S100 ...
... and phosphopyruvate hydratase (PPH), were overrepresented in the transcriptome of L. dendroidea 24 h and 48 h after the ... phosphopyruvate hydratase, PPH. (g) Products of genes involved in tricarboxylic acid cycle and oxidative phosphorylation are ... enoyl-CoA hydratase, ECH; 3-ketoacyl-CoA thiolase, 3KCT; isovaleryl-CoA dehydrogenase, IVD; 3-hydroxyisobutyryl-CoA hydrolase, ... such as those coding for enoyl-CoA hydratase (ECH), 3-ketoacyl-CoA thiolase (3KCT), isovaleryl-CoA dehydrogenase (IVD), 3- ...
Phosphopyruvate Hydratase (Enolase) 10. Copper Related Therapies and Procedures. 1. Denervation CureHunter Inc. provides ...
Phosphopyruvate hydratase; Plasminogen-binding protein; 2-phospho-D-glycerate hydro-lyase; C-myc promoter-binding , Products ... NNE; ENO1L1; MPB1; PPH; Alpha Enolase; Enolase 1; Phosphopyruvate hydratase; Plasminogen-binding protein; 2-phospho-D-glycerate ...
Phosphopyruvate Hydratase/metabolism. MESH. Sequence Homology, Amino Acid. MESH. Structure-Activity Relationship. MESH. ...
phosphopyruvate hydratase activity of enolase dimer [cytosol] Physical Entity enolase dimer [cytosol] (Canis familiaris) ...
Phosphopyruvate Hydratase 13% * Interleukin-17 12% * Mycoses 11% * Electrophoresis 11% * Polysaccharides 11% ...
Phosphopyruvate Hydratase Medicine & Life Sciences 98% * Fluorides Medicine & Life Sciences 91% * Growth Medicine & Life ...
Phosphopyruvate Hydratase Medicine & Life Sciences 29% * Giant Cells Medicine & Life Sciences 26% ...
Phosphopyruvate Hydratase Medicine & Life Sciences 94% * Epithelium Medicine & Life Sciences 61% * Connexin 43 Medicine & Life ...
phosphopyruvate hydratase activity GO:0004634 Molecular Function 0.0. - Sma3. copper ion binding GO:0005507 Molecular Function ...
phosphopyruvate hydratase YP_001280554 unclonable 0.000000000737356 normal 1 Psychrobacter sp. PRwf-1 Bacteria -. ... enoyl-CoA hydratase YP_001279293 hitchhiker 0.0000000165934 unclonable 0.000000000539782 Psychrobacter sp. PRwf-1 Bacteria -. ...
phosphopyruvate hydratase activity GO:0004634 Molecular Function 0.0. - Sma3. copper ion binding GO:0005507 Molecular Function ...
ec 4.2.1.11: Phosphopyruvate hydratase. pdb deposition date 2015-03-26. pfam database annotations. chain. Pfam Accession Code. ...
Cheng, C. K., Lin, X., Pu, Y., Tse, J. K. Y., Wang, Y., Zhang, C. L., Cao, X., Lau, C. W., Huang, J., He, L., Luo, J. Y., Shih, Y. T., Wan, S., Ng, C. F., Wang, L., Ma, R. C. W., Chiu, J. J., Chan, T. F., Yu Tian, X. & Huang, Y., Jan 2023, In: Journal of Advanced Research. 43, p. 187-203 17 p.. Research output: Contribution to journal › Article › peer-review ...
Lucarini, E., Coppi, E., Micheli, L., Parisio, C., Vona, A., Cherchi, F., Pugliese, A. M., Pedata, F., Failli, P., Palomino, S., Wahl, J., Largent-Milnes, T. M., Vanderah, T. W., Tosh, D. K., Jacobson, K. A., Salvemini, D., Ghelardini, C. & Di Cesare Mannelli, L., Sep 2020, In: Pain. 161, 9, p. 2179-2190 12 p.. Research output: Contribution to journal › Article › peer-review ...
E Equus caballus , phosphopyruvate hydratase [ENO3] Groups For related groups, use main isoform HORSE03367 ...
phosphopyruvate hydratase complex. GO:0005964 phosphorylase kinase complex. GO:1990265 platelet-derived growth factor complex. ...
Phosphopyruvate Hydratase 77% * Sugar Acids 68% * mandelate racemase 47% * Protons 44% * 4-hydroxy-tetrahydrodipicolinate ...
ACLY, ATP citrate synthase; ENO, phosphopyruvate hydratase; FBA, fructose-bisphosphate aldolase; G6PDH, glucose-6-phosphate ...
phosphopyruvate hydratase complex GO:0000015 * taurine dioxygenase complex GO:1990205 * SMAD protein complex ...
phosphopyruvate hydratase 88% 4 Citas (Scopus) * A novel enolase from Taenia solium metacestodes and its evaluation as an ...
Phosphopyruvate Hydratase Medicine & Life Sciences 41% View full fingerprint Collaborations and top research areas from the ...
phosphopyruvate hydratase complex. GO:0005964 phosphorylase kinase complex. GO:1990265 platelet-derived growth factor complex. ...
Phosphopyruvate Hydratase / chemistry; Proteomics / instrumentation; Serum Albumin, Bovine / chemistry ...
4.2.1.11 - Phosphopyruvate hydratase (enolase). 2.7.1.40 - Pyruvate kinase. 1.1.1.27 - Lactate dehydrogenase ...
phosphopyruvate hydratase [4] (data from MRSA252). SAOUHSC_01246. (infB). translation initiation factor IF-2 [4] (data from ...
  • Fumarate Hydratase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
  • Identification of fumarate hydratase inhibitors with nutrient-dependent cytotoxicity. (uchicago.edu)
  • Up-regulated proteins, including phosphoglycerate mutase and phosphopyruvate hydratase, as well as down-regulated proteins such as glyceraldehyde-3-phosphate dehydrogenase and fructose-bisphosphate aldolase, not only directly or indirectly affected a variety of metabolic processes, but were specifically closely related to glycolysis and glycometabolism. (scielo.br)
  • mitochondrion distribution # child [Term] id: GO:0000015 # parent name: phosphopyruvate hydratase complex namespace: cellular_component def: 'A multimeric enzyme complex, usually a dimer or an octamer, that catalyzes the conversion of 2-phospho-D-glycerate to phosphoenolpyruvate and water. (stackexchange.com)
  • They are inactivated form of PHOSPHOPYRUVATE HYDRATASE . (nih.gov)