Oxidoreductases
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Aldehyde Dehydrogenase
Protein Disulfide Reductase (Glutathione)
Alcohol Oxidoreductases
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
Pyruvate Synthase
NADH, NADPH Oxidoreductases
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
Glutaredoxins
A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.
Oxidation-Reduction
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).
Protein Disulfide-Isomerases
Aldehyde Reductase
Oxidoreductases Acting on Sulfur Group Donors
Thioredoxins
Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.
Oxidoreductases Acting on Aldehyde or Oxo Group Donors
Amino Acid Sequence
Molecular Sequence Data
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.
Quinone Reductases
NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
Electron Transport Complex II
Wolinella
NAD
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
Catalysis
NADP
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
Thioredoxin-Disulfide Reductase
Disulfides
Substrate Specificity
Succinate Dehydrogenase
Coenzymes
Acetaldehyde
Oxidoreductases Acting on CH-CH Group Donors
Electron Transport
Glucose Oxidase
An enzyme of the oxidoreductase class that catalyzes the conversion of beta-D-glucose and oxygen to D-glucono-1,5-lactone and peroxide. It is a flavoprotein, highly specific for beta-D-glucose. The enzyme is produced by Penicillium notatum and other fungi and has antibacterial activity in the presence of glucose and oxygen. It is used to estimate glucose concentration in blood or urine samples through the formation of colored dyes by the hydrogen peroxide produced in the reaction. (From Enzyme Nomenclature, 1992) EC 1.1.3.4.
Sequence Homology, Amino Acid
Pleurotus
A genus of basidiomycetous fungi, family POLYPORACEAE, order POLYPORALES, that grows on logs or tree stumps in shelflike layers. The species P. ostreatus, the oyster mushroom, is a choice edible species and is the most frequently encountered member of the genus in eastern North America. (Alexopoulos et al., Introductory Mycology, 4th ed, p531)
NAD(P)H Dehydrogenase (Quinone)
Ferredoxin-NADP Reductase
Flavin-Adenine Dinucleotide
Electron Transport Complex I
A flavoprotein and iron sulfur-containing oxidoreductase complex that catalyzes the conversion of UBIQUINONE to ubiquinol. In MITOCHONDRIA the complex also couples its reaction to the transport of PROTONS across the internal mitochondrial membrane. The NADH DEHYDROGENASE component of the complex can be isolated and is listed as EC 1.6.99.3.
15-Oxoprostaglandin 13-Reductase
Escherichia coli
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Flavins
Stereoisomerism
Alcohol Dehydrogenase
Sequence Alignment
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Iron-Sulfur Proteins
Disulfiram
A carbamate derivative used as an alcohol deterrent. It is a relatively nontoxic substance when administered alone, but markedly alters the intermediary metabolism of alcohol. When alcohol is ingested after administration of disulfiram, blood acetaldehyde concentrations are increased, followed by flushing, systemic vasodilation, respiratory difficulties, nausea, hypotension, and other symptoms (acetaldehyde syndrome). It acts by inhibiting aldehyde dehydrogenase.
Oxidoreductases Acting on CH-NH2 Group Donors
Prokaryotic Cells
Xanthine Dehydrogenase
Protochlorophyllide
Binding Sites
Models, Molecular
Multienzyme Complexes
Electrons
Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.
Retinal Dehydrogenase
Alcohols
FMN Reductase
Molecular Structure
Periplasm
Glucose 1-Dehydrogenase
Isomerases
PQQ Cofactor
Flavodoxin
Rhodobacter capsulatus
Sugar Alcohol Dehydrogenases
Hydroxysteroid Dehydrogenases
Glutathione Reductase
Cloning, Molecular
Cyanamide
Base Sequence
Models, Chemical
Mutation
Hydrogen-Ion Concentration
Archaea
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
Oxidoreductases, O-Demethylating
Glutathione
Catalytic Domain
Succinic Acid
A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)
Multigene Family
A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)
Ferredoxins
Enzyme Stability
Protein Conformation
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Anaerobiosis
Malate Dehydrogenase
Metalloproteins
Mass Spectrometry
Selenocysteine
Bacteria
One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.
Dihydrolipoamide Dehydrogenase
Oxidative Stress
Selenoproteins
Sequence Homology
Quinones
Crystallography, X-Ray
Chromatography, High Pressure Liquid
Magnetic Resonance Spectroscopy
Electron Transport Complex III
A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane.
Electron Spin Resonance Spectroscopy
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
Gene Expression Regulation, Enzymologic
Clostridium
Sequence Analysis
Cattle
Alkenes
Protein Structure, Tertiary
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Ubiquinone
Sjogren-Larsson Syndrome
Plants
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
Protein Binding
Electrophoresis, Polyacrylamide Gel
Protein Structure, Secondary
Aldehyde-Lyases
Sequence Homology, Nucleic Acid
Oxygen
Sulfur
Chemistry, Organic
Amino Acids
Endoplasmic Reticulum
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
Conserved Sequence
Spectrophotometry
Liver
Hydrogenation
Metabolic Networks and Pathways
Gene Expression Regulation, Bacterial
Heme
Isoenzymes
Nitrate-dependent regulation of acetate biosynthesis and nitrate respiration by Clostridium thermoaceticum. (1/1279)
Nitrate has been shown to shunt the electron flow in Clostridium thermoaceticum from CO2 to nitrate, but it did not influence the levels of enzymes involved in the Wood-Ljungdahl pathway (J. M. Frostl, C. Seifritz, and H. L. Drake, J. Bacteriol. 178:4597-4603, 1996). Here we show that under some growth conditions, nitrate does in fact repress proteins involved in the Wood-Ljungdahl pathway. The CO oxidation activity in crude extracts of nitrate (30 mM)-supplemented cultures was fivefold less than that of nitrate-free cultures, while the H2 oxidation activity was six- to sevenfold lower. The decrease in CO oxidation activity paralleled a decrease in CO dehydrogenase (CODH) protein level, as confirmed by Western blot analysis. Protein levels of CODH in nitrate-supplemented cultures were 50% lower than those in nitrate-free cultures. Western blots analyses showed that nitrate also decreased the levels of the corrinoid iron-sulfur protein (60%) and methyltransferase (70%). Surprisingly, the decrease in activity and protein levels upon nitrate supplementation was observed only when cultures were continuously sparged. Northern blot analysis indicates that the regulation of the proteins involved in the Wood-Ljungdahl pathway by nitrate is at the transcriptional level. At least a 10-fold decrease in levels of cytochrome b was observed with nitrate supplementation whether the cultures were sparged or stoppered. We also detected nitrate-inducible nitrate reductase activity (2 to 39 nmol min-1 mg-1) in crude extracts of C. thermoaceticum. Our results indicate that nitrate coordinately represses genes encoding enzymes and electron transport proteins in the Wood-Ljungdahl pathway and activates transcription of nitrate respiratory proteins. CO2 also appears to induce expression of the Wood-Ljungdahl pathway genes and repress nitrate reductase activity. (+info)Aldehyde oxidase-dependent marked species difference in hepatic metabolism of the sedative-hypnotic, zaleplon, between monkeys and rats. (2/1279)
A marked difference in hepatic activity of aldehyde oxidase between rats and monkeys was found to be responsible for the previously reported marked species difference in the metabolism of Zaleplon in vivo. In the postmitochondrial fractions, S-9s, from liver homogenates of these animals, Zaleplon was transformed in the presence of NADPH into the side chain oxidation product, N-desethyl-Zaleplon, and the aromatic ring oxidation product, 5-oxo-Zaleplon. In the rat S-9, N-desethyl-Zaleplon and 5-oxo-Zaleplon were a major and a very minor metabolites, respectively. However, in the monkey S-9, Zaleplon was transformed into 5-oxo-Zaleplon at a much higher rate than that for N-desethyl-Zaleplon formation. N-Desethyl-Zaleplon was formed in the monkey S-9 at a rate almost equal to that in the rat S-9. N-Desethyl-5-oxo-Zaleplon was formed at a minor rate only in the monkey S-9 through N-desethyl-Zaleplon as an obligatory intermediate. The hepatic activity for the formation of 5-oxo-Zaleplon in the monkey and rat was localized in cytosol and did not require NADPH. Sensitivity to various inhibitors and requirement of water as oxygen source, using H218O, strongly suggested that the hepatic cytosolic formation of 5-oxo-Zaleplon was mediated by aldehyde oxidase. N-Desethyl-Zaleplon was formed in the presence of NADPH by microsomes from the liver of rats and monkeys, and its formation was strongly suggested using various cytochrome P-450 inhibitors to be mediated by a number of cytochrome P-450 isoforms, such as 3A, 2C, and 2D subfamilies. (+info)A genetic linkage map of rat chromosome 9 with a new locus for variant activity of liver aldehyde oxidase. (3/1279)
A genetic linkage map of rat chromosome 9 consisting of five loci including a new biochemical marker representing a genetic variation of the activity of the liver aldehyde oxidase, (Aox) was constructed. Linkage analysis of the five loci among 92 backcross progeny of (WKS/Iar x IS/Iar)F1 x WKS/Iar revealed significant linkages between these loci. Minimizing crossover frequency resulted in the best gene order: Aox-D9Mit4-Gls-Cryg-Tp53l1. The homologues of the Cryg, Gls, and Aox genes have been mapped on mouse chromosome 1 and human chromosome 2q. The present findings provide further evidence for the conservation of synteny among these regions of rat, mouse, and human chromosomes. (+info)Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase. (4/1279)
Pseudomonas aeruginosa ATCC 17933 grown aerobically on ethanol produces a soluble cytochrome c550 together with a quinoprotein ethanol dehydrogenase. A 3.2 kb genomic DNA fragment containing the gene encoding cytochrome c550 was cloned and sequenced. Two other complete and two truncated ORFs were also identified. A truncated ORF encoding the quinoprotein ethanol dehydrogenase (exaA) was found upstream of the cytochrome c550 gene (exaB) and in reverse orientation. An ORF encoding a NAD(+)-dependent acetaldehyde dehydrogenase (exaC) was located downstream of the cytochrome c550 gene and in the same orientation. Another ORF showed similarity to the pqqA gene and a truncated ORF similarity to the pqqB gene, both involved in the biosynthesis of the prosthetic group PQQ. The organization of these genes was found to be different from the well-studied methanol oxidation system in methylotrophic bacteria. The deduced amino acid sequence of cytochrome c550 from P. aeruginosa showed some similarity to cytochrome c6 of the alga Chlamydomonas reinhardtii and the haem domain of quinohaemoprotein alcohol dehydrogenases of acetic acid bacteria, but no similarity to the soluble cytochrome cL of the quinoprotein methanol oxidation system of methylotrophs could be detected. A mutant of P. aeruginosa with an interrupted cytochrome c550 gene was unable to grow on ethanol, which proves that cytochrome c550 is an essential component of the ethanol oxidation system in this organism. (+info)Xenopus cytosolic thyroid hormone-binding protein (xCTBP) is aldehyde dehydrogenase catalyzing the formation of retinoic acid. (5/1279)
Amino acid sequencing of an internal peptide fragment derived from purified Xenopus cytosolic thyroid hormone-binding protein (xCTBP) demonstrates high similarity to the corresponding sequence of mammalian aldehyde dehydrogenase 1 (ALDH1) (Yamauchi, K., and Tata, J. R. (1994) Eur. J. Biochem. 225, 1105-1112). Here we show that xCTBP was co-purified with ALDH and 3,3',5-triiodo-L-thyronine (T3) binding activities. By photoaffinity labeling with [125I]T3, a T3-binding site in the xCTBP was estimated to reside in amino acid residues 93-114, which is distinct from the active site of the enzyme but present in the NAD+ binding domain. The amino acid sequences deduced from the two isolated xALDH1 cDNAs (xALDH1-I and xALDH1-II) were 94.6% identical to each other and very similar to those of mammalian ALDH1 enzymes. The two recombinant xALDH1 proteins exhibit both T3 binding activity and ALDH activity converting retinal to retinoic acid (RA), which are similar to those of xCTBP. The mRNAs were present abundantly in kidney and intestine of adult female Xenopus. Interestingly, their T3 binding activities were inhibited by NAD+ and NADH but not by NADP+ and NADPH, whereas NAD+ was required for their ALDH activities. Our results demonstrate that xCTBP is identical to ALDH1 and suggest that this protein might modulate RA synthesis and intracellular level of free T3. (+info)Metabolism of daunorubicin by a barbiturate-sensitive aldehyde reductase from rat liver. (6/1279)
A barbiturate-sensitive aldehyde reductase was purified to homogeneity from rat liver and shown to metabolize the cancer-chemotherapeutic antibiotic daunorubicin. The aldehyde reductase may have important roles in the metabolism of exogeneous drugs as well as the aldehyde derivatives of the biogenic amines. (+info)The choline-converting pathway in Staphylococcus xylosus C2A: genetic and physiological characterization. (7/1279)
A Staphylococcus xylosus C2A gene cluster, which encodes enzymes in the pathway for choline uptake and dehydrogenation (cud), to form the osmoprotectant glycine betaine, was identified. The cud locus comprises four genes, three of which encode proteins with significant similarities to those known to be involved in choline transport and conversion in other organisms. The physiological role of the gene products was confirmed by analysis of cud deletion mutants. The fourth gene possibly codes for a regulator protein. Part of the gene cluster was shown to be transcriptionally regulated by choline and elevated NaCl concentrations as inducers. (+info)The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme--an aldehyde oxidoreductase. (8/1279)
In order to investigate the effects of trace elements on different metabolic pathways, the thermoacidophilic Crenarchaeon Sulfolobus acidocaldarius (DSM 639) has been cultivated on various carbon substrates in the presence and absence of molybdate. When grown on glucose (but neither on glutamate nor casein hydrolysate) as sole carbon source, the lack of molybdate results in serious growth inhibition. By analysing cytosolic fractions of glucose adapted cells for molybdenum containing compounds, an aldehyde oxidoreductase was detected that is present in the cytosol to at least 0.4% of the soluble protein. With Cl2Ind (2,6-dichlorophenolindophenol) as artificial electron acceptor, the enzyme exhibits oxidizing activity towards glyceraldehyde, glyceraldehyde-3-phosphate, isobutyraldehyde, formaldehyde, acetaldehyde and propionaldehyde. At its pH-optimum (6.7), close to the intracellular pH of Sulfolobus, the glyceraldehyde-oxidizing activity is predominant. The protein has an apparent molecular mass of 177 kDa and consists of three subunits of 80.5 kDa (alpha), 32 kDa (beta) and 19.5 kDa (gamma). It contains close to one Mo, four Fe, four acid-labile sulphides and four phosphates per protein molecule. Methanol extraction revealed the existence of 1 FAD per molecule and 1 molybdopterin per molecule, which was identified as molybdopterin guanine dinucleotide on the basis of perchloric acid cleavage and thin layer chromatography. EPR-spectra of the aerobically prepared enzyme exhibit the so-called 'desulpho-inhibited'-signal, known from chemically modified forms of molybdenum containing proteins. Anaerobically prepared samples show both, the signals arising from the active molybdenum-cofactor as well as from the two [2Fe-2S]-clusters. According to metal-, cofactor-, and subunit-composition, the enzyme resembles the members of the xanthine oxidase family. Nevertheless, the melting point and long-term thermostability of the protein are outstanding and perfectly in tune with the growth temperature of S. acidocaldarius (80 degrees C). The findings suggest the enzyme to function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylated Entner-Doudoroff pathway and thereby may attribute a new physiological role to this class of enzyme. (+info)
S-nitrosoglutathione reductase activity of human and yeast glutathione-dependent formaldehyde dehydrogenase and its nuclear and...
RCSB PDB
- 1FFU: CARBON MONOXIDE DEHYDROGENASE FROM HYDROGENOPHAGA PSEUDOFLAVA WHICH LACKS THE MO-PYRANOPTERIN MOIETY...
RCSB PDB - 1FFU: CARBON MONOXIDE DEHYDROGENASE FROM HYDROGENOPHAGA PSEUDOFLAVA WHICH LACKS THE MO-PYRANOPTERIN MOIETY OF THE...
EMBL: CP000667.PE356
Fatty aldehyde dehydrogenase deficiency. Causes, symptoms, treatment Fatty aldehyde dehydrogenase deficiency
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Acetaldehyde dehydrogenase
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Retinal Dehydrogenase
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Solyc06g074410.3.1 details
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CATH Superfamily 3.30.460.30
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Retinaldehyde dehydrogenase 1 | definition of retinaldehyde dehydrogenase 1 by Medical dictionary
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Abstract 537: S-Nitrosoglutathione Reductase (GSNOR) Deficiency Reduces Vascular Inflammation and Atherosclerosis. |...
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BADH genes in wheat and their expression by Keshav N. Shrestha, Daniel LE Waters et al.
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UniProt: P0A9Q7
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JCI -
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CiNii 論文 -
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Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an ... Roy R, Menon AL, Adams MW (2001). "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods Enzymol. Methods in Enzymology. ... The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. Other names in common use ... Mukund S, Adams MW (1995). "Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a ...
Alcohol dehydrogenase (nicotinoprotein)
Van Ophem PW, Van Beeumen J, Duine JA (March 1993). "Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. ... N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name ethanol:acceptor oxidoreductase. This enzyme ... catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes ...
Eubacterium acidaminophilum
"Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum". European Journal of Biochemistry / FEBS. 271 (1): ...
Methanol dehydrogenase (nicotinoprotein)
Van Ophem PW, Van Beeumen J, Duine JA (March 1993). "Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. ... N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name methanol:acceptor oxidoreductase. This enzyme ... dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803)". Microbiology. 156 (Pt 2): 463-71. doi: ... dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and ...
Carboxylate reductase
The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase. This enzyme is also called aldehyde:(acceptor) ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... In enzymology, a carboxylate reductase (EC 1.2.99.6) is an enzyme that catalyzes the chemical reaction an aldehyde + acceptor ... oxidoreductase. This enzyme participates in pyruvate metabolism. It employs one cofactor, tungsten. White H, Strobl G, Feicht R ...
Cofactor (biochemistry)
... tungsten in the aldehyde ferredoxin oxidoreductase of the thermophilic archaean Pyrococcus furiosus,[18] and even cadmium in ... aldehyde ferredoxin oxidoreductase". Science. 267 (5203): 1463-9. doi:10.1126/science.7878465. PMID 7878465.. ...
Cofactor (biochemistry)
... tungsten in the aldehyde ferredoxin oxidoreductase of the thermophilic archaean Pyrococcus furiosus, and even cadmium in the ... aldehyde ferredoxin oxidoreductase". Science. 267 (5203): 1463-9. Bibcode:1995Sci...267.1463C. doi:10.1126/science.7878465. ...
Metal dithiolene complex
November 1995). "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas". Science. 270 (5239 ...
Long-chain-fatty-acyl-CoA reductase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... The systematic name of this enzyme class is long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming). Other names in common ... H+ The 3 substrates of this enzyme are long-chain aldehyde, CoA, and NADP+, whereas its 3 products are long-chain acyl-CoA, ... is an enzyme that catalyzes the chemical reaction a long-chain aldehyde + CoA + NADP+ ⇌ {\displaystyle \rightleftharpoons } a ...
Sabyasachi Sarkar
... the Tungsten Sites of Inactive and Active Forms of Hyperthermophilic Pyrococcus furiosus Aldehyde Ferredoxin Oxidoreductase". ...
Pyruvate oxidase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (phosphorylating). Other names in common use ...
Formaldehyde dismutase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... Other names in common use include aldehyde dismutase, and cannizzanase. As of late 2007, only one structure has been solved for ... Kato N, Shirakawa K, Kobayashi H, Sakazawa C (1983). "The dismutation of aldehydes by a bacterial enzyme". Agric. Biol. Chem. ... The systematic name of this enzyme class is formaldehyde:formaldehyde oxidoreductase. ...
Carbon monoxide dehydrogenase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is carbon-monoxide:acceptor oxidoreductase. Other names in common use include ... oxidoreductase. Aerobic carboxydotrophic bacteria utilize copper-molybdenum flavoenzymes. Anaerobic bacteria utilize nickel- ... clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]". European Journal of Biochemistry ...
Formylmethanofuran dehydrogenase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is formylmethanofuran:acceptor oxidoreductase. This enzyme is also called ... formylmethanofuran:(acceptor) oxidoreductase. This enzyme participates in folate biosynthesis. It has 2 cofactors: molybdenum, ...
Aldo-keto reductase
... these include a number of related monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose reductase, ... This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases. Some proteins of this family contain a potassium ... cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". J. Biol. Chem. 264 (16): 9547-51. PMID 2498333 ... channel beta chain regulatory domain; these are reported to have oxidoreductase activity. AKR1 Steroidogenic enzyme Bohren KM, ...
Oxalate oxidase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is oxalate:oxygen oxidoreductase. Other names in common use include aero-oxalo ...
Retinal oxidase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... Mandal SK, Datta Chaudhuri B (1987). "Enzymic oxidation of vitamin A aldehyde to vitamin A acid by rat livers of experimental ... The systematic name of this enzyme class is retinal:oxygen oxidoreductase. This enzyme is also called retinene oxidase. This ... Huang DY, Furukawa A, Ichikawa Y (1999). "Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse ...
Glyoxylate oxidase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is glyoxylate:oxygen oxidoreductase. This enzyme participates in glyoxylate and ...
Indole-3-acetaldehyde oxidase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... T; Akaba, S; Oritani, T; Delarue, M; Bellini, C; Caboche, M; Koshiba, T (1998). "Higher activity of an aldehyde oxidase in the ... The systematic name of this enzyme class is (indol-3-yl)acetaldehyde:oxygen oxidoreductase. Other names in common use include ... Marion-Poll A, Caboche M, Kamiya Y, Koshiba T (1998). "Molecular cloning and characterization of aldehyde oxidases in ...
Pyruvate oxidase (CoA-acetylating)
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (CoA-acetylating). This enzyme participates in ...
Pyridoxal oxidase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is pyridoxal:oxygen 4-oxidoreductase. This enzyme participates in vitamin B6 ...
4-hydroxyphenylpyruvate oxidase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating). This enzyme ...
Pyruvate dehydrogenase (cytochrome)
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... The systematic name of this enzyme class is pyruvate:ferricytochrome-b1 oxidoreductase. Other names in common use include ... pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, and ...
Formate dehydrogenase (cytochrome)
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... The systematic name of this enzyme class is formate:ferricytochrome-b1 oxidoreductase. Other names in common use include ... formate dehydrogenase, and formate:cytochrome b1 oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate ...
Formate dehydrogenase (cytochrome-c-553)
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... The systematic name of this enzyme class is formate:ferricytochrome-c-553 oxidoreductase. Yagi T (October 1969). "Formate: ... cytochrome oxidoreductase of Desulfovibrio vulgaris". Journal of Biochemistry. 66 (4): 473-8. doi:10.1093/oxfordjournals.jbchem ...
3-methyl-2-oxobutanoate dehydrogenase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ...
Carbon-monoxide dehydrogenase (cytochrome b-561)
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... The systematic name of this enzyme class is carbon monoxide,water:cytochrome b-561 oxidoreductase. Other names in common use ... Meyer O, Schlegel HG (1980). "Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans". J. Bacteriol. ... include carbon monoxide oxidase, carbon monoxide oxygenase (cytochrome b-561), carbon monoxide:methylene blue oxidoreductase, ...
Tungsten
Aldehyde ferredoxin oxidoreductase (AOR) in Thermococcus strain ES-1 Formaldehyde ferredoxin oxidoreductase (FOR) in ... Tungsten-using enzymes typically reduce carboxylic acids to aldehydes. The tungsten oxidoreductases may also catalyse ... For example, enzymes called oxidoreductases use tungsten similarly to molybdenum by using it in a tungsten-pterin complex with ... One of the enzymes in the oxidoreductase family which sometimes employ tungsten (bacterial formate dehydrogenase H) is known to ...
Pyrococcus furiosus
... and for being one of the few organisms identified as possessing aldehyde ferredoxin oxidoreductase enzymes containing tungsten ...
List of MeSH codes (D08)
... aldehyde oxidoreductases MeSH D08.811.682.657.163.249 - aldehyde dehydrogenase MeSH D08.811.682.657.163.249.750 - omega- ... amino acid oxidoreductases MeSH D08.811.682.664.500.062 - alanine dehydrogenase MeSH D08.811.682.664.500.125 - d-amino-acid ... succinate cytochrome c oxidoreductase MeSH D08.811.600.250.875.249 - electron transport complex ii MeSH D08.811.600.250.875.249 ... aldehyde reductase MeSH D08.811.682.047.150.700.237 - d-xylulose reductase MeSH D08.811.682.047.150.700.400 - glycerolphosphate ...
2-alkenal reductase
The systematic name of this enzyme class is n-alkanal:NAD(P)+ 2-oxidoreductase. Other names in common use include NAD(P)H- ... detoxication of the lipid peroxide-derived reactive aldehydes". Plant Cell Physiol. 43 (12): 1445-55. doi:10.1093/pcp/pcf187. ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ ... dependent alkenal/one oxidoreductase, and NADPH:2-alkenal alpha,beta-hydrogenase. Structural studies[edit]. As of late 2007, ...
HADHB
EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
Pyruvate dehydrogenase (lipoamide) alpha 2
oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor. • pyruvate dehydrogenase (NAD+) ... oxidoreductase activity. • pyruvate dehydrogenase (acetyl-transferring) activity. • ...
پیرووات دهیدروژناز (لیپوآمید) آلفا ۱ - ویکیپدیا، دانشنامهٔ آزاد
oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor. • pyruvate dehydrogenase (NAD+) ... oxidoreductase activity. • pyruvate dehydrogenase (acetyl-transferring) activity. • ...
AKR1B1
oxidoreductase activity. • glyceraldehyde oxidoreductase activity. • alditol:NADP+ 1-oxidoreductase activity. • alcohol ... cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". The Journal of Biological Chemistry. 264 (16 ... AR belongs to the aldehyde-keto reductase superfamily, with a widely expression in human organs including the kidney, lens, ... It also participates in glucose metabolism and osmoregulation and plays a protective role against toxic aldehydes derived from ...
Oxidoreductase
Aldehyde of keton + NADH + H+ Alcoholdehydrogenase (NAD+) Ja 1.1.1.2 Alcohol + NADP+ ⇌. {\displaystyle \rightleftharpoons }. ... Aldehyde + NADPH + H+ Alcoholdehydrogenase (NADP+) Ja 1.1.1.3 L-Homoserine + NAD(P)+ ⇌. {\displaystyle \rightleftharpoons }. L- ... Overgenomen van "https://nl.wikipedia.org/w/index.php?title=Oxidoreductase&oldid=53921510" ...
Glutamate decarboxylase
4.1.2: Aldehyde-lyases. *Fructose-bisphosphate aldolase *Aldolase A. *Aldolase B. *Aldolase C ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
AKR1A1 - Wicipedia
cellular aldehyde metabolic process. • aldehyde catabolic process. • D-glucuronate catabolic process. • L-ascorbic acid ... alditol:NADP+ 1-oxidoreductase activity. • electron carrier activity. • oxidoreductase activity. • alcohol dehydrogenase (NADP+ ... "The role of aldehyde reductase AKR1A1 in the metabolism of γ-hydroxybutyrate in 1321N1 human astrocytoma cells. ". Chem Biol ... "Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. ". Acta Crystallogr D Biol ...
Transferase
Enzymes that transfer aldehyde or ketone groups and included in EC 2.2. This category consists of various transketolases and ... hydrogen transfer is included under oxidoreductases, due to electron transfer considerations. EC 2.1 includes enzymes that ... Transaldolase, the namesake of aldehyde transferases, is an important part of the pentose phosphate pathway. The reaction it ...
Acetyl-CoA carboxylase
EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
Entner-Doudoroff pathway
The aldehyde groups of the triose sugars are oxidised, and inorganic phosphate is added to them, forming 1,3- ... The G6P is then converted to 6-phosphogluconolactone in the presence of enzyme glucose-6-phosphate dehydrogenase( an oxido- ... The G3P is converted to 1,3-bisphosphoglycerate int the presence of enzyme glyceraldehyde-3-phosphate dehydrogenase (an oxido- ...
3-oxoacyl-(acyl-carrier-protein) reductase
The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase. Other names in ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
Acetaldehyde dehydrogenase
Aldehyde/oxo oxidoreductases (EC 1.2). 1.2.1: NAD or NADP. *Aldehyde dehydrogenase *Acetaldehyde dehydrogenase ... Oxidoreductase. References[edit]. *^ a b PDB: 1NVM; Manjasetty BA, Powlowski J, Vrielink A (Jun 2003). "Crystal structure of a ... Wang X, Weiner H (Jan 1995). "Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde ... Crabb D, Xiao Q (Jun 1998). "Studies on the enzymology of aldehyde dehydrogenase-2 in genetically modified HeLa cells". ...
BCKDHA
oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor. • protein binding. • metal ion ... oxidoreductase activity. • carboxy-lyase activity. • 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) ...
Caspase 8
1qtn: CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
ALDH2
oxidoreductase activity. • aldehyde dehydrogenase [NAD(P)+ activity]. • aldehyde dehydrogenase (NAD) activity. • NAD binding. • ... oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor. • glyceraldehyde-3-phosphate ... Mitochondrial aldehyde dehydrogenase belongs to the aldehyde dehydrogenase family of enzymes that catalyze the chemical ... ALDH2, ALDH-E2, ALDHI, ALDM, aldehyde dehydrogenase 2 family (mitochondrial), aldehyde dehydrogenase 2 family member. ...
ALDH16A1
oxidoreductase activity. • aldehyde dehydrogenase (NAD) activity. • oxidoreductase activity, acting on the aldehyde or oxo ... Aldehyde dehydrogenase 16 family, member A1 also known as ALDH16A1 is an aldehyde dehydrogenase gene. ... "Interaction of the SPG21 protein ACP33/maspardin with the aldehyde dehydrogenase ALDH16A1". Neurogenetics. 10 (3): 217-28. doi ...
ACADM
oxidoreductase activity, acting on the CH-CH group of donors. • acyl-CoA dehydrogenase activity. • identical protein binding. • ... oxidoreductase activity. • medium-chain-acyl-CoA dehydrogenase activity. • flavin adenine dinucleotide binding. ...
Lanosterol 14 alpha-demethylase
The aldehyde then departs as formic acid and a double bond is simultaneously introduced to yield the demethylated product.[7] ... Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14). 1.14.11: 2-oxoglutarate. *Prolyl hydroxylase ...
Glycolysis
The aldehyde groups of the triose sugars are oxidised, and inorganic phosphate is added to them, forming 1,3- ... an oxidoreductase D-1,3-bisphosphoglycerate (1,3BPG) NAD+ + Pi. NADH + H+. ...
Carbohydrate dehydrogenase
... s are the most common quinoprotein oxidoreductases,[1] which are enzymes that oxidize a wide range of ... a group of dehydrogenase enzymes that occur in many organisms and facilitate the conversion from a carbohydrate to an aldehyde ...
List of enzymes
1 Category:Oxidoreductases (EC 1) (Oxidoreductase) *1.1 Category:EC 1.1 (act on the CH-OH group of donors) ... Category:EC 1.2 (act on the aldehyde or oxo group of donors)Edit. *Category:EC 1.2.1 (with NAD+ or NADP+ as acceptor) * ... Category:EC 2.2 (transfer aldehyde or ketone groups)Edit. *Category:EC 2.2.1 *Transketolase EC 2.2.1.1 ... Category:EC 5.3 (intramolecular oxidoreductases)Edit. *Category:EC 5.3.3 *Enoyl CoA isomerase (EC 5.3.3.8) ...
Alkohol dehidrogenase bahasa Indonesia, ensiklopedia bebas
NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ oxidoreductase, ADH; EC 1.1.1.1) ... Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase ...
Enzyme inhibitor
Irreversible inhibitors often contain reactive functional groups such as nitrogen mustards, aldehydes, haloalkanes, alkenes, ... Oxidoreductase (EC 1). *1.1 Aldose reductase. *HMG-CoA reductase. *1.3 5α-Reductase ...
Enoyl-acyl carrier protein reductase
Oxidoreductases: CH-CH oxidoreductases (EC 1.3). 1.3.1: NAD/NADP acceptor. *Enoyl-acyl carrier protein reductase/Enoyl ACP ...
Dihydrokaempferol 4-reductase
The systematic name of this enzyme class is cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase. Other names in common use include ... In Arabidopsis thaliana, the enzyme uses sinapaldehyde or coniferyl aldehyde or coumaraldehyde and NADPH to produce sinapyl ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
Fatty acid synthase
oxidoreductase activity. • 3-oxoacyl-[acyl-carrier-protein synthase activity]. • acyl-[acyl-carrier-protein hydrolase activity] ...
Category:Protein pages needing a picture
Aldehyde ferredoxin oxidoreductase. *Aldehyde oxidase. *Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain ...
Aldehyde ferredoxin oxidoreductase - Wikipedia
In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction an aldehyde ... Aldehyde Ferredoxin Oxidoreductase is a member of an AOR family, which includes glyceraldehyde-3-phosphate ferredoxin ... The systematic name of this enzyme class is aldehyde:ferredoxin oxidoreductase. This enzyme is also called AOR. It is a ... Roy R, Dhawan IK, Johnson MK, Rees DC, Adams MW (2006-04-15). Handbook of Metalloproteins: Aldehyde Ferredoxin Oxidoreductase ( ...
Aldehyde ferredoxin oxidoreductase, N-terminal domain superfamily (IPR036503) | InterPro | EMBL-EBI
Aldehyde ferredoxin oxidoreductase, N-terminal domain superfamily (IPR036503). Short name: Ald_Fedxn_OxRdtase_N_sf ... Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family [PMID: 9242907] contain a tungsten cofactor and an 4Fe4S cluster ... Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase.. Science 267 1463-9 1995 ... formaldehyde ferredoxin oxidoreductase (FOR), glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), all isolated from ...
paoA - Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA precursor - Escherichia coli (strain K12) - paoA gene & protein
It might play a role in the detoxification of aldehydes to avoid cell damage. ... Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. ... oxidoreductase activity, acting on the aldehyde or oxo group of donors Source: EcoCycInferred from direct assayi*. Ref.5 ... Aldehyde oxidoreductase iron-sulfur-binding subunit PaoACurated (EC:1.2.99.6*Search proteins in UniProtKB for this EC number. ...
Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4...
Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ... Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ... Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ... Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ...
Tungsten-containing aldehyde oxidoreductases
Three different types of tungsten-containing aldehyde oxidizing enzymes aldehyde ferredoxin oxidoreductase (AOR), formaldehyde ... Detailed kinetic analyses of FOR indicate that C4 - C6 dialdehyde or acid-substituted aldehyde may serve as the physiological ... ferredoxin oxidoreductase (FOR) and glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) have previously been isolated ...
ECMDB: aldehyde oxidoreductase, ethanolamine utilization protein (P77445)
eco:b2455 eutE; aldehyde oxidoreductase, ethanolamine utilization protein; K04021 aldehyde dehydrogenase (N) ... eco:b2455 eutE; aldehyde oxidoreductase, ethanolamine utilization protein; K04021 aldehyde dehydrogenase (A) ... aldehyde oxidoreductase, ethanolamine utilization protein (P77445). Identification. Name:. aldehyde oxidoreductase, ...
Mo MOLYBDENUM TUNGSTEN Nitrogenase Xanthine oxidase Aldehyde Oxidoreductase MOP
Скачать презентацию Mo MOLYBDENUM TUNGSTEN Nitrogenase Xanthine oxidase Aldehyde Oxidoreductase MOP 19-Mo Ni Mn Со Биохимия ... Mo MOLYBDENUM/TUNGSTEN Nitrogenase Xanthine oxidase Aldehyde Oxidoreductase (MOP) Dimethylsulfoxide Reductase Trimethylamine N- ... Oxide Reductase Dissimilatory Nitrate Reductase Formaldehyde Ferredoxin Oxidoreductase Aldehyde Ferredoxin Oxidoreductase ...
NAVER Academic | Aldehyde oxidoreductase as a biocatalyst: Reductions of vanillic acid
ATP and NADPH dependent reduction of carboxylic acids to their corresponding aldehydes. The identification of the gene from ... Aldehyde oxidoreductase (carboxylic acid reductase) catalyzes the Mg 2+, ... Aldehyde oxidoreductase as a biocatalyst: Reductions of vanillic acid. Author. Venkitasubramanian Padmesh, Daniels Lacy, Das ... Aldehyde oxidoreductase (carboxylic acid reductase) catalyzes the Mg 2+, ATP and NADPH dependent reduction of carboxylic acids ...
Cloning of the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine...
Aldehyde oxidase as a cell marker for internal organs in Drosophila melanogaster. - PubMed - NCBI
1dgj.1 | SWISS-MODEL Template Library
CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 ... CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774. Coordinates. PDB Format Method. X ... Rebelo, J. et al., Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC ...
New tasks for old enzymes: xanthine oxidase and aldehyde oxidoreductase
- Universidade NOVA de Lisboa
Table of Contents - March 10, 1995, 267 (5203) | Science
Increased production of wax esters in transgenic tobacco plants by expression of a fatty acid reductase:wax synthase gene fusion
Down-regulation of the AtCCR1 gene in Arabidopsis thaliana: effects on phenotype, lignins and cell wall degradability
Proteins matched: AFOR N (SM00790) | InterPro | EMBL-EBI
Tungsten-containing aldehyde ferredoxin oxidoreductase. Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). ... Tungsten-containing aldehyde ferredoxin oxidoreductase. Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1). ... Aldehyde ferredoxin oxidoreductase, domains 2 & 3 family protein. Escherichia coli 1-176-05_S3_C2. Loading... ... Tungsten-containing aldehyde ferredoxin oxidoreductase. Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC ...
Energies | Free Full-Text | Microbial Conversion of Waste Glycerol from Biodiesel Production into Value-Added Products | HTML
... aldehyde oxidoreductase; DHAK, dihydroxyacetone kinase; FHL, formate hydrogen lyase complex; FRD, fumarate reductase; GlyD, ... aldehyde oxidoreductase; DHAK, dihydroxyacetone kinase; FHL, formate hydrogen lyase complex; FRD, fumarate reductase; GlyD, ... Zhang, Y.; Li, Y.; Du, C.; Liu, M.; Cao, Z. Inactivation of aldehyde dehydrogenase: A key factor for engineering 1,3- ... By inactivating aldehyde dehydrogenase (ADH), the enzyme responsible for ethanol formation in K. pneumoniae YMU2, less ethanol ...
Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes<...
Maia, Luisa B. ; Moura, José J.G. / Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite ... Maia, L. B., & Moura, J. J. G. (2018). Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite ... Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes. / Maia, ... Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes. Redox ...
MEDLINE - Resultado p gina 1
MEDLINE - Resultado p gina 1
Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) - Wikipedia
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an ... Roy R, Menon AL, Adams MW (2001). "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods Enzymol. Methods in Enzymology. ... The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. Other names in common use ... Mukund S, Adams MW (1995). "Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a ...
Isotropic exchange interaction between Mo and the proximal FeS center in the xanthine oxidase family member aldehyde...
Aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is a homodimeric molybdenum-containing protein that catalyzes the ... exchange interaction between Mo and the proximal FeS center in the xanthine oxidase family member aldehyde oxidoreductase from ... exchange interaction between Mo and the proximal FeS center in the xanthine oxidase family member aldehyde oxidoreductase from ... hydroxylation of aldehydes to carboxylic acids and contains a Mo-pyranopterin active site and two FeS centers called FeS 1 and ...
Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for...
The XO family member aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is an exception as presents in its catalytically ... Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for ... Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for ... Mononuclear Mo-containing enzymes of the xanthine oxidase (XO) family catalyze the oxidative hydroxylation of aldehydes and ...
RCSB PDB - 1GAD: COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE...
RCSB PDB - 3GPD: TWINNING IN CRYSTALS OF HUMAN SKELETAL MUSCLE D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
Cofactor (biochemistry) - Wikipedia
KEGG ENZYME: 1.2.99.7
Oxidoreductases;. Acting on the aldehyde or oxo group of donors;. With unknown physiological acceptors. ... Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491 EPR assignment of the proximal [2Fe-2S] cluster to the ... Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from ... Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. ...
KEGG ENZYME: 1.2.1.29
Oxidoreductases;. Acting on the aldehyde or oxo group of donors;. With NAD+ or NADP+ as acceptor. ... an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+ [RN:R01486]. ... The oxidation of gentisaldehyde by nicotinamide-adenine dinucleotide-specific, aromatic aldehyde dehydrogenase from rabbit ...
EC 1.2.2 to EC 1.2.99
Other name(s): aldehyde oxidase; aldehyde oxidoreductase; Mop; AORDd. Systematic name: aldehyde:acceptor oxidoreductase (FAD- ... Other name(s): aldehyde:(acceptor) oxidoreductase. Systematic name: aldehyde:acceptor oxidoreductase. Comments: A tungsten ... Accepted name: aldehyde ferredoxin oxidoreductase. Reaction: an aldehyde + H2O + 2 oxidized ferredoxin = a carboxylate + 2 H+ ... Systematic name: aldehyde:quinone oxidoreductase. Comments: Wide specificity; acts on straight-chain aldehydes up to C10, ...
OxidaseFerredoxinEnzymesNADHPyrococcusMetabolismFormaldehydeRole in the detoxification of aldehydesAcceptorAlcoholsSubstrateOxidation of fatty aldehydesCarboxylateAryl-aldehydeDesulfovibrioMolybdenumCarboxylic acid reductaseGenesAlcoholEndogenous and exogenousGeneGeneticsAromatic aldehydeAliphatic aldehydesCatalyzesMitochondrialPyruvateProteinPMID
Oxidase16
- Aldehyde oxidase as a cell marker for internal organs in Drosophila melanogaster. (nih.gov)
- Herein, we will review the current knowledge on two of those "non-dedicated nitrite reductases", the molybdoenzymes xanthine oxidoreductase and aldehyde oxidase, discussing the in vitro and in vivo studies to provide the current picture of the role of these enzymes on the NO metabolism in humans. (unl.pt)
- Maia, LB & Moura, JJG 2018, ' Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes ', Redox Biology , vol. 19, pp. 274-289. (unl.pt)
- Mononuclear Mo-containing enzymes of the xanthine oxidase (XO) family catalyze the oxidative hydroxylation of aldehydes and heterocyclic compounds. (conicet.gov.ar)
- Purification and characterization of an aldehyde oxidase from Pseudomonas sp. (genome.jp)
- Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. (genome.jp)
- 2. Knox, W.E. The quinine-oxidizing enzyme and liver aldehyde oxidase. (qmul.ac.uk)
- Aldehyde oxidase: a molybdoflavoprotein. (qmul.ac.uk)
- 6. Yoshihara, S. and Tatsumi, K. Purification and characterization of hepatic aldehyde oxidase in male and female mice. (qmul.ac.uk)
- The trace element molybdenum is essential for nearly all organisms and forms the catalytic centre of a large variety of enzymes such as nitrogenase, nitrate reductases, sulphite oxidase and xanthine oxidoreductases. (nature.com)
- Other enzymes such as xanthine oxidoreductase or aldehyde oxidase may also be involved. (labome.org)
- Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (uni-potsdam.de)
- Aldehyde oxidase (AOX1) is an enzyme with broad substrate specificity, catalyzing the oxidation of a wide range of endogenous and exogenous aldehydes as well as N-heterocyclic aromatic compounds. (aspetjournals.org)
- The enzymes xanthine oxidoreductase (XOR) and aldehyde oxidase (AO) catalyzed the oxidation of M1dG and M1G. (vanderbilt.edu)
- Other names in common use include betaine aldehyde oxidase , BADH , betaine aldehyde dehydrogenase , and BetB . (academic.ru)
- The molybdoflavoenzymes (MFEs), aldehyde oxidase (AOX) and xanthine oxidoreductase (XOR) catalyse the oxidation of many drugs, environmental pollutants and N-heterocyclic compounds. (hud.ac.uk)
Ferredoxin15
- In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction an aldehyde + H2O + 2 oxidized ferredoxin ⇌ an acid + 2 H+ + 2 reduced ferredoxin This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. (wikipedia.org)
- The systematic name of this enzyme class is aldehyde:ferredoxin oxidoreductase. (wikipedia.org)
- Aldehyde Ferredoxin Oxidoreductase is a member of an AOR family, which includes glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) and Formaldehyde Ferredoxin Oxidoreductase. (wikipedia.org)
- The main substrates for aldehyde ferredoxin oxidoreductase are acetaldehyde, phenylacetaldehyde, and isovalerdehyde, which is a metabolic product from common amino acids and glucose. (wikipedia.org)
- thus, they utilize aldehyde ferredoxin oxidoreductase to metabolize the amino acid carbon source. (wikipedia.org)
- Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family [ PMID: 9242907 ] contain a tungsten cofactor and an 4Fe4S cluster and catalyse the interconversion of aldehydes to carboxylates [ PMID: 8672295 ]. (ebi.ac.uk)
- Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. (ebi.ac.uk)
- Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase. (ebi.ac.uk)
- Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. (ebi.ac.uk)
- Three different types of tungsten-containing aldehyde oxidizing enzymes aldehyde ferredoxin oxidoreductase (AOR), formaldehyde ferredoxin oxidoreductase (FOR) and glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) have previously been isolated from this microorganism. (uga.edu)
- The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. (wikipedia.org)
- Other names in common use include GAPOR, glyceraldehyde-3-phosphate Fd oxidoreductase, and glyceraldehyde-3-phosphate ferredoxin reductase. (wikipedia.org)
- Consistently, most of the other active oxidoreductases rely on either reduced ferredoxin and/or NADPH as the electron donor. (asm.org)
- Key to the understanding of this energy metabolism is the presence of membrane-associated reduced ferredoxin:NAD + oxidoreductase (Rnf), of electron-bifurcating and ferredoxin-dependent transhydrogenase (Nfn), and of acetaldehyde:ferredoxin oxidoreductase, which is present with very high specific activities in H 2 /CO 2 -grown cells. (asm.org)
- In the case of substrate-level phosphorylation, acetyl-CoA reduction to ethanol proceeds via free acetic acid involving acetaldehyde:ferredoxin oxidoreductase (carboxylate reductase). (asm.org)
Enzymes5
- During an analysis of the C. bescii genome sequence for oxidoreductase-type enzymes, evidence was uncovered to suggest that the primary redox metabolism of C. bescii has a completely uncharacterized aspect involving tungsten, a rarely used element in biology. (asm.org)
- [ 17 ] Schiff-base aldehyde adducts with other amino-containing molecules, including key membrane enzymes and proteins, may also be detrimental to their function. (medscape.com)
- Aldehyde dehydrogenase enzymes oxidize aldehydes to generate carboxylic acids for use in the muscle and heart. (genecards.org)
- Any of a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones. (thefreedictionary.com)
- The two main enzymes involved in alcohol metabolism are alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). (thefreedictionary.com)
NADH3
- 3. Schenkels, P. and Duine, J.A. Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes. (qmul.ac.uk)
- The 3 substrates of this enzyme are betaine aldehyde , NAD + , and H 2 O , whereas its 3 products are betaine , NADH , and H + . (academic.ru)
- Catalysis of the reaction: an aldehyde + NAD+ + H2O = an acid + NADH + H+. (yeastgenome.org)
Pyrococcus1
- The archaeons Pyrococcus ES-4 strain and Thermococcus ES-1 strain differ by their substrate specificity: AFOs show a broader size range of its aldehyde substrates. (wikipedia.org)
Metabolism8
- Its primary role is to oxidize aldehyde coming derived from the metabolism of amino acids and glucoses. (wikipedia.org)
- However, other proposals include its role in oxidation of amino acid metabolism aldehyde side products coming from de-aminated 2-ketoacids. (wikipedia.org)
- The aim of this study was to identify the cardiac oxidoreductases involved in the metabolism of 4-hydroxy-2- trans -nonenal (HNE), an α,β unsaturated aldehyde generated during the peroxidation of ω-6 polyunsaturated fatty acids. (biochemj.org)
- The enzyme from liver exhibits a broad substrate specificity, and is involved in the metabolism of xenobiotics, including the oxidation of N- heterocycles and aldehydes and the reduction of N- oxides, nitrosamines, hydroxamic acids, azo dyes, nitropolycyclic aromatic hydrocarbons, and sulfoxides [4,6]. (qmul.ac.uk)
- Two decades later, Sjögren-Larsson syndrome was shown to be an inborn error of lipid metabolism caused by deficient activity of fatty alcohol:NAD oxidoreductase. (medscape.com)
- Therefore, patients with Sjögren-Larsson syndrome have deficient activity of FALDH and fatty alcohol:NAD oxidoreductase, which results in defective metabolism of both fatty aldehyde and fatty alcohol. (medscape.com)
- Aldehyde dehydrogenase is the second enzyme of the major oxidative pathway of alcohol metabolism. (genecards.org)
- This gene encodes a member of the aldehyde dehydrogenase family, a group of isozymes that may play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. (creativebiomart.net)
Formaldehyde2
- Here, we tested the removal of formaldehyde and aromatic aldehydes using effective microorganisms including yeast, lactic acid bacteria, and photosynthetic bacteria. (springer.com)
- Other aldehydes were analyzed by GC-MS. Results show that effective microorganisms remove 70-100 % of formaldehyde, benzaldehyde, and 4-methylbenzaldehyde in about a week. (springer.com)
Role in the detoxification of aldehydes1
- It might play a role in the detoxification of aldehydes to avoid cell damage. (uniprot.org)
Acceptor1
- This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. (wikipedia.org)
Alcohols4
- Reduction of aromatic acids to aldehydes and alcohols in the cell-free system. (naver.com)
- Gröger H, Hummel W, Borchert S, Kraußer M (2011) Reduction of ketones and aldehydes to alcohols. (springer.com)
- Sjögren-Larsson syndrome is a genetic disease characterized by ichthyosis, mental retardation, spasticity and mutations in the ALDH3A2 gene coding for fatty aldehyde dehydrogenase, an enzyme necessary for oxidation of fatty aldehydes and fatty alcohols. (pubmedcentralcanada.ca)
- Fatty aldehydes and their precursor lipids, such as fatty alcohols [ 30 ] and leukotriene B4 [ 38 , 39 ], accumulate in tissues of SLS patients. (pubmedcentralcanada.ca)
Substrate2
- Detailed kinetic analyses of FOR indicate that C4 - C6 dialdehyde or acid-substituted aldehyde may serve as the physiological substrate for this enzyme. (uga.edu)
- Described herein are multimeric oxidoreductase complexes which function in the enzymatic conversion of a carbon substrate. (freepatentsonline.com)
Oxidation of fatty aldehydes1
- [ 9 ] FALDH is involved in the oxidation of fatty aldehydes produced by catabolism of ether glycerolipids (plasmalogens), which are prominent phospholipids in myelin. (medscape.com)
Carboxylate1
- Carboxylate reductases (CARs, E.C. 1.2.1.30) generate aldehydes from their corresponding carboxylic acid with high selectivity. (frontiersin.org)
Aryl-aldehyde2
Desulfovibrio5
- Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774. (expasy.org)
- Aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is a homodimeric molybdenum-containing protein that catalyzes the hydroxylation of aldehydes to carboxylic acids and contains a Mo-pyranopterin active site and two FeS centers called FeS 1 and FeS 2. (conicet.gov.ar)
- The XO family member aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is an exception as presents in its catalytically competent form an equatorial oxo ligand instead of the sulfido ligand. (conicet.gov.ar)
- Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from Desulfovibrio desulfuricans ATCC 27774. (genome.jp)
- Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491 EPR assignment of the proximal [2Fe-2S] cluster to the Mo site. (genome.jp)
Molybdenum3
- and hydroxycarboxylate viologen oxidoreductase from Proteus vulgaris, the sole member of the AOR family containing molybdenum. (wikipedia.org)
- and hydroxycarboxylate viologen oxidoreductase from Proteus vulgaris, the sole member of the AOR family containing molybdenum [ PMID: 8026480 ]. (ebi.ac.uk)
- The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein. (ebi.ac.uk)
Carboxylic acid reductase3
- Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes. (ebi.ac.uk)
- Aldehyde oxidoreductase (carboxylic acid reductase) catalyzes the Mg 2+, ATP and NADPH dependent reduction of carboxylic acids to their corresponding aldehydes. (naver.com)
- carboxylic acid reductase: cloning, expression, and characterization of a new aldehyde oxidoreductase family. (naver.com)
Genes1
- Numerous aldehyde dehydrogenase genes exist, of which ALDH2 is best known for its role in alcohol oxidation. (genecards.org)
Alcohol6
- [ 3 ] Subsequent studies identified a defect in fatty aldehyde dehydrogenase (FALDH), a component of the fatty alcohol:NAD oxidoreductase enzyme complex. (medscape.com)
- [ 9 ] FALDH is a component of the fatty alcohol:NAD oxidoreductase enzyme complex that catalyzes the sequential oxidation of fatty alcohol to aldehyde and fatty acid. (medscape.com)
- Fatty alcohol and aldehyde may likewise alter the normal integrity of myelin membranes in the brain, leading to white-matter disease and spasticity. (medscape.com)
- Impaired fatty alcohol oxidation in cultured fibroblasts due to deficient fatty alcohol:nicotinamide adenine dinucleotide oxidoreductase activity. (medscape.com)
- Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. (medscape.com)
- 1. Van Ophem, P.W., Van Beeumen, J. and Duine, J.A. Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. (qmul.ac.uk)
Endogenous and exogenous1
- Thus AR might constitute an antioxidative enzyme involved in myocardial protection against endogenous and exogenous cytotoxic aldehydes and against oxidative stress. (biochemj.org)
Gene5
- Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene. (medscape.com)
- Rizzo WB, Carney G. Sjogren-Larsson syndrome: diversity of mutations and polymorphisms in the fatty aldehyde dehydrogenase gene (ALDH3A2). (medscape.com)
- ALDH2 (Aldehyde Dehydrogenase 2 Family (Mitochondrial)) is a Protein Coding gene. (genecards.org)
- GO annotations related to this gene include oxidoreductase activity and aldehyde dehydrogenase (NAD) activity . (genecards.org)
- Sjögren-Larsson syndrome (SLS) is caused by mutations in the ALDH3A2 gene that encodes fatty aldehyde dehydrogenase (FALDH) [ 2 ], an enzyme that catalyzes the oxidation of aliphatic aldehydes to fatty acids [ 17 , 29 ]. (pubmedcentralcanada.ca)
Genetics1
- Sjogren-Larsson syndrome: molecular genetics and biochemical pathogenesis of fatty aldehyde dehydrogenase deficiency. (medscape.com)
Aromatic aldehyde1
- The oxidation of gentisaldehyde by nicotinamide-adenine dinucleotide-specific, aromatic aldehyde dehydrogenase from rabbit liver. (genome.jp)
Aliphatic aldehydes2
- Oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes. (genome.jp)
- FALDH acts on several aliphatic aldehydes, but no single lipid has been identified yet as central to the pathogenesis. (pubmedcentralcanada.ca)
Catalyzes3
- Aldehyde Dehydrogenase, Yeast, CAS 9028-88-0, is a native aldehyde dehydrogenase from yeast that catalyzes the oxidation of acetaldehyde to acetic acid. (merckmillipore.com)
- The genetic defect in Sjögren-Larsson syndrome results in deficient activity of FALDH, which catalyzes the oxidation of fatty aldehyde to fatty acid. (medscape.com)
- Microsomal fatty aldehyde dehydrogenase catalyzes the oxidation of aliphatic aldehyde derived from ether glycerolipid catabolism: implications for Sjogren-Larsson syndrome. (medscape.com)
Mitochondrial2
- Two major liver isoforms of aldehyde dehydrogenase, cytosolic and mitochondrial, can be distinguished by their electrophoretic mobilities, kinetic properties, and subcellular localizations. (genecards.org)
- Vascular responses to nitrite are mediated by xanthine oxidoreductase and mitochondrial aldehyde dehydrogenase in the rat. (semanticscholar.org)
Pyruvate1
- The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (phosphorylating). (wikipedia.org)
Protein1
- This protein belongs to the aldehyde dehydrogenase family of proteins. (genecards.org)
PMID1
- AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid oxidoreductases [ PMID: 9275170 ]. (ebi.ac.uk)