Oxidoreductases
Aldehyde Dehydrogenase
Protein Disulfide Reductase (Glutathione)
Alcohol Oxidoreductases
Pyruvate Synthase
NADH, NADPH Oxidoreductases
Glutaredoxins
Oxidation-Reduction
Protein Disulfide-Isomerases
Aldehyde Reductase
Oxidoreductases Acting on Sulfur Group Donors
Thioredoxins
Oxidoreductases Acting on Aldehyde or Oxo Group Donors
Amino Acid Sequence
Molecular Sequence Data
Quinone Reductases
Electron Transport Complex II
Wolinella
NAD
Catalysis
NADP
Thioredoxin-Disulfide Reductase
Disulfides
Substrate Specificity
Succinate Dehydrogenase
Coenzymes
Acetaldehyde
Oxidoreductases Acting on CH-CH Group Donors
Electron Transport
Glucose Oxidase
Sequence Homology, Amino Acid
Pleurotus
NAD(P)H Dehydrogenase (Quinone)
Ferredoxin-NADP Reductase
Flavin-Adenine Dinucleotide
Electron Transport Complex I
15-Oxoprostaglandin 13-Reductase
Escherichia coli
Flavins
Stereoisomerism
Alcohol Dehydrogenase
Sequence Alignment
Iron-Sulfur Proteins
Disulfiram
Oxidoreductases Acting on CH-NH2 Group Donors
Prokaryotic Cells
Xanthine Dehydrogenase
Protochlorophyllide
Binding Sites
Models, Molecular
Multienzyme Complexes
Electrons
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
Oxidoreductases, O-Demethylating
Glutathione
Catalytic Domain
Succinic Acid
Multigene Family
Ferredoxins
Enzyme Stability
Protein Conformation
Anaerobiosis
Malate Dehydrogenase
Metalloproteins
Mass Spectrometry
Selenocysteine
Bacteria
Dihydrolipoamide Dehydrogenase
Oxidative Stress
Selenoproteins
Sequence Homology
Quinones
Crystallography, X-Ray
Chromatography, High Pressure Liquid
Magnetic Resonance Spectroscopy
Electron Transport Complex III
Electron Spin Resonance Spectroscopy
Gene Expression Regulation, Enzymologic
Clostridium
Sequence Analysis
Cattle
Alkenes
Protein Structure, Tertiary
Ubiquinone
Sjogren-Larsson Syndrome
Plants
Protein Binding
Electrophoresis, Polyacrylamide Gel
Protein Structure, Secondary
Aldehyde-Lyases
Sequence Homology, Nucleic Acid
Oxygen
Sulfur
Chemistry, Organic
Amino Acids
Endoplasmic Reticulum
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)* Intellectual disability: Individuals with Sjogren-Larsson syndrome typically have mild to moderate intellectual disability, which can range from mild cognitive impairment to more severe developmental delays.
* Seizures: Seizures are a common feature of Sjogren-Larsson syndrome, and they can be difficult to control with medication.
* Physical abnormalities: Individuals with Sjogren-Larsson syndrome may have distinctive physical features, such as short stature, thinning of the hair on the scalp, and thin, brittle skin. They may also have joint deformities, such as clubfoot or scoliosis.
* Vision problems: Sjogren-Larsson syndrome can cause vision problems, including nearsightedness, farsightedness, and astigmatism.
* Hearing loss: Some individuals with Sjogren-Larsson syndrome may experience hearing loss or auditory processing disorders.
There is no cure for Sjogren-Larsson syndrome, but various treatments can help manage the symptoms. These may include medications to control seizures, physical therapy to improve joint mobility and strength, and occupational therapy to develop daily living skills. In addition, speech and language therapy may be helpful for individuals with hearing loss or communication difficulties.
Early diagnosis of Sjogren-Larsson syndrome is important to ensure that children receive appropriate interventions and support as early as possible. Diagnosis typically involves a combination of clinical evaluation, genetic testing, and imaging studies, such as MRI or CT scans. Genetic counseling can also be helpful for families who have a history of the condition.
Overall, Sjogren-Larsson syndrome is a rare and complex disorder that requires careful management and support. With appropriate interventions and resources, individuals with this condition can lead fulfilling lives.
Aldehyde ferredoxin oxidoreductase
Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
Peptoclostridium acidaminophilum
Alcohol dehydrogenase (nicotinoprotein)
Methanol dehydrogenase (nicotinoprotein)
Carboxylate reductase
Cofactor (biochemistry)
Metal dithiolene complex
Aldehyde dehydrogenase (NAD+)
Aldehyde dehydrogenase (NADP+)
Betaine-aldehyde dehydrogenase
Aldehyde dehydrogenase (pyrroloquinoline-quinone)
Aryl-aldehyde dehydrogenase (NADP+)
Aryl-aldehyde oxidase
Aldehyde dehydrogenase (NAD(P)+)
Abscisic-aldehyde oxidase
Aryl-aldehyde dehydrogenase
Aldehyde dehydrogenase (FAD-independent)
Coniferyl-aldehyde dehydrogenase
Pyrococcus furiosus
Long-chain-fatty-acyl-CoA reductase
Sabyasachi Sarkar
Artemisinic aldehyde Delta11(13)-reductase
Formaldehyde dismutase
Carbon monoxide dehydrogenase
Formylmethanofuran dehydrogenase
Aldo-keto reductase
Oxalate oxidase
Retinal oxidase
Glyoxylate oxidase
Molybdopterin
Aflatoxin B1
Luciferase
2-alkenal reductase
Oxoglutarate dehydrogenase (NADP+)
Toxication
Dihydrokaempferol 4-reductase
Benzene
Fluoroacetaldehyde dehydrogenase
Cinnamoyl-CoA reductase
Coniferyl-alcohol dehydrogenase
Xanthoxin dehydrogenase
Methylmalonate-semialdehyde dehydrogenase (acylating)
Phenylglyoxylate dehydrogenase (acylating)
Long-chain-alcohol oxidase
Choline dehydrogenase
Aspartate-semialdehyde dehydrogenase
5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase
Pyridoxine 5′-phosphate oxidase
Nitroalkane oxidase
YRC Public Data Repository - Protein Overview - dhs-16 / CE08067
DeCS
Improvement in outcomes after cardiac arrest and resuscitation by inhibition of S-nitrosoglutathione reductase
Search results | TNO Publications
Network Portal - Gene DVU1674
Pesquisa | Portal Regional da BVS
Glyceraldehyde 3-phosphate dehydrogenase
Browsing TOBIAS-lib - Publikationen und Dissertationen by Title
"sequence id","alias","species","description",...
Pyrococcus furiosus - Alchetron, The Free Social Encyclopedia
Find Research outputs - Discovery - the University of Dundee Research Portal
MedlinePlus: Genetic Conditions: C
ExplorEnz: a MySQL database of the IUBMB enzyme nomenclature | BMC Biochemistry | Full Text
Le, N. Q. K.<...
Hollmann, F.<...
ExplorEnz: EC 1.1.1.164
yajO protein (Escherichia coli K12 MG1655) - STRING interaction network
Pathway analysis of kidney cancer using proteomics and metabolic profiling | Molecular Cancer | Full Text
DeCS
DeCS 2011 - December 22, 2011 version
1.2.99.10: 4,4'-diapolycopenoate synthase - BRENDA Enzyme Database
Granty: Katedra biochemie
Computer simulation studies of the catalytic mechanism of human aldose reductase : Sussex Research Online
CAL00874 details
Comparison of prokaryotes between Mount Everest and the Mariana Trench | Microbiome | Full Text
PDB 5OUJ | Chain CRYSTAL STRUCTURE OF HUMAN AKR1B1 COMPLEXED WITH NADP+ AND COMPOUND 39 | 5OUJ A | 3D Structure | canSARS
Enzyme families | IUPHAR/BPS Guide to IMMUNOPHARMACOLOGY
Molecules | Free Full-Text | Genetically Encodable Scaffolds for Optimizing Enzyme Function
Dehydrogenase1
- aldehyde dehydrogenase (predicted). (ntu.edu.sg)
Reductase activity1
- Is a major source of NADPH-dependent aldehyde reductase activity in E.coli. (string-db.org)
Alcohols1
- Catalyzes the reduction of a wide range of aldehydes into their corresponding alcohols. (string-db.org)
Enzyme2
- For example, in the case of EC 1.2.3.4, the digits indicate that the enzyme is an oxidoreductase (class 1), that it acts on the aldehyde or oxo group of donors (subclass 2), that oxygen is an acceptor (sub-subclass 3) and that it was the fourth enzyme classified in this sub-subclass (serial number 4). (biomedcentral.com)
- The Euglena enzyme also oxidizes the corresponding aldehydes to fatty acids. (enzyme-database.org)
Acts1
- We conclude that Tyr-48 acts as the proton donor in the reduction of aldehydes by aldose reductase, while the neutral His-110 has a role in substrate binding during the catalysis. (sussex.ac.uk)