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Identification
YMDB IDYMDB00143
NameNADH
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionNADH is a coenzyme found in all living cells. The main functions of NADH are electron transfer reactions by being alternately oxidized (NAD+) and reduced (NADH).
Structure
Thumb
Synonyms
  • 1,4-Dihydronicotinamide adenine dinucleotide
  • b-DPNH
  • b-NADH
  • beta-DPNH
  • beta-NADH
  • Dihydrocodehydrogenase I
  • Dihydrocozymase
  • Dihydronicotinamide adenine dinucleotide
  • Dihydronicotinamide mononucleotide
  • DPNH
  • ENADA
  • NADH
  • NADH2
  • Reduced codehydrogenase I
  • Reduced diphosphopyridine nucleotide
  • Reduced nicotinamide adenine diphosphate
  • Reduced nicotinamide-adenine dinucleotide
  • Nicotinamide adenine dinucleotide (reduced)
  • Reduced nicotinamide adenine dinucleotide
  • Nadide
  • Coenzyme I
  • DPN
  • Diphosphopyridine nucleotide
  • Nicotinamide adenine dinucleotide
  • Nicotinamide-adenine dinucleotide
  • NAD
  • Nucleotide, diphosphopyridine
  • Adenine dinucleotide, dihydronicotinamide
  • Dinucleotide, dihydronicotinamide adenine
  • Dinucleotide, nicotinamide-adenine
CAS number58-68-4
WeightAverage: 665.441
Monoisotopic: 665.124771695
InChI KeyBOPGDPNILDQYTO-UHFFFAOYSA-N
InChIInChI=1S/C21H29N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1,3-4,7-8,10-11,13-16,20-21,29-32H,2,5-6H2,(H2,23,33)(H,34,35)(H,36,37)(H2,22,24,25)
IUPAC Name[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]({[(2R,3S,4R,5R)-5-(3-carbamoyl-1,4-dihydropyridin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy})phosphinic acid
Traditional IUPAC NameNADH
Chemical FormulaC21H29N7O14P2
SMILES[H]OC1([H])C([H])(OC([H])(C([H])([H])OP(=O)(O[H])OP(=O)(O[H])OC([H])([H])C2([H])OC([H])(N3C([H])=C([H])C([H])([H])C(=C3[H])C(=O)N([H])[H])C([H])(O[H])C2([H])O[H])C1([H])O[H])N1C([H])=NC2=C1N=C([H])N=C2N([H])[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as (5'->5')-dinucleotides. These are dinucleotides where the two bases are connected via a (5'->5')-phosphodiester linkage.
KingdomOrganic compounds
Super ClassNucleosides, nucleotides, and analogues
Class(5'->5')-dinucleotides
Sub ClassNot Available
Direct Parent(5'->5')-dinucleotides
Alternative Parents
Substituents
  • (5'->5')-dinucleotide
  • Purine nucleotide sugar
  • Purine ribonucleoside diphosphate
  • Purine ribonucleoside monophosphate
  • Nicotinamide-nucleotide
  • Pentose phosphate
  • Pentose-5-phosphate
  • Glycosyl compound
  • N-glycosyl compound
  • 6-aminopurine
  • Monosaccharide phosphate
  • N-substituted nicotinamide
  • Organic pyrophosphate
  • Imidazopyrimidine
  • Purine
  • Monoalkyl phosphate
  • Dihydropyridine
  • Aminopyrimidine
  • Pyrimidine
  • Imidolactam
  • Monosaccharide
  • N-substituted imidazole
  • Alkyl phosphate
  • Phosphoric acid ester
  • Hydropyridine
  • Organic phosphoric acid derivative
  • Heteroaromatic compound
  • Tetrahydrofuran
  • Imidazole
  • Vinylogous amide
  • Azole
  • Amino acid or derivatives
  • Primary carboxylic acid amide
  • Secondary alcohol
  • Carboxamide group
  • Organoheterocyclic compound
  • Enamine
  • Azacycle
  • Oxacycle
  • Carboxylic acid derivative
  • Hydrocarbon derivative
  • Alcohol
  • Organic nitrogen compound
  • Organonitrogen compound
  • Organooxygen compound
  • Carbonyl group
  • Organic oxygen compound
  • Organopnictogen compound
  • Primary amine
  • Amine
  • Organic oxide
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting point140.0-142.0 °C
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility2.95 g/LALOGPS
logP-1.4ALOGPS
logP-6.5ChemAxon
logS-2.4ALOGPS
pKa (Strongest Acidic)-7ChemAxon
pKa (Strongest Basic)5ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count16ChemAxon
Hydrogen Donor Count8ChemAxon
Polar Surface Area317.62 ŲChemAxon
Rotatable Bond Count11ChemAxon
Refractivity143 m³·mol⁻¹ChemAxon
Polarizability57.65 ųChemAxon
Number of Rings5ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • mitochondrion
  • endoplasmic reticulum
  • peroxisome
  • cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
4-aminobutanoate degradationPW002382 ThumbThumb?image type=greyscaleThumb?image type=simple
Aspartate metabolismPW002375 ThumbThumb?image type=greyscaleThumb?image type=simple
Choline metabolismPW002494 ThumbThumb?image type=greyscaleThumb?image type=simple
Citric Acid CyclePW000952 ThumbThumb?image type=greyscaleThumb?image type=simple
Citric Acid Cycle 1434561204PW000970 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Fatty acid elongation in mitochondriaec00062 Map00062
Fatty acid metabolismec00071 Map00071
Glycerophospholipid metabolismec00564 Map00564
Nitrogen metabolismec00910 Map00910
Oxidative phosphorylationec00190 Map00190
SMPDB Reactions
Pyruvic acid + Coenzyme A + NADAcetyl-CoA + Carbon dioxide + NADH
Isocitric acid + NADOxoglutaric acid + Carbon dioxide + NADH + hydron
Oxoglutaric acid + NAD + Coenzyme ASuccinyl-CoA + NADH + hydron + Carbon dioxide
(S)-Malic acid + NADOxalacetic acid + NADH + hydron
Oxalacetic acid + hydron + NADH(S)-Malic acid + NAD
KEGG Reactions
NAD + (R,R)-butane-2,3-diolNADH + hydron + (R)-Acetoin
water + NAD + 1-Pyrroline-5-carboxylic acidNADH + L-Glutamic acid + hydron
NAD + 2-hydroxybutyric acidNADH + hydron + 2-Ketobutyric acid
NAD + Coenzyme A + 2-Ketobutyric acidNADH + propionyl-CoA + Carbon dioxide
NADH + (4-hydroxyphenyl)pyruvic acid + hydronNAD + 3-(4-hydroxyphenyl)lactic acid
Concentrations
Intracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
70 ± 0 µM Minimal medium supplemented with ammonia saltsaerobic;resting cellsBaker's yeastPMID: 4578278
250 ± 0 µM Minimal medium supplemented with ammonia salts and glucoseaerobic;resting cellsBaker's yeastPMID: 4578278
500 ± 0 µM Minimal medium supplemented with ammonia salts and glucoseanaerobic;resting cellsBaker's yeastPMID: 4578278
1025 ± 775 µM Minimal medium supplemented with ammonia salts and (glucose or galactose)aerobic;growing cellsBaker's yeastPMID: 4578278
Conversion Details Here
Extracellular ConcentrationsNot Available
Spectra
Spectra
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Vuralhan, Z., Morais, M. A., Tai, S. L., Piper, M. D., Pronk, J. T. (2003). "Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae." Appl Environ Microbiol 69:4534-4541.12902239
  • Takada, Y., Noguchi, T. (1985). "Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates." Biochem J 231:157-163.3933486
  • Moreira dos Santos, M., Thygesen, G., Kotter, P., Olsson, L., Nielsen, J. (2003). "Aerobic physiology of redox-engineered Saccharomyces cerevisiae strains modified in the ammonium assimilation for increased NADPH availability." FEMS Yeast Res 4:59-68.14554197
  • Liger, D., Graille, M., Zhou, C. Z., Leulliot, N., Quevillon-Cheruel, S., Blondeau, K., Janin, J., van Tilbeurgh, H. (2004). "Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities." J Biol Chem 279:34890-34897.15184374
  • Saint-Prix, F., Bonquist, L., Dequin, S. (2004). "Functional analysis of the ALD gene family of Saccharomyces cerevisiae during anaerobic growth on glucose: the NADP+-dependent Ald6p and Ald5p isoforms play a major role in acetate formation." Microbiology 150:2209-2220.15256563
  • Amako, K., Fujita, K., Shimohata, T. A., Hasegawa, E., Kishimoto, R., Goda, K. (2006). "NAD+-specific D-arabinose dehydrogenase and its contribution to erythroascorbic acid production in Saccharomyces cerevisiae." FEBS Lett 580:6428-6434.17097644
  • Shi, F., Kawai, S., Mori, S., Kono, E., Murata, K. (2005). "Identification of ATP-NADH kinase isozymes and their contribution to supply of NADP(H) in Saccharomyces cerevisiae." FEBS J 272:3337-3349.15978040
  • Bhattacharjee, J. K. (1985). "alpha-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes." Crit Rev Microbiol 12:131-151.3928261
  • Albertyn, J., Hohmann, S., Thevelein, J. M., Prior, B. A. (1994). "GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway." Mol Cell Biol 14:4135-4144.8196651
  • Gonzalez, E., Fernandez, M. R., Larroy, C., Sola, L., Pericas, M. A., Pares, X., Biosca, J. A. (2000). "Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product. Disruption and induction of the gene." J Biol Chem 275:35876-35885.10938079
  • White, W. H., Skatrud, P. L., Xue, Z., Toyn, J. H. (2003). "Specialization of function among aldehyde dehydrogenases: the ALD2 and ALD3 genes are required for beta-alanine biosynthesis in Saccharomyces cerevisiae." Genetics 163:69-77.12586697
  • Cupp, J. R., McAlister-Henn, L. (1992). "Cloning and characterization of the gene encoding the IDH1 subunit of NAD(+)-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae." J Biol Chem 267:16417-16423.1644826
  • Leskovac, V., Trivic, S., Pericin, D. (2002). "The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae." FEMS Yeast Res 2:481-494.12702265
  • Zabriskie, T. M., Jackson, M. D. (2000). "Lysine biosynthesis and metabolism in fungi." Nat Prod Rep 17:85-97.10714900
  • McAlister, L., Holland, M. J. (1985). "Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenase genes." J Biol Chem 260:15019-15027.3905788
  • Dickinson, J. R., Salgado, L. E., Hewlins, M. J. (2003). "The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae." J Biol Chem 278:8028-8034.12499363
  • Thomas, D., Barbey, R., Surdin-Kerjan, Y. (1993). "Evolutionary relationships between yeast and bacterial homoserine dehydrogenases." FEBS Lett 323:289-293.8500624
  • Hyle, J. W., Shaw, R. J., Reines, D. (2003). "Functional distinctions between IMP dehydrogenase genes in providing mycophenolate resistance and guanine prototrophy to yeast." J Biol Chem 278:28470-28478.12746440
  • Hiltunen, J. K., Mursula, A. M., Rottensteiner, H., Wierenga, R. K., Kastaniotis, A. J., Gurvitz, A. (2003). "The biochemistry of peroxisomal beta-oxidation in the yeast Saccharomyces cerevisiae." FEMS Microbiol Rev 27:35-64.12697341
  • Luttik, M. A., Overkamp, K. M., Kotter, P., de Vries, S., van Dijken, J. P., Pronk, J. T. (1998). "The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH." J Biol Chem 273:24529-24534.9733747
  • Geisbrecht, B. V., Zhu, D., Schulz, K., Nau, K., Morrell, J. C., Geraghty, M., Schulz, H., Erdmann, R., Gould, S. J. (1998). "Molecular characterization of Saccharomyces cerevisiae Delta3, Delta2-enoyl-CoA isomerase." J Biol Chem 273:33184-33191.9837886
  • Albers, E., Laize, V., Blomberg, A., Hohmann, S., Gustafsson, L. (2003). "Ser3p (Yer081wp) and Ser33p (Yil074cp) are phosphoglycerate dehydrogenases in Saccharomyces cerevisiae." J Biol Chem 278:10264-10272.12525494
  • Valenzuela, L., Ballario, P., Aranda, C., Filetici, P., Gonzalez, A. (1998). "Regulation of expression of GLT1, the gene encoding glutamate synthase in Saccharomyces cerevisiae." J Bacteriol 180:3533-3540.9657994
  • Lamb, D. C., Kelly, D. E., Manning, N. J., Kaderbhai, M. A., Kelly, S. L. (1999). "Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction." FEBS Lett 462:283-288.10622712
  • Gancedo, J. M., Gancedo, C. (1973). "Concentrations of intermediary metabolites in yeast." Biochimie 55:205-211.4578278
Synthesis Reference:Marek, Miroslav; Vrbova, Eva; Horakova, Irena; Musil, Petr; Kefurt, Karel. NADH manufacture with immobilized Candida formate dehydrogenase. Czech. (1992), 4 pp.
External Links:
ResourceLink
CHEBI ID16908
HMDB IDHMDB01487
Pubchem Compound ID928
Kegg IDC00004
ChemSpider ID903
FOODB IDFDB022649
WikipediaNicotinamide_adenine_dinucleotide
BioCyc IDNADH

Enzymes

General function:
Involved in catalytic activity
Specific function:
Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate
Gene Name:
GLT1
Uniprot ID:
Q12680
Molecular weight:
238100.0
Reactions
2 L-glutamate + NAD(+) → L-glutamine + 2-oxoglutarate + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
D-arabinose + NAD(+) = D-arabinono-1,4-lactone + NADH
Gene Name:
ARA2
Uniprot ID:
Q04212
Molecular weight:
38220.0
Reactions
D-arabinose + NAD(+) → D-arabinono-1,4-lactone + NADH.
General function:
Involved in iron ion binding
Specific function:
Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
Gene Name:
ERG11
Uniprot ID:
P10614
Molecular weight:
60719.80078
Reactions
Obtusifoliol + 3 O(2) + 3 NADPH → 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP(+) + 4 H(2)O.
General function:
Involved in oxidoreductase activity
Specific function:
Lipoamide dehydrogenase is a component of the alpha- ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine
Gene Name:
LPD1
Uniprot ID:
P09624
Molecular weight:
54009.69922
Reactions
Protein N(6)-(dihydrolipoyl)lysine + NAD(+) → protein N(6)-(lipoyl)lysine + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate
Gene Name:
LYS1
Uniprot ID:
P38998
Molecular weight:
41464.39844
Reactions
N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+) + H(2)O → L-lysine + 2-oxoglutarate + NADH.
General function:
Involved in zinc ion binding
Specific function:
An alcohol + NAD(+) = an aldehyde or ketone + NADH
Gene Name:
ADH3
Uniprot ID:
P07246
Molecular weight:
40369.19922
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H
Gene Name:
ALD2
Uniprot ID:
P47771
Molecular weight:
55187.39844
Reactions
An aldehyde + NAD(P)(+) + H(2)O → an acid + NAD(P)H.
General function:
Involved in zinc ion binding
Specific function:
Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde. Is responsible for yeast resistance to formaldehyde
Gene Name:
SFA1
Uniprot ID:
P32771
Molecular weight:
41041.69922
Reactions
S-(hydroxymethyl)glutathione + NAD(P)(+) → S-formylglutathione + NAD(P)H.
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
An aldehyde + NAD(+) + H(2)O = an acid + NADH
Gene Name:
ALD4
Uniprot ID:
P46367
Molecular weight:
56723.19922
Reactions
An aldehyde + NAD(+) + H(2)O → an acid + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H
Gene Name:
ALD3
Uniprot ID:
P54114
Molecular weight:
55384.80078
Reactions
An aldehyde + NAD(P)(+) + H(2)O → an acid + NAD(P)H.
General function:
Involved in oxidoreductase activity
Specific function:
An aldehyde + NAD(+) + H(2)O = an acid + NADH
Gene Name:
ALD6
Uniprot ID:
P54115
Molecular weight:
54413.69922
Reactions
An aldehyde + NAD(+) + H(2)O → an acid + NADH.
General function:
Involved in zinc ion binding
Specific function:
This isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols
Gene Name:
ADH1
Uniprot ID:
P00330
Molecular weight:
36849.0
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
Minor mitochondrial aldehyde dehydrogenase isoform. Plays a role in regulation or biosynthesis of electron transport chain components. Involved in the biosynthesis of acetate during anaerobic growth on glucose
Gene Name:
ALD5
Uniprot ID:
P40047
Molecular weight:
56620.39844
Reactions
An aldehyde + NAD(+) + H(2)O → an acid + NADH.
An aldehyde + NADP(+) + H(2)O → an acid + NADPH.
General function:
Involved in oxidoreductase activity
Specific function:
Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all
Gene Name:
ADH4
Uniprot ID:
P10127
Molecular weight:
41141.69922
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in zinc ion binding
Specific function:
An alcohol + NAD(+) = an aldehyde or ketone + NADH
Gene Name:
ADH5
Uniprot ID:
P38113
Molecular weight:
37647.89844
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in zinc ion binding
Specific function:
This isozyme preferentially catalyzes the conversion of ethanol to acetaldehyde. Acts on a variety of primary unbranched aliphatic alcohols
Gene Name:
ADH2
Uniprot ID:
P00331
Molecular weight:
36731.60156
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in magnesium ion binding
Specific function:
Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'- untranslated leaders of mitochondrial mRNAs
Gene Name:
IDH1
Uniprot ID:
P28834
Molecular weight:
39323.69922
Reactions
Isocitrate + NAD(+) → 2-oxoglutarate + CO(2) + NADH.
General function:
Involved in magnesium ion binding
Specific function:
Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'- untranslated leaders of mitochondrial mRNAs
Gene Name:
IDH2
Uniprot ID:
P28241
Molecular weight:
39739.0
Reactions
Isocitrate + NAD(+) → 2-oxoglutarate + CO(2) + NADH.
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2)
Gene Name:
POX1
Uniprot ID:
P13711
Molecular weight:
84041.39844
Reactions
Acyl-CoA + O(2) → trans-2,3-dehydroacyl-CoA + H(2)O(2).
General function:
Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Specific function:
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Gene Name:
POT1
Uniprot ID:
P27796
Molecular weight:
44729.89844
Reactions
Acyl-CoA + acetyl-CoA → CoA + 3-oxoacyl-CoA.
General function:
Involved in transferase activity
Specific function:
Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for:[acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
Gene Name:
FAS1
Uniprot ID:
P07149
Molecular weight:
228689.0
Reactions
Acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH → long-chain-acyl-CoA + n CoA + n CO(2) + 2n NAD(+) + 2n NADP(+).
Acetyl-CoA + [acyl-carrier-protein] → CoA + acetyl-[acyl-carrier-protein].
Malonyl-CoA + [acyl-carrier-protein] → CoA + malonyl-[acyl-carrier-protein].
(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] → hexadec-2-enoyl-[acyl-carrier-protein] + H(2)O.
Acyl-[acyl-carrier-protein] + NAD(+) → trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
Oleoyl-[acyl-carrier-protein] + H(2)O → [acyl-carrier-protein] + oleate.
General function:
Involved in magnesium ion binding
Specific function:
Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for:acyl carrier protein, 3- oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl- carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex
Gene Name:
FAS2
Uniprot ID:
P19097
Molecular weight:
206945.0
Reactions
Acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH → long-chain-acyl-CoA + n CoA + n CO(2) + 2n NAD(+) + 2n NADP(+).
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] → 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) → 3-oxoacyl-[acyl-carrier-protein] + NADPH.
General function:
Involved in acyltransferase activity
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2)
Gene Name:
PDA2
Uniprot ID:
P12695
Molecular weight:
51817.5
Reactions
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine → CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
General function:
Involved in oxidoreductase activity
Specific function:
Maintains high levels of reduced glutathione in the cytosol
Gene Name:
GLR1
Uniprot ID:
P41921
Molecular weight:
53440.60156
Reactions
2 glutathione + NADP(+) → glutathione disulfide + NADPH.
General function:
Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific function:
3-phospho-D-glycerate + NAD(+) = 3- phosphonooxypyruvate + NADH
Gene Name:
SER33
Uniprot ID:
P40510
Molecular weight:
51187.80078
Reactions
3-phospho-D-glycerate + NAD(+) → 3-phosphonooxypyruvate + NADH.
2-hydroxyglutarate + NAD(+) → 2-oxoglutarate + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the production and accumulation of glycerol during hyperosmotic stress conditions. Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells
Gene Name:
GPD1
Uniprot ID:
Q00055
Molecular weight:
42868.5
Reactions
sn-glycerol 3-phosphate + NAD(+) → glycerone phosphate + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the production of glycerol under anaerobic growth conditions. Glycerol production serves as a redox sink by consuming the excess cytosolic NADH during anaerobic metabolism
Gene Name:
GPD2
Uniprot ID:
P41911
Molecular weight:
49421.30078
Reactions
sn-glycerol 3-phosphate + NAD(+) → glycerone phosphate + NADH.
General function:
Involved in electron carrier activity
Specific function:
Could be a fumarate reductase
Gene Name:
Not Available
Uniprot ID:
P32614
Molecular weight:
50843.69922
Reactions
Succinate + NAD(+) → fumarate + NADH.
General function:
Involved in FMN reductase activity
Specific function:
Has several reductase activities that are NAD(P)H- dependent and involve FMN as a cofactor, ferricyanide being the best substrate for reduction. May be involved in ferric iron assimilation
Gene Name:
LOT6
Uniprot ID:
Q07923
Molecular weight:
21280.40039
Reactions
FMNH(2) + NAD(P)(+) → FMN + NAD(P)H.
General function:
Involved in zinc ion binding
Specific function:
L-iditol + NAD(+) = L-sorbose + NADH
Gene Name:
SOR1
Uniprot ID:
P35497
Molecular weight:
38165.39844
Reactions
L-iditol + NAD(+) → L-sorbose + NADH.
General function:
Involved in zinc ion binding
Specific function:
L-iditol + NAD(+) = L-sorbose + NADH
Gene Name:
SOR2
Uniprot ID:
Q07786
Molecular weight:
38096.30078
Reactions
L-iditol + NAD(+) → L-sorbose + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
External NADH dehydrogenase required for optimum cellular growth with a number of nonfermentable carbon sources, including ethanol. With NDE1, performes the mitochondrial oxidation of cytosolic NADH under these growth conditions. Regulates the mitochondrial glycerol-3-phosphate dehydrogenase, GUT2, also involved in cytosolic NADH oxydation
Gene Name:
NDE2
Uniprot ID:
Q07500
Molecular weight:
61658.69922
Reactions
NADH + ubiquinone → NAD(+) + ubiquinol.
General function:
Involved in oxidoreductase activity
Specific function:
External NADH dehydrogenase required for optimum cellular growth with a number of nonfermentable carbon sources, including ethanol. With NDE2, performes the mitochondrial oxidation of cytosolic NADH under these growth conditions. Regulates the mitochondrial glycerol-3-phosphate dehydrogenase, GUT2, also involved in cytosolic NADH oxydation
Gene Name:
NDE1
Uniprot ID:
P40215
Molecular weight:
62773.60156
Reactions
NADH + ubiquinone → NAD(+) + ubiquinol.
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the oxidation of NADH generated inside the Mitochondrion
Gene Name:
NDI1
Uniprot ID:
P32340
Molecular weight:
57249.30078
Reactions
NADH + ubiquinone → NAD(+) + ubiquinol.
General function:
Involved in oxidoreductase activity
Specific function:
L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate + NH(3) + NADH
Gene Name:
GDH2
Uniprot ID:
P33327
Molecular weight:
124331.0
Reactions
L-glutamate + H(2)O + NAD(+) → 2-oxoglutarate + NH(3) + NADH.
General function:
Involved in ligase activity
Specific function:
Catalyzes the activation of alpha-aminoadipate by ATP- dependent adenylation and the reduction of activated alpha- aminoadipate by NADPH
Gene Name:
LYS2
Uniprot ID:
P07702
Molecular weight:
155344.0
Reactions
L-2-aminoadipate 6-semialdehyde + NAD(P)(+) + H(2)O → L-2-aminoadipate + NAD(P)H.
General function:
Involved in NAD+ kinase activity
Specific function:
Specifically phosphorylates NAD in the presence of ATP, dATP, or CTP as phosphoryl donors
Gene Name:
UTR1
Uniprot ID:
P21373
Molecular weight:
59468.69922
Reactions
ATP + NAD(+) → ADP + NADP(+).
General function:
Involved in NAD+ kinase activity
Specific function:
Phosphorylates both NADH and NAD(+), with a twofold preference for NADH. Anti-oxidant factor and key source of the cellular reductant NADPH
Gene Name:
POS5
Uniprot ID:
Q06892
Molecular weight:
46246.5
Reactions
ATP + NADH → ADP + NADPH.
General function:
Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific function:
The isoenzyme MDH2 may function primarily in the glyoxylate cycle
Gene Name:
MDH2
Uniprot ID:
P22133
Molecular weight:
40730.39844
Reactions
(S)-malate + NAD(+) → oxaloacetate + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
(S)-malate + NAD(+) = pyruvate + CO(2) + NADH
Gene Name:
MAE1
Uniprot ID:
P36013
Molecular weight:
74375.29688
Reactions
(S)-malate + NAD(+) → pyruvate + CO(2) + NADH.
General function:
Involved in zinc ion binding
Specific function:
Xylitol + NAD(+) = D-xylulose + NADH
Gene Name:
XYL2
Uniprot ID:
Q07993
Molecular weight:
38600.10156
Reactions
Xylitol + NAD(+) → D-xylulose + NADH.
General function:
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Specific function:
D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Gene Name:
TDH1
Uniprot ID:
P00360
Molecular weight:
35749.60156
Reactions
D-glyceraldehyde 3-phosphate + phosphate + NAD(+) → 3-phospho-D-glyceroyl phosphate + NADH.
General function:
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Specific function:
D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Gene Name:
TDH2
Uniprot ID:
P00358
Molecular weight:
35846.60156
Reactions
D-glyceraldehyde 3-phosphate + phosphate + NAD(+) → 3-phospho-D-glyceroyl phosphate + NADH.
General function:
Involved in binding
Specific function:
Catalyzes oxidation of cytoplasmic one-carbon units for purine biosynthesis
Gene Name:
MTD1
Uniprot ID:
Q02046
Molecular weight:
36239.30078
Reactions
5,10-methylenetetrahydrofolate + NAD(+) → 5,10-methenyltetrahydrofolate + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
An aldehyde + NAD(+) + H(2)O = an acid + NADH
Gene Name:
ALD1
Uniprot ID:
P22281
Molecular weight:
59506.80078
Reactions
An aldehyde + NAD(+) + H(2)O → an acid + NADH.
General function:
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Specific function:
D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Gene Name:
TDH3
Uniprot ID:
P00359
Molecular weight:
35746.39844
Reactions
D-glyceraldehyde 3-phosphate + phosphate + NAD(+) → 3-phospho-D-glyceroyl phosphate + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
The outer membrane form may mediate the reduction of outer membrane cytochrome b5, and the soluble inter-membrane space form may transfer electrons from external NADH to cytochrome c, thereby mediating an antimycin-insensitive, energy-coupled oxidation of external NADH by yeast mitochondria. Involved in the reduction of D-erythroascorbyl free radicals
Gene Name:
MCR1
Uniprot ID:
P36060
Molecular weight:
34137.69922
Reactions
NADH + 2 ferricytochrome b5 → NAD(+) + H(+) + 2 ferrocytochrome b5.
General function:
Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific function:
Formate + NAD(+) = CO(2) + NADH
Gene Name:
FDH1
Uniprot ID:
Q08911
Molecular weight:
41714.0
Reactions
Formate + NAD(+) → CO(2) + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
1-(5-phosphoribosyl)-AMP + H(2)O = 1-(5- phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4-carboxamide
Gene Name:
HIS4
Uniprot ID:
P00815
Molecular weight:
87720.5
Reactions
1-(5-phosphoribosyl)-AMP + H(2)O → 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide.
1-(5-phosphoribosyl)-ATP + H(2)O → 1-(5-phosphoribosyl)-AMP + diphosphate.
L-histidinol + H(2)O + 2 NAD(+) → L-histidine + 2 NADH.
General function:
Involved in zinc ion binding
Specific function:
Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH (Potential)
Gene Name:
BDH2
Uniprot ID:
P39713
Molecular weight:
46098.19922
Reactions
(R)-acetoin + NAD(+) → diacetyl + NADH.
General function:
Involved in zinc ion binding
Specific function:
Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH
Gene Name:
BDH1
Uniprot ID:
P39714
Molecular weight:
41537.69922
Reactions
(R)-acetoin + NAD(+) → diacetyl + NADH.
General function:
Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific function:
(S)-malate + NAD(+) = oxaloacetate + NADH
Gene Name:
MDH3
Uniprot ID:
P32419
Molecular weight:
37185.89844
Reactions
(S)-malate + NAD(+) → oxaloacetate + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
Second trifunctional enzyme acting on the beta-oxidation pathway for fatty acids, possessing hydratase-dehydrogenase- epimerase activities. Converts trans-2-enoyl-CoA via D-3- hydroxyacyl-CoA to 3-ketoacyl-CoA
Gene Name:
FOX2
Uniprot ID:
Q02207
Molecular weight:
98702.39844
Reactions
(3R)-3-hydroxyacyl-CoA → (2E)-2-enoyl-CoA + H(2)O.
(R)-3-hydroxyacyl-CoA + NAD(+) → 3-oxoacyl-CoA + NADH.
General function:
Involved in iron ion binding
Specific function:
Required for the uptake of Fe(3+) ions. May participate in the transport of electrons from cytoplasm to an extracellular substrate (Fe(3+) ion) via FAD and heme intermediates. Involved in iron homeostasis
Gene Name:
FRE8
Uniprot ID:
Q12209
Molecular weight:
78947.70313
Reactions
2 Fe(2+) + NAD(+) → 2 Fe(3+) + NADH.
General function:
Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific function:
Formate + NAD(+) = CO(2) + NADH
Gene Name:
FDH2
Uniprot ID:
P0CF35
Molecular weight:
26487.19922
Reactions
Formate + NAD(+) → CO(2) + NADH.
General function:
Involved in magnesium ion binding
Specific function:
Catalyzes the NAD(+)-dependent conversion of homoisocitrate to alpha-ketoadipate
Gene Name:
LYS12
Uniprot ID:
P40495
Molecular weight:
40068.60156
Reactions
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD(+) → 2-oxoadipate + CO(2) + NADH.
General function:
Involved in binding
Specific function:
Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin- 2 into sirohydrochlorin and its subsequent ferrochelation into siroheme
Gene Name:
MET8
Uniprot ID:
P15807
Molecular weight:
31917.40039
Reactions
Precorrin-2 + NAD(+) → sirohydrochlorin + NADH.
Siroheme + 2 H(+) → sirohydrochlorin + Fe(2+).
General function:
Involved in catalytic activity
Specific function:
Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH
Gene Name:
IMD4
Uniprot ID:
P50094
Molecular weight:
56393.5
Reactions
Inosine 5'-phosphate + NAD(+) + H(2)O → xanthosine 5'-phosphate + NADH.
General function:
Involved in catalytic activity
Specific function:
Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH
Gene Name:
IMD3
Uniprot ID:
P50095
Molecular weight:
56584.39844
Reactions
Inosine 5'-phosphate + NAD(+) + H(2)O → xanthosine 5'-phosphate + NADH.
General function:
Involved in catalytic activity
Specific function:
Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH
Gene Name:
IMD2
Uniprot ID:
P38697
Molecular weight:
56529.5
Reactions
Inosine 5'-phosphate + NAD(+) + H(2)O → xanthosine 5'-phosphate + NADH.
General function:
Involved in catalytic activity
Specific function:
Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH
Gene Name:
IMD1
Uniprot ID:
P39567
Molecular weight:
44385.80078
Reactions
Inosine 5'-phosphate + NAD(+) + H(2)O → xanthosine 5'-phosphate + NADH.
General function:
Involved in magnesium ion binding
Specific function:
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate
Gene Name:
LEU2
Uniprot ID:
P04173
Molecular weight:
38952.5
Reactions
(2R,3S)-3-isopropylmalate + NAD(+) → 4-methyl-2-oxopentanoate + CO(2) + NADH.
General function:
Involved in zinc ion binding
Specific function:
NADP-dependent alcohol dehydrogenase with a broad substrate specificity
Gene Name:
ADH7
Uniprot ID:
P25377
Molecular weight:
39348.19922
Reactions
An alcohol + NADP(+) → an aldehyde + NADPH.
General function:
Involved in zinc ion binding
Specific function:
NADP-dependent alcohol dehydrogenase with a broad substrate specificity
Gene Name:
ADH6
Uniprot ID:
Q04894
Molecular weight:
39617.30078
Reactions
An alcohol + NADP(+) → an aldehyde + NADPH.
General function:
Involved in protein complex assembly
Specific function:
Required for the assembly of yeast cytochrome oxidase. Involved in the biosynthesis of heme A and the initial step in this pathway, the hydroxylation of heme O, is thought to be catalyzed by a three-component mono-oxygenase consisting of COX15, ferredoxin and ferredoxin reductase
Gene Name:
COX15
Uniprot ID:
P40086
Molecular weight:
54657.89844
General function:
Involved in oxidoreductase activity
Specific function:
(S)-1-pyrroline-5-carboxylate + NAD(P)(+) + 2 H(2)O = L-glutamate + NAD(P)H
Gene Name:
PUT2
Uniprot ID:
P07275
Molecular weight:
64434.60156
Reactions
(S)-1-pyrroline-5-carboxylate + NAD(P)(+) + 2 H(2)O → L-glutamate + NAD(P)H.
General function:
Involved in proline dehydrogenase activity
Specific function:
Converts proline to delta-1-pyrroline-5-carboxylate
Gene Name:
PUT1
Uniprot ID:
P09368
Molecular weight:
53270.89844
Reactions
L-proline + acceptor → (S)-1-pyrroline-5-carboxylate + reduced acceptor.
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway
Gene Name:
ERG1
Uniprot ID:
P32476
Molecular weight:
55125.39844
Reactions
Squalene + AH(2) + O(2) → (S)-squalene-2,3-epoxide + A + H(2)O.
General function:
Involved in oxidoreductase activity
Specific function:
L-proline + NAD(P)(+) = 1-pyrroline-5- carboxylate + NAD(P)H
Gene Name:
PRO3
Uniprot ID:
P32263
Molecular weight:
30131.59961
Reactions
L-proline + NAD(P)(+) → 1-pyrroline-5-carboxylate + NAD(P)H.
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the NADPH dependent reduction of L-gamma- glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate
Gene Name:
PRO2
Uniprot ID:
P54885
Molecular weight:
49740.0
Reactions
L-glutamate 5-semialdehyde + phosphate + NADP(+) → L-glutamyl 5-phosphate + NADPH.
General function:
Involved in oxidoreductase activity
Specific function:
Not Available
Gene Name:
DSF1
Uniprot ID:
P39941
Molecular weight:
56469.69922
Reactions
D-mannitol + NAD+ → D-fructose + NADH + H+
General function:
Involved in ubiquinone biosynthetic process
Specific function:
Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of COQ3, COQ4, COQ6, COQ7 and COQ9 polypeptides
Gene Name:
COQ4
Uniprot ID:
O13525
Molecular weight:
38626.80078
General function:
Involved in 3-beta-hydroxy-delta5-steroid dehydrogenase activity
Specific function:
3-beta-hydroxy-4-beta-methyl-5-alpha-cholest- 7-ene-4-alpha-carboxylate + NAD(P)(+) = 4-alpha-methyl-5-alpha- cholest-7-en-3-one + CO(2) + NAD(P)H
Gene Name:
ERG26
Uniprot ID:
P53199
Molecular weight:
38706.10156
Reactions
3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)(+) → 4-alpha-methyl-5-alpha-cholest-7-en-3-one + CO(2) + NAD(P)H.
General function:
Involved in oxidoreductase activity
Specific function:
Prephenate + NADP(+) = 4-hydroxyphenylpyruvate + CO(2) + NADPH
Gene Name:
TYR1
Uniprot ID:
P20049
Molecular weight:
50922.89844
Reactions
Prephenate + NADP(+) → 4-hydroxyphenylpyruvate + CO(2) + NADPH.
General function:
Involved in 5-amino-6-(5-phosphoribosylamino)uracil reductase activity
Specific function:
5-amino-6-(5-phosphoribitylamino)uracil + NADP(+) = 5-amino-6-(5-phosphoribosylamino)uracil + NADPH
Gene Name:
RIB7
Uniprot ID:
P33312
Molecular weight:
27116.0
Reactions
5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) → 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH.
General function:
Involved in oxoglutarate dehydrogenase (succinyl-transferring) activity
Specific function:
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components:2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3)
Gene Name:
KGD1
Uniprot ID:
P20967
Molecular weight:
114416.0
Reactions
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine → [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
General function:
Involved in catalytic activity
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2)
Gene Name:
PDB1
Uniprot ID:
P32473
Molecular weight:
40053.19922
Reactions
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine → [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
General function:
Involved in oxidoreductase activity
Specific function:
L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Gene Name:
HOM6
Uniprot ID:
P31116
Molecular weight:
38501.69922
Reactions
L-homoserine + NAD(P)(+) → L-aspartate 4-semialdehyde + NAD(P)H.
General function:
Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific function:
3-phospho-D-glycerate + NAD(+) = 3- phosphonooxypyruvate + NADH
Gene Name:
SER3
Uniprot ID:
P40054
Molecular weight:
51192.80078
Reactions
3-phospho-D-glycerate + NAD(+) → 3-phosphonooxypyruvate + NADH.
2-hydroxyglutarate + NAD(+) → 2-oxoglutarate + NADH.
General function:
Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific function:
(S)-malate + NAD(+) = oxaloacetate + NADH
Gene Name:
MDH1
Uniprot ID:
P17505
Molecular weight:
35649.60156
Reactions
(S)-malate + NAD(+) → oxaloacetate + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
Electron donor reductase for cytochrome b5. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes. Plays a role in bud morphology
Gene Name:
CBR1
Uniprot ID:
P38626
Molecular weight:
31493.59961
Reactions
NADH + 2 ferricytochrome b5 → NAD(+) + H(+) + 2 ferrocytochrome b5.