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Your query returned 5 entries. Printable version
EC | 1.1.1.85 | ||||||||||
Accepted name: | 3-isopropylmalate dehydrogenase | ||||||||||
Reaction: | (2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH + H+ (overall reaction) (1a) (2R,3S)-3-isopropylmalate + NAD+ = (2S)-2-isopropyl-3-oxosuccinate + NADH + H+ (1b) (2S)-2-isopropyl-3-oxosuccinate = 4-methyl-2-oxopentanoate + CO2 (spontaneous) |
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For diagram of leucine biosynthesis, click here | |||||||||||
Other name(s): | β-isopropylmalic enzyme; β-isopropylmalate dehydrogenase; threo-Ds-3-isopropylmalate dehydrogenase; 3-carboxy-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase | ||||||||||
Systematic name: | (2R,3S)-3-isopropylmalate:NAD+ oxidoreductase | ||||||||||
Comments: | The product decarboxylates spontaneously to yield 4-methyl-2-oxopentanoate. | ||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-97-1 | ||||||||||
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EC | 1.2.4.4 | ||||||||||
Accepted name: | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) | ||||||||||
Reaction: | 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 | ||||||||||
For diagram of oxo-acid-dehydrogenase complexes, click here | |||||||||||
Glossary: | dihydrolipoyl group thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium |
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Other name(s): | 2-oxoisocaproate dehydrogenase; 2-oxoisovalerate (lipoate) dehydrogenase; 3-methyl-2-oxobutanoate dehydrogenase (lipoamide); 3-methyl-2-oxobutanoate:lipoamide oxidoreductase (decarboxylating and acceptor-2-methylpropanoylating); α-keto-α-methylvalerate dehydrogenase; α-ketoisocaproate dehydrogenase; α-ketoisocaproic dehydrogenase; α-ketoisocaproic-α-keto-α-methylvaleric dehydrogenase; α-ketoisovalerate dehydrogenase; α-oxoisocaproate dehydrogenase; BCKDH (ambiguous); BCOAD; branched chain keto acid dehydrogenase; branched-chain (-2-oxoacid) dehydrogenase (BCD); branched-chain 2-keto acid dehydrogenase; branched-chain 2-oxo acid dehydrogenase; branched-chain α-keto acid dehydrogenase; branched-chain α-oxo acid dehydrogenase; branched-chain keto acid dehydrogenase; branched-chain ketoacid dehydrogenase; dehydrogenase, 2-oxoisovalerate (lipoate); dehydrogenase, branched chain α-keto acid | ||||||||||
Systematic name: | 3-methyl-2-oxobutanoate:[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-2-methylpropanoylating) | ||||||||||
Comments: | Contains thiamine diphosphate. It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168. | ||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9082-72-8 | ||||||||||
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EC | 2.3.1.182 | ||||||||||
Transferred entry: | (R)-citramalate synthase. Now classified as EC 2.3.3.21, (R)-citramalate synthase. | ||||||||||
EC | 2.3.3.21 | ||||||||||
Accepted name: | (R)-citramalate synthase | ||||||||||
Reaction: | acetyl-CoA + pyruvate + H2O = CoA + (2R)-2-hydroxy-2-methylbutanedioate | ||||||||||
Glossary: | (2R)-2-hydroxy-2-methylbutanedioate = (2R)-2-methylmalate = (–)-citramalate 3-methyl-2-oxobutanoate = α-ketoisovalerate 2-oxobutanoate = α-ketobutyrate 4-methyl-2-oxopentanoate = α-ketoisocaproate 2-oxohexanoate = α-ketopimelate 2-oxoglutarate = α-ketoglutarate |
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Other name(s): | CimA | ||||||||||
Comments: | One of the enzymes involved in a pyruvate-derived pathway for isoleucine biosynthesis that is found in some bacterial and archaeal species [1,2]. The enzyme can be inhibited by isoleucine, the end-product of the pathway, but not by leucine [2]. The enzyme is highly specific for pyruvate as substrate, as the 2-oxo acids 3-methyl-2-oxobutanoate, 2-oxobutanoate, 4-methyl-2-oxopentanoate, 2-oxohexanoate and 2-oxoglutarate cannot act as substrate [1,2]. | ||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||
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EC | 2.6.1.28 | ||||||||||
Accepted name: | tryptophan—phenylpyruvate transaminase | ||||||||||
Reaction: | L-tryptophan + phenylpyruvate = (indol-3-yl)pyruvate + L-phenylalanine | ||||||||||
For diagram of reaction, click here and for mechanism, click here | |||||||||||
Other name(s): | L-tryptophan-α-ketoisocaproate aminotransferase | ||||||||||
Systematic name: | L-tryptophan:phenylpyruvate aminotransferase | ||||||||||
Comments: | Valine, leucine and isoleucine can replace tryptophan as amino donor. | ||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-87-5 | ||||||||||
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