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| Accepted Name |
|---|
| 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).
|
| Alternative 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). |
| Alpha-keto-alpha-methylvalerate dehydrogenase. |
| Alpha-ketoisocaproate dehydrogenase. |
| Alpha-ketoisocaproic dehydrogenase. |
| Alpha-ketoisocaproic-alpha-keto-alpha-methylvaleric dehydrogenase. |
| Alpha-ketoisovalerate dehydrogenase. |
| Alpha-oxoisocaproate dehydrogenase. |
| BCKDH. |
| 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 alpha-keto acid dehydrogenase. |
| Branched-chain alpha-oxo acid dehydrogenase. |
| Branched-chain keto acid dehydrogenase. |
| Branched-chain ketoacid dehydrogenase. |
| Dehydrogenase, 2-oxoisovalerate (lipoate). |
| Dehydrogenase, branched chain alpha-keto acid. |
| Reaction catalysed |
|---|
| 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine <=> [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO(2) |
| Cofactor(s) |
|---|
| Thiamine diphosphate.
|
| Comment(s) |
|---|
- 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, which also binds multiple copies
of EC 1.8.1.4.
- It does not act on free lipoamide or lipoyllysine, but only on the
lipoyllysine residue in EC 2.3.1.168.
- Formerly EC 1.2.4.3.
|
| Cross-references |
|---|
| BRENDA | 1.2.4.4 |
| EC2PDB | 1.2.4.4 |
| ExplorEnz | 1.2.4.4 |
| PRIAM enzyme-specific profiles | 1.2.4.4 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.2.4.4 |
| IUBMB Enzyme Nomenclature | 1.2.4.4 |
| IntEnz | 1.2.4.4 |
| MEDLINE | Find literature relating to 1.2.4.4 |
| MetaCyc | 1.2.4.4 |
| UniProtKB/Swiss-Prot |
| P9WIS2, BKDA_MYCTO; | P9WIS3, BKDA_MYCTU; | P9WIS0, BKDB_MYCTO; |
| P9WIS1, BKDB_MYCTU; | Q9LPL5, ODBA1_ARATH; | Q84JL2, ODBA2_ARATH; |
| P37940, ODBA_BACSU; | P11178, ODBA_BOVIN; | O45924, ODBA_CAEEL; |
| Q54M22, ODBA_DICDI; | P12694, ODBA_HUMAN; | Q8HXY4, ODBA_MACFA; |
| P50136, ODBA_MOUSE; | A5A6H9, ODBA_PANTR; | Q9I1M2, ODBA_PSEAE; |
| P09060, ODBA_PSEPU; | P11960, ODBA_RAT; | Q72GU1, ODBA_THET2; |
| Q5SLR4, ODBA_THET8; | Q9SAV3, ODBB1_ARATH; | Q9LDY2, ODBB2_ARATH; |
| P37941, ODBB_BACSU; | P21839, ODBB_BOVIN; | Q55FN7, ODBB_DICDI; |
| P21953, ODBB_HUMAN; | Q6P3A8, ODBB_MOUSE; | Q9I1M1, ODBB_PSEAE; |
| P09061, ODBB_PSEPU; | P35738, ODBB_RAT; | Q72GU2, ODBB_THET2; |
| Q5SLR3, ODBB_THET8; |
|