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ENZYME entry: EC 1.1.1.110
| Accepted Name |
|---|
| Aromatic 2-oxoacid reductase.
|
| Alternative Name(s) |
|---|
| (R)-4-hydroxyphenyllactate dehydrogenase. |
| (R)-aromatic lactate dehydrogenase. |
| Indole-3-lactate dehydrogenase. |
| Indolelactate dehydrogenase. |
| Reaction catalysed |
|---|
- (R)-3-(phenyl)lactate + NAD(+) <=> 3-phenyl-2-oxopropanoate + NADH
- (R)-3-(4-hydroxyphenyl)lactate + NAD(+) <=> 3-(4-hydroxyphenyl)pyruvate + NADH
- (Indol-3-yl)lactate + NAD(+) <=> (indol-3-yl)pyruvate + NADH
|
| Comment(s) |
|---|
- The enzymes from anaerobic bacteria such as Clostridium sporogenes
participate in the fermentation pathways of L-phenylalanine,
L-tyrosine and L-tryptophan.
- The enzyme from the yeast Candida maltosa has similar activity, but,
unlike the bacterial enzyme, requires Mn(2+) and can also use NADPH
with lower activity.
- Formerly EC 1.1.1.222.
|
| Cross-references |
|---|
| BRENDA | 1.1.1.110 |
| EC2PDB | 1.1.1.110 |
| ExplorEnz | 1.1.1.110 |
| PRIAM enzyme-specific profiles | 1.1.1.110 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.1.1.110 |
| IUBMB Enzyme Nomenclature | 1.1.1.110 |
| IntEnz | 1.1.1.110 |
| MEDLINE | Find literature relating to 1.1.1.110 |
| MetaCyc | 1.1.1.110 |
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All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-