EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.320 | enzyme KRED1-Pglu, X-ray diffraction structure determination and analysis at 1.77 A resolution | Ogataea glucozyma |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.320 | benzil + NADPH + H+ | Ogataea glucozyma | - |
(S)-benzoin + NADP+ | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.320 | Ogataea glucozyma | A0A0H4SN47 | Pichia glucozyma | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.320 | benzil + NADPH + H+ | - |
Ogataea glucozyma | (S)-benzoin + NADP+ | - |
r | |
1.1.1.320 | additional information | the enzyme is preferentiallly active on aromatic 1,2-diketones. It catalyzes the stereoselective monoreduction and desymmerization of bulky dicarbonyls. Mechanism and in silico prediction of substrates reactivity, overview | Ogataea glucozyma | ? | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.320 | benzil reductase | - |
Ogataea glucozyma |
1.1.1.320 | KRED1-Pglu | - |
Ogataea glucozyma |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.320 | NADP+ | - |
Ogataea glucozyma | |
1.1.1.320 | NADPH | - |
Ogataea glucozyma |