A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 4.1.2.46
| Accepted Name |
|---|
| Aliphatic (R)-hydroxynitrile lyase.
|
| Alternative Name(s) |
|---|
| (R)-hydroxynitrile lyase. |
| (R)-oxynitrilase. |
| Reaction catalysed |
|---|
| (2R)-2-hydroxy-2-methylbutanenitrile <=> cyanide + butan-2-one |
| Cofactor(s) |
|---|
| Zn(2+).
|
| Comment(s) |
|---|
- The enzyme catalyzes the stereoselective synthesis of aliphatic (R)-
cyanohydrins.
- No activity toward mandelonitrile and 4-hydroxymandelonitrile.
- Natural substrates for the (R)-oxynitrilase from Linum usitatissimum
are acetone and butan-2-one, which are the building blocks of the
cyanogen glycosides in Linum, linamarin and lotaustralin,
or linustatin and neolinustatin, respectively.
- Formerly EC 4.1.2.37 and EC 4.1.2.39.
|
| Cross-references |
|---|
| BRENDA | 4.1.2.46 |
| EC2PDB | 4.1.2.46 |
| ExplorEnz | 4.1.2.46 |
| PRIAM enzyme-specific profiles | 4.1.2.46 |
| KEGG Ligand Database for Enzyme Nomenclature | 4.1.2.46 |
| IUBMB Enzyme Nomenclature | 4.1.2.46 |
| IntEnz | 4.1.2.46 |
| MEDLINE | Find literature relating to 4.1.2.46 |
| MetaCyc | 4.1.2.46 |
| UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 4.1.2.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-