| blasticidin-S deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.4.23 | ||||||||
| CAS no. | 54576-55-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a blasticidin-S deaminase (EC 3.5.4.23) is an enzyme that catalyzes the chemical reaction
- blasticidin S + H2O deaminohydroxyblasticidin S + NH3
deaminohydroxyblasticidin S + NH3Thus, the two substrates of this enzyme are blasticidin S and H2O, whereas its two products are deaminohydroxyblasticidin S and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is blasticidin-S aminohydrolase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1WN5 and 1WN6.
References
- Yamaguchi I, Shibata H, Seto H, Misato T (January 1975). "Isolation and purification of blasticidin S deaminase from Aspergillus terreus". J. Antibiot. 28 (1). Tokyo: 7–14. doi:10.7164/antibiotics.28.7. PMID 236272.
| Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
|---|---|
| 3.5.1: Linear amides / Amidohydrolases | |
| 3.5.2: Cyclic amides/ Amidohydrolases | |
| 3.5.3: Linear amidines/ Ureohydrolases | |
| 3.5.4: Cyclic amidines/ Aminohydrolases | |
| 3.5.5: Nitriles/ Aminohydrolases | |
| 3.5.99: Other | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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