|
|
d-aa deaminase |
Description |
beta-hydroxy D-amino acid ammonia-lyase (4.3.1.-) |
Alternative names |
beta-hydroxy D-amino acid deaminase;
D-serine deaminase;
D-phenylserine deaminase;
beta-hydroxy D-amino acid acid dehydratase.
|
Catalyzed reaction |
D-serine = pyruvate + NH(3).
D-phenylserine = phenylpyruvate + NH(3).
|
Cofactor |
Pyridoxal-phosphate and Zn(II). |
Comments |
A pyridoxal-phosphate protein that is activated by divalent metal cations (e.g., Zn2+, Cu2+ or Co2+).
The enzyme acts on the D-forms of β-hydroxy-α-amino acids, such as D-serine, D-threo-phenylserine and D-threonine. |
Organisms |
-Eubacteria |
| |
Family |
|
| |
Links |
Enzyme (activities) d-aa deaminase
BRENDA (activities) d-aa deaminase
KEGG (pathways) d-aa deaminase
PLPMDB (PLP mutants) d-aa deaminase
|
| |
References |
Articles on d-aa.deaminase |
| |
last changed |
2016/10/05 14:54 |
|