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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.
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Catalyzed reaction |
D-serine = pyruvate + NH(3).
D-phenylserine = phenylpyruvate + NH(3).
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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 |
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Family |
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Links |
Enzyme (activities) d-aa deaminase
BRENDA (activities) d-aa deaminase
KEGG (pathways) d-aa deaminase
PLPMDB (PLP mutants) d-aa deaminase
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References |
Muramatsu H, Suzuki Y, Imai T, Ueshima S, Ozaki J, Matsui Y, Kato SI, Ohnishi K, Kimoto N, Yamamoto H, Nagata S. (2011) Discovery and characterization of D-phenylserine deaminase from Arthrobacter sp. TKS1 Appl Microbiol Biotechnol 90 159-72. Articles on d-aa.deaminase |
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last changed |
2016/10/05 14:54 |
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