KEGG ENZYME: 4.3.1.13

ENZYME: 4.3.1.13

Entry

EC 4.3.1.13                 Enzyme

Name

carbamoyl-serine ammonia-lyase;
O-carbamoyl-L-serine deaminase;
carbamoylserine deaminase;
O-carbamoyl-L-serine ammonia-lyase (pyruvate-forming)

Class

Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases

Sysname

O-carbamoyl-L-serine ammonia-lyase (decarboxylating; pyruvate-forming)

Reaction(IUBMB)

O-carbamoyl-L-serine + H2O = pyruvate + 2 NH3 + CO2 (overall reaction) [RN:R00213];
(1a) O-carbamoyl-L-serine = CO2 + NH3 + 2-aminoprop-2-enoate;
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous);
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)

Reaction(KEGG)

R00213

Substrate

O-carbamoyl-L-serine [CPD:C03015];
H2O [CPD:C00001];
2-aminoprop-2-enoate [CPD:C02218];
2-iminopropanoate [CPD:C20904]

Product

pyruvate [CPD:C00022];
NH3 [CPD:C00014];
CO2 [CPD:C00011];
2-aminoprop-2-enoate [CPD:C02218];
2-iminopropanoate [CPD:C20904]

Comment

A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing CO2, ammonia, and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and a second ammonia molecule. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase.

History

EC 4.3.1.13 created 1976

Reference

1 [PMID:4761084]

Authors

Copper AJ, Meister A.

Title

Enzymatic conversion of O-carbamyl-L-serine to pyruvate and ammonia.

Journal

Biochem Biophys Res Commun 55:780-7 (1973)
DOI:10.1016/0006-291X(73)91212-6

Other DBs

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