Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.77
Description:N-carbamoyl-D-amino-acid hydrolase.
Alternative Name: N-carbamoylase.
N-carbamoyl-D-amino acid hydrolase.
D-N-carbamoylase.
Cath: 3.30.70.360; 3.40.630.10; 3.60.110.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.77
BRENDA Enzyme Link: BRENDA 3.5.1.77
KEGG Enzyme Link: KEGG3.5.1.77
BioCyc Enzyme Link: BioCyc 3.5.1.77
ExPASy Enzyme Link: ExPASy3.5.1.77
EC2PDB Enzyme Link: EC2PDB 3.5.1.77
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.77
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.77
IntEnz Enzyme Link: IntEnz 3.5.1.77
MEDLINE Enzyme Link: MEDLINE 3.5.1.77
MSA:

3.5.1.77;

Phylogenetic Tree:

3.5.1.77;

Uniprot:
M-CSA:
RHEA:11000 an N-carbamoyl-D-amino acid + 2 H(+) + H2O = a D-amino acid + CO2 + NH4(+)
RULE(radius=1) [*:1]-[NH;+0:2]-[C;H0;+0:3](=[*:4])-[NH2;+0:5].[H+;H0:6].[H+;H0:7].[OH2;+0:8]>>[*:1]-[NH2;+0:2].[*:4]=[C;H0;+0:3]=[O;H0;+0:8].[NH3;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
N-carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c purification and characterization.Ogawa J, Shimizu S, Yamada H1993 Mar 158462543
Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids.Altenbuchner J, Siemann-Herzberg M, Syldatk C2001 Dec11849938