EC number:3.5.1.72

Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.72
Description:D-benzoylarginine-4-nitroanilide amidase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.72
BRENDA Enzyme Link: BRENDA 3.5.1.72
KEGG Enzyme Link: KEGG3.5.1.72
BioCyc Enzyme Link: BioCyc 3.5.1.72
ExPASy Enzyme Link: ExPASy3.5.1.72
EC2PDB Enzyme Link: EC2PDB 3.5.1.72
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.72
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.72
IntEnz Enzyme Link: IntEnz 3.5.1.72
MEDLINE Enzyme Link: MEDLINE 3.5.1.72

EC number:3.5.1.72

MSA:

3.5.1.72;
Phylogenetic Tree:

3.5.1.72;
Uniprot:
M-CSA:
RHEA:14421 H2O + N(2)-benzoyl-D-arginine-4-nitroanilide = 4-nitroaniline + H(+) + N(2)-benzoyl-D-arginine
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[NH2;+0:4]
Reaction
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References

TitleAuthorsDatePubMed ID
Bacteria of the genus Bacillus have a hydrolase stereospecific to the D isomer of benzoyl-arginine-p-nitroanilide.Gofshtein-Gandman LV, Keynan A, Milner Y1988 Dec3142860