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:3.5.1.101
Description:L-proline amide hydrolase.
Alternative Name: S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase.
L-amino acid amidase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.101
BRENDA Enzyme Link: BRENDA 3.5.1.101
KEGG Enzyme Link: KEGG3.5.1.101
BioCyc Enzyme Link: BioCyc 3.5.1.101
ExPASy Enzyme Link: ExPASy3.5.1.101
EC2PDB Enzyme Link: EC2PDB 3.5.1.101
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.101
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.101
IntEnz Enzyme Link: IntEnz 3.5.1.101
MEDLINE Enzyme Link: MEDLINE 3.5.1.101
MSA:

3.5.1.101;

Phylogenetic Tree:

3.5.1.101;

Uniprot:
M-CSA:
RHEA:26550 (S)-piperazine-2-carboxamide + H2O = (S)-piperazine-2-carboxylate + NH4(+)
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[NH2;+0:4].[OH2;+0:5]>>[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:5].[NH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase from Pseudomonas azotoformans IAM 1603 is a novel L-amino acid amidase.Komeda H, Harada H, Washika S, Sakamoto T, Ueda M, Asano Y2004 Apr15066172

RHEA:26510 H2O + L-prolinamide = L-proline + NH4(+)
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[NH2;+0:4].[OH2;+0:5]>>[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:5].[NH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase from Pseudomonas azotoformans IAM 1603 is a novel L-amino acid amidase.Komeda H, Harada H, Washika S, Sakamoto T, Ueda M, Asano Y2004 Apr15066172