EC number:3.5.1.86

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:3.5.1.86
Description:Mandelamide amidase.
Alternative Name: Mandelamide hydrolase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.86
BRENDA Enzyme Link: BRENDA 3.5.1.86
KEGG Enzyme Link: KEGG3.5.1.86
BioCyc Enzyme Link: BioCyc 3.5.1.86
ExPASy Enzyme Link: ExPASy3.5.1.86
EC2PDB Enzyme Link: EC2PDB 3.5.1.86
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.86
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.86
IntEnz Enzyme Link: IntEnz 3.5.1.86
MEDLINE Enzyme Link: MEDLINE 3.5.1.86

EC number:3.5.1.86

MSA:

3.5.1.86;
Phylogenetic Tree:

3.5.1.86;
Uniprot:
M-CSA:
RHEA:22876 (R)-mandelamide + H2O = (R)-mandelate + 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
Using directed evolution to probe the substrate specificity of mandelamide hydrolase.Wang PF, Yep A, Kenyon GL, McLeish MJ2009 Feb19074156
Production of R-(-)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750.Yamamoto K, Oishi K, Fujimatsu I, Komatsu K1991 Oct1660699
Mandelamide hydrolase from Pseudomonas putida: characterization of a new member of the amidase signature family.Gopalakrishna KN, Stewart BH, Kneen MM, Andricopulo AD, Kenyon GL, McLeish MJ2004 Jun 2215196015
Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633.McLeish MJ, Kneen MM, Gopalakrishna KN, Koo CW, Babbitt PC, Gerlt JA, Kenyon GL2003 Apr12670968