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:3.5.1.115
Description:Mycothiol S-conjugate amidase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.115
BRENDA Enzyme Link: BRENDA 3.5.1.115
KEGG Enzyme Link: KEGG3.5.1.115
BioCyc Enzyme Link: BioCyc 3.5.1.115
ExPASy Enzyme Link: ExPASy3.5.1.115
EC2PDB Enzyme Link: EC2PDB 3.5.1.115
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.115
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.115
IntEnz Enzyme Link: IntEnz 3.5.1.115
MEDLINE Enzyme Link: MEDLINE 3.5.1.115
MSA:

3.5.1.115;

Phylogenetic Tree:

3.5.1.115;

Uniprot:
M-CSA:
RHEA:36543 H2O + mycothiol S-conjugate = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + an N-acetyl-L-cysteine-S-conjugate
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:5]-[NH2;+0:4].[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Characterization of Mycobacterium tuberculosis mycothiol S-conjugate amidase.Steffek M, Newton GL, Av-Gay Y, Fahey RC2003 Oct 2114556638
A novel mycothiol-dependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase.Newton GL, Av-Gay Y, Fahey RC2000 Sep 510978158