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 |
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Description: | Mycothiol S-conjugate amidase. |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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: | |
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Phylogenetic Tree: | |
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 |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Characterization of Mycobacterium tuberculosis mycothiol S-conjugate amidase. | Steffek M, Newton GL, Av-Gay Y, Fahey RC | 2003 Oct 21 | 14556638 |
A novel mycothiol-dependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase. | Newton GL, Av-Gay Y, Fahey RC | 2000 Sep 5 | 10978158 |