EC Tree |
3. Hydrolases |
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
3.5.2 In cyclic amides |
ID: | 3.5.2.19 |
---|---|
Description: | Streptothricin hydrolase. |
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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 3.5.2.19 |
BRENDA Enzyme Link: | BRENDA 3.5.2.19 |
KEGG Enzyme Link: | KEGG3.5.2.19 |
BioCyc Enzyme Link: | BioCyc 3.5.2.19 |
ExPASy Enzyme Link: | ExPASy3.5.2.19 |
EC2PDB Enzyme Link: | EC2PDB 3.5.2.19 |
ExplorEnz Enzyme Link: | ExplorEnz 3.5.2.19 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.5.2.19 |
IntEnz Enzyme Link: | IntEnz 3.5.2.19 |
MEDLINE Enzyme Link: | MEDLINE 3.5.2.19 |
RHEA:28142 | H2O + streptothricin D = streptothricin D acid |
RULE(radius=1) | ([*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[NH2;+0:6])>>[*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:6]-[*:5].[OH2;+0:4] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
The biological function of the bacterial isochorismatase-like hydrolase SttH. | Maruyama C, Hamano Y | 2009 Nov | 19897889 |
A novel enzyme conferring streptothricin resistance alters the toxicity of streptothricin D from broad-spectrum to bacteria-specific. | Hamano Y, Matsuura N, Kitamura M, Takagi H | 2006 Jun 23 | 16641084 |
RHEA:28138 | H2O + streptothricin F = streptothricin F acid |
RULE(radius=1) | ([*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[NH2;+0:6])>>[*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:6]-[*:5].[OH2;+0:4] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
The biological function of the bacterial isochorismatase-like hydrolase SttH. | Maruyama C, Hamano Y | 2009 Nov | 19897889 |
A novel enzyme conferring streptothricin resistance alters the toxicity of streptothricin D from broad-spectrum to bacteria-specific. | Hamano Y, Matsuura N, Kitamura M, Takagi H | 2006 Jun 23 | 16641084 |