Enzyme

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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.

3D structure

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References

External Links

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
MSA:

3.5.2.19;

Phylogenetic Tree:

3.5.2.19;

Uniprot:
M-CSA:
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 More

References

TitleAuthorsDatePubMed ID
The biological function of the bacterial isochorismatase-like hydrolase SttH.Maruyama C, Hamano Y2009 Nov19897889
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 H2006 Jun 2316641084

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 More

References

TitleAuthorsDatePubMed ID
The biological function of the bacterial isochorismatase-like hydrolase SttH.Maruyama C, Hamano Y2009 Nov19897889
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 H2006 Jun 2316641084