Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.39
Description:Streptomycin-6-phosphatase.
Prosite: PDOC00113;
PDB:
PDBScop

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.39
BRENDA Enzyme Link: BRENDA 3.1.3.39
KEGG Enzyme Link: KEGG3.1.3.39
BioCyc Enzyme Link: BioCyc 3.1.3.39
ExPASy Enzyme Link: ExPASy3.1.3.39
EC2PDB Enzyme Link: EC2PDB 3.1.3.39
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.39
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.39
IntEnz Enzyme Link: IntEnz 3.1.3.39
MEDLINE Enzyme Link: MEDLINE 3.1.3.39
MSA:

3.1.3.39;

Phylogenetic Tree:

3.1.3.39;

Uniprot:
M-CSA:
RHEA:10688 H2O + streptomycin 6-phosphate = phosphate + streptomycin
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Streptomycin biosynthesis. Separation and substrate specificities of phosphatases acting on guanidinodeoxy-scyllo-inositol phosphate and streptomycin-(streptidino)phosphate.Walker MS, Walker JB1971 Nov 254331203
Streptomycin biosynthesis and metabolism. Phosphate transfer from dihydrostreptomycin 6-phosphate to inosamines, streptamine, and 2-deoxystreptamine.Walker JB, Skorvaga M1973 Apr 104121457