Streptomycin 6-kinase
From Wikipedia, the free encyclopedia
In enzymology, a streptomycin 6-kinase (EC 2.7.1.72) is an enzyme that catalyzes the chemical reaction
- ATP + streptomycin ADP + streptomycin 6-phosphate
streptomycin 6-kinase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 2.7.1.72 | ||||||||
CAS no. | 37278-11-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
|
Thus, the two substrates of this enzyme are ATP and streptomycin, whereas its two products are ADP and streptomycin 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:streptomycin 6-phosphotransferase. Other names in common use include streptidine kinase, SM 6-kinase, streptomycin 6-kinase (phosphorylating), streptidine kinase (phosphorylating), streptomycin 6-O-phosphotransferase, and streptomycin 6-phosphotransferase. This enzyme participates in streptomycin biosynthesis.