- References
| Name = glutamine-scyllo-inositol transaminase
| EC_number = 2.6.1.50
| CAS_number = 9033-03-8
| IUBMB_EC_number = 2/6/1/50
| GO_code = 0047310
| image =
| width =
| caption =
}}
In enzymology, a glutamine-scyllo-inositol transaminase ({{EC number|2.6.1.50}}) is an enzyme that catalyzes the chemical reaction
L-glutamine + 2,4,6/3,5-pentahydroxycyclohexanone2-oxoglutaramate + 1-amino-1-deoxy-scyllo-inositol
Thus, the two substrates of this enzyme are L-glutamine and 2,4,6/3,5-pentahydroxycyclohexanone, whereas its two products are 2-oxoglutaramate and 1-amino-1-deoxy-scyllo-inositol.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:2,4,6/3,5-pentahydroxycyclohexanone aminotransferase. Other names in common use include glutamine scyllo-inosose aminotransferase, L-glutamine-keto-scyllo-inositol aminotransferase, glutamine-scyllo-inosose transaminase, and L-glutamine-scyllo-inosose transaminase. It employs one cofactor, pyridoxal phosphate.
References
- {{cite journal | vauthors = Walker JB, Walker MS | year = 1969 | title = Streptomycin biosynthesis. Transamination reactions involving inosamines and inosadiamines | journal = Biochemistry | volume = 8 | pages = 763–70 | pmid = 5781017 | doi = 10.1021/bi00831a003 | issue = 3 }}