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In enzymology, a glutamine-scyllo-inositol transaminase (EC 2.6.1.50) is an enzyme that catalyzes the chemical reaction

L-glutamine + 2,4,6/3,5-pentahydroxycyclohexanone ${\displaystyle \rightleftharpoons }$ 2-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

• Walker JB, Walker MS (1969). "Streptomycin biosynthesis. Transamination reactions involving inosamines and inosadiamines". Biochemistry. 8 (3): 763–70. doi:10.1021/bi00831a003. PMID 5781017.

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