Substrate specificity of rainbow trout testis CMP-3-deoxy-D-glycero-D-galacto-nonulosonic acid (CMP-Kdn) synthetase: kinetic studies of the reaction of natural and synthetic analogues of nonulosonic acid catalyzed by CMP-Kdn synthetase.
In this report we present kinetic data of the activation reaction of several synthetic 3-deoxy-D-glycero-D-galacto-nonulosonic acid (Kdn) and N-acetylneuraminic acid (Neu5Ac) analogues catalyzed by the rainbow trout testis CMP-Kdn synthetase. This enzyme showed broad substrate specificity in terms of substitutions at C4 or C5 position of Kdn and Neu5Ac. In contrast, calf brain CMP-N-acylneuraminic acid synthetase had narrow substrate specificity, being active only on various N-acyl analogues of Neu5Ac and only slightly active on Kdn derivatives. Usefulness of the trout testis enzyme for synthesis of various CMP-sialate analogues, which could be donor substrates for sialyltransferases, was demonstrated.
Terada
T
T
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
Kitajima
K
K
Inoue
S
S
Koppert
K
K
Brossmer
R
R
Inoue
Y
Y
D000818:Animals; D001921:Brain / Q000201:enzymology; D002236:Carbohydrate Conformation; D002417:Cattle; D007700:Kinetics; D008297:Male; D015394:Molecular Structure; D009713:Nucleotidyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D017686:Oncorhynchus mykiss; D012794:Sialic Acids / Q000378:metabolism; D013379:Substrate Specificity; D013400:Sugar Acids / Q000737:chemistry / Q000378:metabolism; D013737:Testis / Q000201:enzymology*
D012794:Sialic Acids; D013400:Sugar Acids; C079494:CTP-CMP-3-deoxynonulosonate cytidyltransferase; D009713:Nucleotidyltransferases