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CMP–3‐Deoxy‐ d ‐ Glycerol ‐ d ‐ Galacto ‐Nonulosonic Acid (CMP‐Kdn) Synthetase
Author(s) -
Terada Takaho,
Kitajima Ken,
Inoue Sadako,
Koppert Klaus,
Brossmer Reinhard,
Inoue Yasuo
Publication year - 1996
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1996.00852.x
Subject(s) - chemistry , enzyme , substrate (aquarium) , stereochemistry , biochemistry , rainbow trout , glycerol , substrate specificity , trout , fish <actinopterygii> , biology , fishery , ecology
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.

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