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CMP-3-deoxy-D-glycerol-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 o...

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Hauptverfasser: Terada, Takaho (VerfasserIn) , Kitajima, Ken (VerfasserIn) , Inoue, Sadako (VerfasserIn) , Koppert, Klaus (VerfasserIn) , Brossmer, Reinhard (VerfasserIn) , Inoue, Yasuo (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: March 1996
In: EJB
Year: 1996, Jahrgang: 236, Heft: 3, Pages: 852-855
ISSN:1432-1033
DOI:10.1111/j.1432-1033.1996.00852.x
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1111/j.1432-1033.1996.00852.x
Verlag, lizenzpflichtig, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1432-1033.1996.00852.x
Volltext
Verfasserangaben:Takaho Terada, Ken Kitajima, Sadako Inoue, Klaus Koppert, Reinhard Brossmer, Yasuo Inoue
Beschreibung
Zusammenfassung: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.
Beschreibung:Elektronische Reproduktion der Druck-Ausgabe 31. August 2004
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Beschreibung:Online Resource
ISSN:1432-1033
DOI:10.1111/j.1432-1033.1996.00852.x

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