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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| Main Authors: | , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
March 1996
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| In: |
EJB
Year: 1996, Volume: 236, Issue: 3, Pages: 852-855 |
| ISSN: | 1432-1033 |
| DOI: | 10.1111/j.1432-1033.1996.00852.x |
| Online Access: | 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 
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| Author Notes: | Takaho Terada, Ken Kitajima, Sadako Inoue, Klaus Koppert, Reinhard Brossmer, Yasuo Inoue |
| Summary: | 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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| Item Description: | Elektronische Reproduktion der Druck-Ausgabe 31. August 2004 Gesehen am 27.06.2024 |
| Physical Description: | Online Resource |
| ISSN: | 1432-1033 |
| DOI: | 10.1111/j.1432-1033.1996.00852.x |