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Abstract

Cytidine monophosphate-N-acetylneuraminic acid hydroxylase (CMP-NeuAc hydroxylase) participates in the hydroxylation reaction of CMP-NeuAc to form CMP-N- glycolylneuraminic acid (CMP-NeuGc). The hydroxylation is carried out by an enzyme complex composed of cytochrome b5, NADH cytochrome b5 reductase, and CMP-NeuAc hydroxylase in the presence of NADH. Other characteristic features of the hydroxylation are that (1) the reaction is a rate-limiting step for the expression of NeuGc; (2) CMP-NeuAc hydroxylase is a soluble and cytosolic protein, but the other enzymes, cytochrome b5 and NADH cytochrome b5 reductase, are endoplasmic reticulum (ER) membrane-bound proteins; and (3) the expression of NeuGc is tissue- and species-specific, and both phenotypes are regulated by CMP-NeuAc hydroxylase.

Keywords

Sialic Acid Microsomal Fraction Acid Hydroxylation Acid Hydroxylase D86324 AF074480 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Akemi Suzuki
    • 1
  1. 1.RIKEN Frontier Research SystemSaitamaJapan

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