CMP-N-acylneuraminate phosphodiesterase

CMP-N-acylneuraminate phosphodiesterase

In enzymology, a CMP-N-acylneuraminate phosphodiesterase (EC number|3.1.4.40) is an enzyme that catalyzes the chemical reaction

:CMP-N-acylneuraminate + H2O ightleftharpoons CMP + N-acylneuraminate

Thus, the two substrates of this enzyme are CMP-N-acylneuraminate and H2O, whereas its two products are CMP and N-acylneuraminate.

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is CMP-N-acylneuraminate N-acylneuraminohydrolase. Other names in common use include CMP-sialate hydrolase, CMP-sialic acid hydrolase, CMP-N-acylneuraminic acid hydrolase, cytidine monophosphosialic hydrolase, cytidine monophosphosialate hydrolase, cytidine monophosphate-N-acetylneuraminic acid hydrolase, and CMP-N-acetylneuraminate hydrolase.

References

*

External links

::"The CAS registry number for this enzyme class is CAS registry|55326-41-5."

Gene Ontology (GO) codes


Wikimedia Foundation. 2010.

Игры ⚽ Нужно сделать НИР?

Look at other dictionaries:

  • Hydrolase — Cristal de lysozyme Les hydrolases constituent une classe d enzymes qui catalysent les réactions d hydrolyse de molécules suivant la réaction générale : R R + H2O ⇌ R OH + R H On y trouve par exemple les estérases, qui hydrolysent les …   Wikipédia en Français

  • EC 3.1 — Le groupe EC3.1 est un groupe d hydrolases rassemblant les estérases, c est à dire les enzymes catalysant la réaction générale : R O R + H2O ⇌ R OH + R OH où R représente un acide quelconque et R son substrat. En fonction du milieu, l ester… …   Wikipédia en Français

  • List of EC numbers (EC 3) — This list contains a list of EC numbers for the third group, EC 3, hydrolases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.EC 3.1: Acting on Ester BondsEC… …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”