N-acylneuraminate-9-phosphatase
From Wikipedia, the free encyclopedia
In enzymology, a N-acylneuraminate-9-phosphatase (EC 3.1.3.29) is an enzyme that catalyzes the chemical reaction
- N-acylneuraminate 9-phosphate + H2O
N-acylneuraminate + phosphate
Thus, the two substrates of this enzyme are N-acylneuraminate 9-phosphate and H2O, whereas its two products are N-acylneuraminate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is N-acylneuraminate-9-phosphate phosphohydrolase. Other names in common use include acylneuraminate 9-phosphatase, N-acylneuraminic acid 9-phosphate phosphatase, and N-acylneuraminic (sialic) acid 9-phosphatase. This enzyme participates in aminosugars metabolism.
[edit] References
- IUBMB entry for 3.1.3.29
- BRENDA references for 3.1.3.29 (Recommended.)
- PubMed references for 3.1.3.29
- PubMed Central references for 3.1.3.29
- Google Scholar references for 3.1.3.29
- Jourdian GW, Swanson A, Watson D and Roseman S (1966). "N-Acetylneuraminic (sialic) acid 9-phosphatase". Methods Enzymol. 8: 205–208.
[edit] External links
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- The CAS registry number for this enzyme class is 37288-13-4.

