Function
Proposed Functions
- Hydrolase Activity
- Magnesium Ion Binding
- N-acylneuraminate-9-phosphatase Activity
- Phosphoglycolate Phosphatase Activity
3. N-acylneuraminate-9-phosphatase Activity
4. Phosphoglycolate Phosphatase Activity
Catalytic activity | N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate |
Cofactor | Magnesium (By similarity) |
Enzyme regulation | Inhibited by vanadate and calcium (By similarity) |
Pathway | Carbohydrate metabolism; aminosugar metabolism |
Similarity | Belongs to the haloacid dehalogenase-like hydrolase superfamily. NANP family |
GO Terms
Polymer: haloacid dehalogenase-like hydrolase domain containing 4
Molecular Function: None
Biological Process: None
Cellular Component: None
info
N-acetylneuraminic acid phosphatase
Homologous to mouse (Mus musculus)
Haloacid Dehalogenase Like Hydrolase Domain Containing 4
Classified as Hydrolase
Infomation on ProFunc (useful 2gfhA)
Information on PDBsum (2gfh)
From FASTA most likely function is N-acetylneuraminic acid phosphatase.
The haloalkanoate dehalogenase superfamily (HADSF) is one of the largest and most ubiquitous enzyme families identified to date, with over 3,000 members in organisms ranging from bacteria to humans. Remarkable diversity of chemistry and function has emerged through evolution of the HAD catalytic scaffold. Despite the name, the dehalogenases, which catalyze carbon group transfer, represent a minute fraction of the family. All other known catalytic activities are directed at phosphoryl transfer. Numerous proteins from the HADSF are found in each organism (29 in E. coli and 58 in humans, for example) where they perform a diverse collection of novel physiological functions in primary and secondary metabolism, membrane transport, signal transduction, and nucleic acid repair. http://biophysics.bumc.bu.edu/faculty/allen/allenpage/had.htm
Haloacid dehalogenases (E.C.3.8.1.2) are members of the haloacid dehalogenase superfamily, which also contains ATPases, phosphatases and epoxide hydrolases. They catalyse the conversion of α-halo-carboxylic acids to the corresponding hydroxyalkanoic acid by nucleophilic attack on the α-carbon by a conserved aspartic acid residue to form an ester intermediate, which is then further hydrolysed by a water molecule. There are three subtypes of haloacid dehalogenase based on substrate specificity; those that can use both enantiomers as substrates, those that act only on the L enantiomer and those that act only on the D enantiomer.
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