N-acylmannosamine kinase
N-acetylmannosamine kinase dimer, Human
Identifiers
EC no.2.7.1.60
CAS no.9027-53-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a N-acylmannosamine kinase (EC 2.7.1.60) is an enzyme that catalyzes the chemical reaction

ATP + N-acyl-D-mannosamine ADP + N-acyl-D-mannosamine 6-phosphate

Thus, the two substrates of this enzyme are ATP and N-acyl-D-mannosamine, whereas its two products are ADP and N-acyl-D-mannosamine 6-phosphate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:N-acyl-D-mannosamine 6-phosphotransferase. Other names in common use include acylmannosamine kinase (phosphorylating), acetylamidodeoxymannokinase, acetylmannosamine kinase, acylaminodeoxymannokinase, acylmannosamine kinase, N-acyl-D-mannosamine kinase, N-acetylmannosamine kinase, and ATP:N-acetylmannosamine 6-phosphotransferase. This enzyme participates in aminosugars metabolism.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2AA4.

References

    • Banerjee S, Ghosh S (1969). "Purification and properties of N-acetylmannosamine kinase from Salmonella typhimurium". Eur. J. Biochem. 8 (2): 200–6. doi:10.1111/j.1432-1033.1969.tb00515.x. PMID 4889177.
    • GHOSH S, ROSEMAN S (1961). "Enzymatic phosphorylation of N-acetyl-D-mannosamine". Proc. Natl. Acad. Sci. U.S.A. 47 (7): 955–8. doi:10.1073/pnas.47.7.955. PMC 221308. PMID 13704957.
    • Kundig W, Ghosh S, Roseman S (1966). "The sialic acids. VII. N-acyl-D-mannosamine kinase from rat liver". J. Biol. Chem. 241 (23): 5619–26. doi:10.1016/S0021-9258(18)96389-1. PMID 5928201.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.