N-acylmannosamine kinase
| N-acylmannosamine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 N-acetylmannosamine kinase dimer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.1.60 | ||||||||
| CAS no. | 9027-53-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
N-acylmannosamine kinase (EC 2.7.1.60) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from rat liver and Salmonella typhimurium converts N-acetylmannosamine to N-acetyl-D-mannosamine 6-phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1][2] The enzyme also accepts N-acyl derivatives other than N-acetyl, which are part of biochemical pathways to sialic acids.[3]
This enzyme is a transferase, specifically one 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.[4]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 2AA4.
References
- ↑ Ghosh, Sudhamoy; Roseman, Saul (1961). "Enzymatic Phosphorylation of N-Acetyl-D-Mannosamine". Proceedings of the National Academy of Sciences. 47 (7): 955–958. doi:10.1073/pnas.47.7.955. PMC 221308. PMID 13704957.
- ↑ Banerjee, S.; Ghosh, S. (1969). "Purification and Properties of N-Acetylmannosamine Kinase from Salmonella typhimurium". European Journal of Biochemistry. 8 (2): 200–206. doi:10.1111/j.1432-1033.1969.tb00515.x. PMID 4889177.
- ↑ Kundig, Werner; Ghosh, Sudhamoy; Roseman, Saul (1966). "The Sialic Acids". Journal of Biological Chemistry. 241 (23): 5619–5626. doi:10.1016/S0021-9258(18)96389-1.
- ↑ Enzyme 2.7.1.60 at KEGG Pathway Database.
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