N-acetylhexosamine 1-kinase
| N-acetylhexosamine 1-kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.162 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
N-acetylhexosamine 1-kinase (EC 2.7.1.162, NahK, LnpB, N-acetylgalactosamine/N-acetylglucosamine 1-kinase) is an enzyme with systematic name ATP:N-acetyl-D-hexosamine 1-phosphotransferase. This enzyme catalyses the two related chemical reaction that use adenosine triphosphate (ATP) to transfer a phosphate group to a hexose sugar.[1]
- ATP + N-acetyl-D-hexosamine ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
For example, the enzyme characterised from Bifidobacterium longum converts N-acetyl-D-glucosamine to N-acetyl-α-D-glucosamine 1-phosphate:[1]
Similarly, N-acetylgalactosamine is converted to N-acetyl-α-D-galactosamine 1-phosphate:
The enzyme is involved in the lacto-N-biose I/galacto-N-biose degradation pathway in this probiotic bacterium. It differs from N-acetylgalactosamine kinase, since it can phosphorylate both N-acetylgalactosamine and N-acetylglucosamine at similar rates and is active on some other sugars.[1][2]
References
- 1 2 3 Nishimoto M, Kitaoka M (October 2007). "Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum". Applied and Environmental Microbiology. 73 (20): 6444–9. Bibcode:2007ApEnM..73.6444N. doi:10.1128/aem.01425-07. PMC 2075035. PMID 17720833.
- ↑ Enzyme 2.7.1.162 at KEGG Pathway Database.
External links
- N-acetylhexosamine+1-kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Category: