N-acetylhexosamine 1-kinase
(Redirected from ATP:N-acetyl-D-hexosamine 1-phosphotransferase)
| N-acetylhexosamine 1-kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.162 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| 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.[1] This enzyme catalyses the following chemical reaction
- ATP + N-acetyl-D-hexosamine ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
This enzyme is involved in the lacto-N-biose I/galacto-N-biose degradation pathway in the probiotic bacterium Bifidobacterium longum.
References
[edit]- ^ 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. doi:10.1128/aem.01425-07. PMC 2075035. PMID 17720833.
External links
[edit]- N-acetylhexosamine+1-kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
