EC |
2.7.1.52 |
Accepted name: |
fucokinase |
Reaction: |
ATP + L-fucose = ADP + β-L-fucose 1-phosphate |
|
For diagram of GDP-L-fucose and GDP-mannose biosynthesis, click here |
Other name(s): |
fucokinase (phosphorylating); fucose kinase; L-fucose kinase; L-fucokinase; ATP:6-deoxy-L-galactose 1-phosphotransferase; ATP:L-fucose 1-phosphotransferase |
Systematic name: |
ATP:β-L-fucose 1-phosphotransferase |
Comments: |
Requires a divalent cation for activity, with Mg2+ and Fe2+ giving rise to the highest enzyme activity. Forms part of a salvage pathway for reutilization of L-fucose. Can also phosphorylate D-arabinose, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 37278-00-5 |
References: |
1. |
Ishihara, H., Massaro, D.J. and Heath, E.C. The metabolism of L-fucose. 3. The enzymatic synthesis of β-L-fucose 1-phosphate. J. Biol. Chem. 243 (1968) 1103–1109. [PMID: 5646161] |
2. |
Butler, W. and Serif, G.S. Fucokinase, its anomeric specificity and mechanism of phosphate group transfer. Biochim. Biophys. Acta 829 (1985) 238–243. [DOI] [PMID: 2986701] |
3. |
Park, S.H., Pastuszak, I., Drake, R. and Elbein, A.D. Purification to apparent homogeneity and properties of pig kidney L-fucose kinase. J. Biol. Chem. 273 (1998) 5685–5691. [DOI] [PMID: 9488699] |
|
[EC 2.7.1.52 created 1972, modified 2004] |
|
|
|
|