Literature summary for 2.7.1.45 extracted from
Mathews, I.I.; McMullan, D.; Miller, M.D.; Canaves, J.M.; Elsliger, M.; Floyd, R.; Grzechnik, S.K.; Jaroszewski, L.; Klock, H.E.; Koesema, E.; Kovarik, J.S.; Kreusch, A.; Kuhn, P.; McPhillips, T.M.; Morse, A.T.; Quijano, K.; Rife, C.L.; Schwarzenbacher, R
Crystal structure of 2-keto-3-deoxygluconate kinase (TM0067) from Thermotoga maritima at 2.05 A resolution (2007), Proteins Struct. Funct. Bioinform., 70, 603-608.
No PubMed abstract available
Cloned(Commentary)
Cloned (Comment) |
Organism |
expression in Escherichia coli |
Thermotoga maritima |
Crystallization (Commentary)
Crystallization (Comment) |
Organism |
2.05 A resolution. Comparison with structure of Thermus thermophilus |
Thermotoga maritima |
Organism
Organism |
UniProt |
Comment |
Textmining |
Thermotoga maritima |
Q9WXS2 |
- |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
recombinant protein |
Thermotoga maritima |
Reaction
Reaction |
Comment |
Organism |
Reaction ID |
ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate |
reaction is initiated by the deprotonation of the hydroxyl group of the substrate by the catalytic base Asp280. A nucleophilic attack on the gamma-phosphate of ATP by the negatively charged hydroxyl group generates the transition state intermediate |
Thermotoga maritima |
|