Stereochemistry of the reduction step mediated by recombinant 1-deoxy-D-xylulose 5-phosphate isomeroreductase.
[formula: see text] The stereochemistry of the 1-deoxy-D-xylulose 5-phosphate (DXP) isomeroreductase reduction step has been examined using the recombinant enzyme from Synechocystis sp. PCC6803. Using [3-2H]DXP and [4S-2H]NADPH, it has been determined that the C1 pro-S hydrogen in the 2-C-methyl-D-erythritol 4-phosphate product derives from C3 of DXP, indicating that hydride attack occurs on the re face of the intermediate aldehyde. The 4S-hydride from NADPH is delivered, assigning this enzyme as a class B dehydrogenase.
Proteau
P J
PJ
College of Pharmacy, Oregon State University, Corvallis 97331-3507, USA.
Woo
Y H
YH
Williamson
R T
RT
Phaosiri
C
C
D019747:Aldose-Ketose Isomerases / Q000737:chemistry*; D000458:Cyanobacteria / Q000201:enzymology*; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D009097:Multienzyme Complexes / Q000737:chemistry*; D009249:NADP / Q000737:chemistry; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D013237:Stereoisomerism
D009097:Multienzyme Complexes; D011994:Recombinant Proteins; D009249:NADP; D010088:Oxidoreductases; C114231:1-deoxy-D-xylulose 5-phosphate reductoisomerase; D019747:Aldose-Ketose Isomerases