Substrate ambiguity of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Neisseria gonorrhoeae revisited.
Homogeneous, recombinant 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Neisseria gonorrhoeae is shown to catalyze the formation of 3-deoxy-D-manno-octulosonate 8-phosphate from phosphoenolpyruvate and D-arabinose 5-phosphate as determined from (1)H-nuclear magnetic resonance analysis of the product. This enzyme does not catalyze the condensation of D-erythrose 4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-ribo-heptulosonate 7-phosphate, as was previously reported (P. S. Subramaniam, G. Xie, T. Xia, and R. A. Jensen, J. Bacteriol. 180:119-127, 1998).
Sheflyan
G Y
GY
Interdepartmental Program in Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan 48109-1065, USA.
Sundaram
A K
AK
Taylor
W P
WP
Woodard
R W
RW
D000446:Aldehyde-Lyases / Q000235:genetics / Q000378:metabolism*; D002413:Cations, Divalent; D008345:Manganese; D009344:Neisseria gonorrhoeae / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D010428:Pentosephosphates / Q000378:metabolism; D010728:Phosphoenolpyruvate / Q000378:metabolism; D013379:Substrate Specificity; D015032:Zinc
D002413:Cations, Divalent; D010428:Pentosephosphates; C028055:arabinose 5-phosphate; D008345:Manganese; D010728:Phosphoenolpyruvate; C020011:2-dehydro-3-deoxyphosphooctonate aldolase; D000446:Aldehyde-Lyases; D015032:Zinc