Work

Substrate Ambiguity of 3-Deoxy- d - manno -Octulosonate 8-Phosphate Synthase from Neisseria gonorrhoeae Revisited

Year: 2000

Type: article

Abstract: 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).

Source: Journal of Bacteriology

DOI: 10.1128/jb.182.17.5005-5008.2000

Authors: Galina Ya Sheflyan, Appavu K. Sundaram, William P. Taylor, Ronald W. Woodard

Institution: University of Michigan

Language: English

Topic: Carbohydrate Chemistry and Synthesis

Subfield: Organic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases

Awards: Mechanism of KDO 8-P and DAH 7-P Synthase, MICROBIAL PATHOGEN GENOME PROJECT--NEISSERIA GONORRHOEAE