Journal article
Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ.
Abstract
The MurZ enzyme catalyzes enolpyruvoyl transfer from phosphoenolpyruvate to the 3-OH of UDP-N-acetylglucosamine (UDP-GlcNAc) in Escherichia coli peptidoglycan biosynthesis. The kinetic mechanism of MurZ has been shown to involve the generation of a non-covalently bound tetrahedral phospholactoyl-UDP-GlcNAc intermediate [Marquardt, J.L., et al. (1993) J. Am. Chem. Soc. 115, 10398-10399]. In the work described here, MurZ overproduced in E. coli …
Authors
Brown ED; Marquardt JL; Lee JP; Walsh CT; Anderson KS
Journal
Biochemistry, Vol. 33, No. 35, pp. 10638–10645
Publisher
American Chemical Society (ACS)
Publication Date
September 1, 1994
DOI
10.1021/bi00201a010
ISSN
0006-2960