Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 1
Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
UDP-N-acetylenolpyruvoylglucosamine reductase
UDP-N-acetylglucosamine-enoylpyruvate reductase
uridine diphosphoacetylpyruvoylglucosamine reductase
uridine diphospho-N-acetylglucosamine-enolpyruvate reductase
Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase.
Crystallization and preliminary X-ray crystallographic studies of UDP-N-acetylenolpyruvylglucosamine reductase.
An enzyme-substrate complex involved in bacterial cell wall biosynthesis.
(E)-enolbutyryl-UDP-N-acetylglucosamine as a mechanistic probe of UDP-N-acetylenolpyruvylglucosamine reductase (MurB).
Localizing the NADP+ binding site on the MurB enzyme by NMR.
The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls.
X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution.
Kinetic characterization of wild-type and S229A mutant MurB: evidence for the role of Ser 229 as a general acid.
Characterization of NADP+ binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift changes.