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An enzyme-substrate complex involved in bacterial cell wall biosynthesis.
Nat Struct Biol. 1995 Aug; 2(8):644-53.NS

Abstract

The crystal structure of UDP-N-acetylenolpyruvylglucosamine reductase in the presence of its substrate, enolpyruvyl-UDP-N-acetylglucosamine, has been solved to 2.7 A resolution. This enzyme is responsible for the synthesis of UDP-N-acetylmuramic acid in bacterial cell wall biosynthesis and consequently provides an attractive target for the design of antibacterial agents. The structure reveals a novel flavin binding motif, shows a striking alignment of the flavin with the substrate, and suggests a catalytic mechanism for the reduction of this unusual enol ether.

Authors+Show Affiliations

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

7552726

Citation

Benson, T E., et al. "An Enzyme-substrate Complex Involved in Bacterial Cell Wall Biosynthesis." Nature Structural Biology, vol. 2, no. 8, 1995, pp. 644-53.
Benson TE, Filman DJ, Walsh CT, et al. An enzyme-substrate complex involved in bacterial cell wall biosynthesis. Nat Struct Biol. 1995;2(8):644-53.
Benson, T. E., Filman, D. J., Walsh, C. T., & Hogle, J. M. (1995). An enzyme-substrate complex involved in bacterial cell wall biosynthesis. Nature Structural Biology, 2(8), 644-53.
Benson TE, et al. An Enzyme-substrate Complex Involved in Bacterial Cell Wall Biosynthesis. Nat Struct Biol. 1995;2(8):644-53. PubMed PMID: 7552726.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - An enzyme-substrate complex involved in bacterial cell wall biosynthesis. AU - Benson,T E, AU - Filman,D J, AU - Walsh,C T, AU - Hogle,J M, PY - 1995/8/1/pubmed PY - 1995/8/1/medline PY - 1995/8/1/entrez SP - 644 EP - 53 JF - Nature structural biology JO - Nat Struct Biol VL - 2 IS - 8 N2 - The crystal structure of UDP-N-acetylenolpyruvylglucosamine reductase in the presence of its substrate, enolpyruvyl-UDP-N-acetylglucosamine, has been solved to 2.7 A resolution. This enzyme is responsible for the synthesis of UDP-N-acetylmuramic acid in bacterial cell wall biosynthesis and consequently provides an attractive target for the design of antibacterial agents. The structure reveals a novel flavin binding motif, shows a striking alignment of the flavin with the substrate, and suggests a catalytic mechanism for the reduction of this unusual enol ether. SN - 1072-8368 UR - https://www.unboundmedicine.com/medline/citation/7552726/An_enzyme_substrate_complex_involved_in_bacterial_cell_wall_biosynthesis_ L2 - https://ecocyc.org/gene?orgid=ECOLI&id=EG11205 DB - PRIME DP - Unbound Medicine ER -