1MBB

OXIDOREDUCTASE

1MBB の概要

• エントリーDOI: 10.2210/pdb1mbb/pdb
• 分子名称: URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE, URIDINE-DIPHOSPHATE-3(N-ACETYLGLUCOSAMINYL)BUTYRIC ACID, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: flavoenzyme, oxidoreductase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm (Probable): P08373
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39370.90

構造登録者

Benson, T.E.,Lees, W.J.,Walsh, C.T.,Hogle, J.M. (登録日: 1995-11-07, 公開日: 1996-10-14, 最終更新日: 2024-02-14)

主引用文献

Lees, W.J.,Benson, T.E.,Hogle, J.M.,Walsh, C.T.
(E)-enolbutyryl-UDP-N-acetylglucosamine as a mechanistic probe of UDP-N-acetylenolpyruvylglucosamine reductase (MurB).
Biochemistry, 35:1342-1351, 1996

PubMed Abstract: UDP-N-acetylenolpyruvylglucosamine reductase (MurB), a peptidoglycan biosynthetic enzyme from Escherichia coli, reduces both (E)- and (Z)-isomers of enolbutyryl-UDP-GlcNAc, C4 analogs of the physiological C3 enolpyruvyl substrate, to UDP-methyl-N-acetylmuramic acid in the presence of NADPH. The X-ray crystal structure of the (E)-enolbutyryl-UDP-GlcNAc-MurB complex is similar to that of the enolpyruvyl-UDP-GlcNAc-MurB complex. In both structures the groups thought to be involved in hydride transfer to C3 and protonation at C2 of the enol ether substrate are arranged anti relative to the enol double bond. The stereochemical outcome of reduction of (E)-enolbutyryl-UDP-GlcNAc by NADPD in D2O is thus predicted to yield a (2R,3R)-dideuterio product. This was validated by conversion of the 2,3-dideuterio-UDP-methyl-N-acetylmuramic acid product to 2,3-dideuterio-2-hydroxybutyrate, which was shown to be (2R) by enzymatic analysis and (3R) by NMR comparison to authentic (2R,3R)- and (2R,3S)-2,3-dideuterio-2-hydroxybutyrate. Remarkably, the (E)-enolbutyryl-UDP-GlcNAc was found to partition between reduction to UDP-methyl-N-acetylmuramic and isomerization to the (Z)-substrate isomer in the MurB active site, indicative of a C2 carbanion/enol species that is sufficiently long-lived to rotate around the C2-C3 single bond during catalysis.

PubMed: 8634262
DOI: 10.1021/bi952287w

実験手法

X-RAY DIFFRACTION (2.3 Å)