2PAN

Crystal structure of E. coli glyoxylate carboligase

2PAN の概要

• エントリーDOI: 10.2210/pdb2pan/pdb
• 分子名称: Glyoxylate carboligase, MAGNESIUM ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (7 entities in total)
• 機能のキーワード: thiamin-diphosphate (thdp), thimain-dependent enzymes, fad, enzyme, glyoxylate carboligase, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 419286.24

構造登録者

Kaplun, A.,Chipman, D.M.,Barak, Z.,Vyazmensky, M.,Shaanan, B. (登録日: 2007-03-27, 公開日: 2008-01-01, 最終更新日: 2024-11-13)

主引用文献

Kaplun, A.,Binshtein, E.,Vyazmensky, M.,Steinmetz, A.,Barak, Z.,Chipman, D.M.,Tittmann, K.,Shaanan, B.
Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes.
Nat.Chem.Biol., 4:113-118, 2008

PubMed Abstract: Thiamine diphosphate (ThDP), a derivative of vitamin B1, is an enzymatic cofactor whose special chemical properties allow it to play critical mechanistic roles in a number of essential metabolic enzymes. It has been assumed that all ThDP-dependent enzymes exploit a polar interaction between a strictly conserved glutamate and the N1' of the ThDP moiety. The crystal structure of glyoxylate carboligase challenges this paradigm by revealing that valine replaces the conserved glutamate. Through kinetic, spectroscopic and site-directed mutagenesis studies, we show that although this extreme change lowers the rate of the initial step of the enzymatic reaction, it ensures efficient progress through subsequent steps. Glyoxylate carboligase thus provides a unique illustration of the fine tuning between catalytic stages imposed during evolution on enzymes catalyzing multistep processes.

PubMed: 18176558
DOI: 10.1038/nchembio.62

実験手法

X-RAY DIFFRACTION (2.7 Å)