2IHV

Carboxyethylarginine synthase from Streptomyces clavuligerus: 5-guanidinovaleric acid complex

2IHV の概要

• エントリーDOI: 10.2210/pdb2ihv/pdb
• 分子名称: Carboxyethylarginine synthase, MAGNESIUM ION, POTASSIUM ION, ... (6 entities in total)
• 機能のキーワード: thiamin diphosphate complex, transferase
• 由来する生物種: Streptomyces clavuligerus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 246529.12

構造登録者

Caines, M.E.,Schofield, C.J. (登録日: 2006-09-27, 公開日: 2007-09-18, 最終更新日: 2023-08-30)

主引用文献

Caines, M.E.,Sorensen, J.L.,Schofield, C.J.
Structural and mechanistic studies on N(2)-(2-carboxyethyl)arginine synthase.
Biochem.Biophys.Res.Commun., 385:512-517, 2009

PubMed Abstract: N(2)-(2-Carboxyethyl)arginine synthase (CEAS), an unusual thiamin diphosphate (ThDP)-dependent enzyme, catalyses the committed step in the biosynthesis of the b-lactamase inhibitor clavulanic acid in Streptomyces clavuligerus. Crystal structures of tetrameric CEAS-ThDP in complex with the substrate analogues 5-guanidinovaleric acid (GVA) and tartrate, and a structure reflecting a possible enol(ate)-ThDP reaction intermediate are described. The structures suggest overlapping binding sites for the substrates D-glyceraldehyde-3-phosphate (D-G3P) and L-arginine, and are consistent with the proposed CEAS mechanism in which D-G3P binds at the active site and reacts to form an alpha,beta-unsaturated intermediate,which subsequently undergoes (1,4)-Michael addition with the alpha-amino group of L-arginine. Additional solution studies are presented which probe the amino acid substrate tolerance of CEAS, providing further insight into the L-arginine binding site. These findings may facilitate the engineering of CEAS towards the synthesis of alternative beta-amino acid products.

PubMed: 19477162
DOI: 10.1016/j.bbrc.2009.05.095

実験手法

X-RAY DIFFRACTION (2.3 Å)