3KXP

Crystal Structure of E-2-(Acetamidomethylene)succinate Hydrolase

3KXP の概要

• エントリーDOI: 10.2210/pdb3kxp/pdb
• 分子名称: Alpha-(N-acetylaminomethylene)succinic acid hydrolase, CHLORIDE ION (3 entities in total)
• 機能のキーワード: alpha/beta hydrolase, plp degradation, e-2-(acetamidomethylene)succinate, hydrolase
• 由来する生物種: Mesorhizobium loti
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 410282.02

構造登録者

McCulloch, K.M.,Mukherjee, T.,Begley, T.P.,Ealick, S.E. (登録日: 2009-12-03, 公開日: 2010-02-09, 最終更新日: 2024-10-09)

主引用文献

McCulloch, K.M.,Mukherjee, T.,Begley, T.P.,Ealick, S.E.
Structure determination and characterization of the vitamin B(6) degradative enzyme (E)-2-(acetamidomethylene)succinate hydrolase.
Biochemistry, 49:1226-1235, 2010

PubMed Abstract: The gene identification and kinetic characterization of (E)-2-(acetamidomethylene)succinate (E-2AMS) hydrolase has recently been described. This enzyme catalyzes the final reaction in the degradation of vitamin B(6) and produces succinic semialdehyde, acetate, ammonia, and carbon dioxide from E-2AMS. The structure of E-2AMS hydrolase was determined to 2.3 A using SAD phasing. E-2AMS hydrolase is a member of the alpha/beta hydrolase superfamily and utilizes a serine/histidine/aspartic acid catalytic triad. Mutation of either the nucleophilic serine or the aspartate resulted in inactive enzyme. Mutation of an additional serine residue in the active site causes the enzyme to be unstable and is likely structurally important. The structure also provides insight into the mechanism of hydrolysis of E-2AMS and identifies several potential catalytically important residues.

PubMed: 20099871
DOI: 10.1021/bi901812p

実験手法

X-RAY DIFFRACTION (2.26 Å)