1KKO

CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE

1KKO の概要

• エントリーDOI: 10.2210/pdb1kko/pdb
• 関連するPDBエントリー: 1KKR
• 分子名称: 3-METHYLASPARTATE AMMONIA-LYASE, SULFATE ION (3 entities in total)
• 機能のキーワード: methylaspartate ammonia lyase, enolase superfamily, tim barrel, lyase
• 由来する生物種: Citrobacter amalonaticus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92075.86

構造登録者

Levy, C.W.,Buckley, P.A.,Sedelnikova, S.,Kato, Y.,Asano, Y.,Rice, D.W.,Baker, P.J. (登録日: 2001-12-10, 公開日: 2002-01-30, 最終更新日: 2024-11-06)

主引用文献

Levy, C.W.,Buckley, P.A.,Sedelnikova, S.,Kato, Y.,Asano, Y.,Rice, D.W.,Baker, P.J.
Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase.
Structure, 10:105-113, 2002

PubMed Abstract: Methylaspartate ammonia lyase (MAL) catalyzes the magnesium-dependent reversible alpha,beta-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid. The 1.3 A MAD crystal structure of the dimeric Citrobacter amalonaticus MAL shows that each subunit comprises two domains, one of which adopts the classical TIM barrel fold, with the active site at the C-terminal end of the barrel. Despite very low sequence similarity, the structure of MAL is closely related to those of representative members of the enolase superfamily, indicating that the mechanism of MAL involves the initial abstraction of a proton alpha to the 3-carboxyl of (2S,3S)-3-methylasparic acid to yield an enolic intermediate. This analysis resolves the conflict that had linked MAL to the histidine and phenylalanine ammonia lyase family of enzymes.

PubMed: 11796115
DOI: 10.1016/S0969-2126(01)00696-7

実験手法

X-RAY DIFFRACTION (1.33 Å)