2DKB

DIALKYLGLYCINE DECARBOXYLASE STRUCTURE: BIFUNCTIONAL ACTIVE SITE AND ALKALI METAL BINDING SITES

2DKB の概要

• エントリーDOI: 10.2210/pdb2dkb/pdb
• 分子名称: 2,2-DIALKYLGLYCINE DECARBOXYLASE (PYRUVATE), SODIUM ION, PYRIDOXAL-5'-PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: lyase(decarboxylase)
• 由来する生物種: Burkholderia cepacia
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47065.76

構造登録者

Toney, M.D.,Hohenester, E.,Jansonius, J.N. (登録日: 1994-07-12, 公開日: 1994-10-15, 最終更新日: 2017-11-29)

主引用文献

Toney, M.D.,Hohenester, E.,Cowan, S.W.,Jansonius, J.N.
Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites.
Science, 261:756-759, 1993

PubMed Abstract: The structure of the bifunctional, pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase was determined to 2.1-angstrom resolution. Model building suggests that a single cleavage site catalyzes both decarboxylation and transamination by maximizing stereoelectronic advantages and providing electrostatic and general base catalysis. The enzyme contains two binding sites for alkali metal ions. One is located near the active site and accounts for the dependence of activity on potassium ions. The other is located at the carboxyl terminus of an alpha helix. These sites help show how proteins can specifically bind alkali metals and how these ions can exert functional effects.

PubMed: 8342040

実験手法

X-RAY DIFFRACTION (2.1 Å)