4DBC

Substrate Activation in Aspartate Aminotransferase

4DBC の概要

• エントリーDOI: 10.2210/pdb4dbc/pdb
• 分子名称: Aspartate aminotransferase, SULFATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: aminotransferase, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44368.67

構造登録者

Toney, M.D.,Fisher, A.J.,Griswold, W.R. (登録日: 2012-01-14, 公開日: 2012-12-05, 最終更新日: 2024-02-28)

主引用文献

Griswold, W.R.,Castro, J.N.,Fisher, A.J.,Toney, M.D.
Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase.
J.Am.Chem.Soc., 134:8436-8438, 2012

PubMed Abstract: Binding isotope effects for l-aspartate reacting with the inactive K258A mutant of PLP-dependent aspartate aminotransferase to give a stable external aldimine intermediate are reported. They provide direct evidence for electronic ground-state destabilization via hyperconjugation. The smaller equilibrium isotope effect with deazaPLP-reconstituted K258A indicates that the pyridine nitrogen plays an important role in labilizing the Cα-H bond.

PubMed: 22551424
DOI: 10.1021/ja302809e

実験手法

X-RAY DIFFRACTION (1.5 Å)