Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8Q3H

Capra hircus reactive intermediate deaminase A mutant - A108D

8Q3H の概要
エントリーDOI10.2210/pdb8q3h/pdb
分子名称2-iminobutanoate/2-iminopropanoate deaminase, 1,2-ETHANEDIOL, GLYCEROL, ... (4 entities in total)
機能のキーワード2-iminobutanoate/2-iminopropanoate deaminase - capra hircus, unknown function
由来する生物種Capra hircus (goat)
タンパク質・核酸の鎖数2
化学式量合計29425.45
構造登録者
Rizzi, G.,Visentin, C.,Di Pisa, F.,Ricagno, S. (登録日: 2023-08-04, 公開日: 2024-06-26, 最終更新日: 2025-01-15)
主引用文献Rizzi, G.,Digiovanni, S.,Degani, G.,Barbiroli, A.,Di Pisa, F.,Popolo, L.,Visentin, C.,Vanoni, M.A.,Ricagno, S.
Site-directed mutagenesis reveals the interplay between stability, structure, and enzymatic activity in RidA from Capra hircus.
Protein Sci., 33:e5036-e5036, 2024
Cited by
PubMed Abstract: Reactive intermediate deaminase A (RidA) is a highly conserved enzyme that catalyzes the hydrolysis of 2-imino acids to the corresponding 2-keto acids and ammonia. RidA thus prevents the accumulation of such potentially harmful compounds in the cell, as exemplified by its role in the degradation of 2-aminoacrylate, formed during the metabolism of cysteine and serine, catalyzing the conversion of its stable 2-iminopyruvate tautomer into pyruvate. Capra hircus (goat) RidA (RidA) was the first mammalian RidA to be isolated and described. It has the typical homotrimeric fold of the Rid superfamily, characterized by remarkably high thermal stability, with three active sites located at the interface between adjacent subunits. RidA exhibits a broad substrate specificity with a preference for 2-iminopyruvate and other 2-imino acids derived from amino acids with non-polar non-bulky side chains. Here we report a biophysical and biochemical characterization of eight RidA variants obtained by site-directed mutagenesis to gain insight into the role of specific residues in protein stability and catalytic activity. Each mutant was produced in Escherichia coli cells, purified and characterized in terms of quaternary structure, thermal stability and substrate specificity. The results are rationalized in the context of the high-resolution structures obtained by x-ray crystallography.
PubMed: 38801230
DOI: 10.1002/pro.5036
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.57 Å)
構造検証レポート
Validation report summary of 8q3h
検証レポート(詳細版)ダウンロードをダウンロード

239149

件を2025-07-23に公開中

PDB statisticsPDBj update infoContact PDBjnumon