9J0V

Crystal structure of monomeric PLP-dependent transaminase from Desulfobacula toluolica in P 21 21 21 space group

9J0V の概要

• エントリーDOI: 10.2210/pdb9j0v/pdb
• 分子名称: Dat: predicted D-alanine aminotransferase, DI(HYDROXYETHYL)ETHER, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: daat, d-amino acid transaminase, ta, monomeric ta, transferase
• 由来する生物種: Desulfobacula toluolica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32483.51

構造登録者

Matyuta, I.O.,Bakunova, A.K.,Nikolaeva, A.Y.,Rakitina, T.V.,Bezsudnova, E.Y.,Popov, V.O.,Boyko, K.M. (登録日: 2024-08-03, 公開日: 2024-09-18, 最終更新日: 2025-01-22)

主引用文献

Bakunova, A.K.,Matyuta, I.O.,Nikolaeva, A.Y.,Rakitina, T.V.,Boyko, K.M.,Popov, V.O.,Bezsudnova, E.Y.
From Structure to Function: Analysis of the First Monomeric Pyridoxal-5'-Phosphate-Dependent Transaminase from the Bacterium Desulfobacula toluolica .
Biomolecules, 14:-, 2024

PubMed Abstract: The first monomeric pyridoxal-5'-phosphate (PLP)-dependent transaminase from a marine, aromatic-compound-degrading, sulfate-reducing bacterium Tol2, has been studied using structural, kinetic, and spectral methods. The monomeric organization of the transaminase was confirmed by both gel filtration and crystallography. The PLP-dependent transaminase is of the fold type IV and deaminates D-alanine and ()-phenylethylamine in half-reactions. The enzyme shows high stereoselectivity; no deamination of L-amino acids and ()-phenylethylamine is detected. Structural analysis and subsequent mutagenesis led to the conclusion that the monomeric architecture of the enzyme is the only one possible and sufficient for stereoselectivity and PLP binding, but not for the overall double-substrate transamination reaction and the stability of the holo form with the reduced cofactor-pyridoxamine-5'-phosphate. These results extend the structural university of the PLP fold type IV enzymes and demonstrate the need for deeper analysis of the sequence-structure-function relationships in the transaminases.

PubMed: 39766298
DOI: 10.3390/biom14121591

実験手法

X-RAY DIFFRACTION (1.79 Å)