6D43

CHARACTERIZATION OF HUMAN TRIOSEPHOSPHATE ISOMERASE S-NITROSYLATION

6D43 の概要

• エントリーDOI: 10.2210/pdb6d43/pdb
• 分子名称: Triosephosphate isomerase, ISOPROPYL ALCOHOL, ... (4 entities in total)
• 機能のキーワード: s-nitrosylation, isomerase, glycolysis, tim-barrel, dihydroxyacetone phosphate
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52893.25

構造登録者

Romero, J.M.,Carrizo, M.E.,Curtino, J.M. (登録日: 2018-04-17, 公開日: 2018-05-16, 最終更新日: 2024-10-23)

主引用文献

Romero, J.M.,Carrizo, M.E.,Curtino, J.A.
Characterization of human triosephosphate isomerase S-nitrosylation.
Nitric Oxide, 77:26-34, 2018

PubMed Abstract: Triosephosphate isomerase (TPI), the glycolytic enzyme that catalyzes the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), has been frequently identified as a target of S-nitrosylation by proteomic studies. However, the effect of S-nitrosylation on its activity has only been explored in plants and algae. Here, we describe the in vitro S-nitrosylation of human TPI (hTPI), and the effect of the modification on its enzymatic parameters. NO-incorporation into the enzyme cysteine residues occurred by a time-dependent S-transnitrosylation from both, S-nitrosocysteine (CySNO) and S-nitrosoglutathione (GSNO), with CySNO being the more efficient NO-donor. Both X-ray crystal structure and mass spectrometry analyses showed that only Cys217 was S-nitrosylated. hTPI S-nitrosylation produced a 30% inhibition of the Vmax of the DHAP conversion to G3P, without affecting the Km for DHAP. This is the first study describing features of human TPI S-nitrosylation.

PubMed: 29678765
DOI: 10.1016/j.niox.2018.04.004

実験手法

X-RAY DIFFRACTION (2.04 Å)