1NRG

Structure and Properties of Recombinant Human Pyridoxine-5'-Phosphate Oxidase

1NRG の概要

• エントリーDOI: 10.2210/pdb1nrg/pdb
• 分子名称: pyridoxine 5'-phosphate oxidase, PHOSPHATE ION, FLAVIN MONONUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: plp, fmn, pyridoxine-5'-phosphate, oxidase, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30905.62

構造登録者

Musayev, F.N.,di Salvo, M.L.,Ko, T.P.,Schirch, V.,Safo, M.K. (登録日: 2003-01-24, 公開日: 2003-02-11, 最終更新日: 2023-08-16)

主引用文献

Musayev, F.N.,Di Salvo, M.L.,Ko, T.P.,Schirch, V.,Safo, M.K.
Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase.
Protein Sci., 12:1455-1463, 2003

PubMed Abstract: Pyridoxine 5'-phosphate oxidase catalyzes the terminal step in the synthesis of pyridoxal 5'-phosphate. The cDNA for the human enzyme has been cloned and expressed in Escherichia coli. The purified human enzyme is a homodimer that exhibits a low catalytic rate constant of approximately 0.2 sec(-1) and K(m) values in the low micromolar range for both pyridoxine 5'phosphate and pyridoxamine 5'-phosphate. Pyridoxal 5'-phosphate is an effective product inhibitor. The three-dimensional fold of the human enzyme is very similar to those of the E. coli and yeast enzymes. The human and E. coli enzymes share 39% sequence identity, but the binding sites for the tightly bound FMN and substrate are highly conserved. As observed with the E. coli enzyme, the human enzyme binds one molecule of pyridoxal 5'-phosphate tightly on each subunit.

PubMed: 12824491
DOI: 10.1110/ps.0356203

実験手法

X-RAY DIFFRACTION (1.95 Å)