1ECP

PURINE NUCLEOSIDE PHOSPHORYLASE

1ECP の概要

• エントリーDOI: 10.2210/pdb1ecp/pdb
• 分子名称: PURINE NUCLEOSIDE PHOSPHORYLASE (2 entities in total)
• 機能のキーワード: pentosyltransferase, purine nucleoside phosphorylase, glycosyltransferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 155104.49

構造登録者

Mao, C.,Ealick, S.E. (登録日: 1995-07-13, 公開日: 1996-06-20, 最終更新日: 2024-02-07)

主引用文献

Mao, C.,Cook, W.J.,Zhou, M.,Koszalka, G.W.,Krenitsky, T.A.,Ealick, S.E.
The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology.
Structure, 5:1373-1383, 1997

PubMed Abstract: Purine nucleoside phosphorylase (PNP) from Escherichia coli is a hexameric enzyme that catalyzes the reversible phosphorolysis of 6-amino and 6-oxopurine (2'-deoxy)ribonucleosides to the free base and (2'-deoxy)ribose-1-phosphate. In contrast, human and bovine PNPs are trimeric and accept only 6-oxopurine nucleosides as substrates. The difference in the specificities of these two enzymes has been utilized in gene therapy treatments in which certain prodrugs are cleaved by E. coli PNP but not the human enzyme. The trimeric and hexameric PNPs show no similarity in amino acid sequence, even though they catalyze the same basic chemical reaction. Structural comparison of the active sites of mammalian and E. coli PNPs would provide an improved basis for the design of potential prodrugs that are specific for E. coli PNP.

PubMed: 9351810
DOI: 10.1016/S0969-2126(97)00287-6

実験手法

X-RAY DIFFRACTION (2 Å)