5ZGO

Crystal structure of APRT2 from Thermus thermophilus HB8

5ZGO の概要

• エントリーDOI: 10.2210/pdb5zgo/pdb
• 分子名称: Adenine phosphoribosyltransferase (2 entities in total)
• 機能のキーワード: phosphoribosyltransferase, thermostable, enzyme, nucleic acid, transferase
• 由来する生物種: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 113472.81

構造登録者

Kunishima, N.,Naitow, H.,Matsuura, Y. (登録日: 2018-03-09, 公開日: 2019-03-06, 最終更新日: 2023-11-22)

主引用文献

Arco, J.D.,Perez, E.,Naitow, H.,Matsuura, Y.,Kunishima, N.,Fernandez-Lucas, J.
Structural and functional characterization of thermostable biocatalysts for the synthesis of 6-aminopurine nucleoside-5'-monophospate analogues.
Bioresour. Technol., 276:244-252, 2019

PubMed Abstract: The present work describes the functional and structural characterization of adenine phosphoribosyltransferase 2 from Thermus thermophilus HB8 (TtAPRT2). The combination of structural and substrate specificity data provided valuable information for immobilization studies. Dimeric TtAPRT2 was immobilized onto glutaraldehyde-activated MagReSyn®Amine magnetic iron oxide porous microparticles by two different strategies: a) an enzyme immobilization at pH 8.5 to encourage the immobilization process by N-termini (MTtAPRT2A, MTtAPRT2B, MTtAPRT2C) or b) an enzyme immobilization at pH 10.0 to encourage the immobilization process through surface exposed lysine residues (MTtAPRT2D, MTtAPRT2E, MTtAPRT2F). According to catalyst load experiments, MTtAPRT2B (activity: 480 IU g, activity recovery: 52%) and MTtAPRT2F (activity: 507 IU g, activity recovery: 44%) were chosen as optimal derivatives. The biochemical characterization studies demonstrated that immobilization process improved the thermostability of TtAPRT2. Moreover, the potential reusability of MTtAPRT2B and MTtAPRT2F was also tested. Finally, MTtAPRT2F was employed in the synthesis of nucleoside-5'-monophosphate analogues.

PubMed: 30640018
DOI: 10.1016/j.biortech.2018.12.120

実験手法

X-RAY DIFFRACTION (2.6 Å)