Purification, crystallization and preliminary X-ray diffraction analysis of NADP-dependent glutamate dehydrogenase from Aspergillus niger

被引：2

作者：

Prakash, Prem ^{[1
]}

Walvekar, Adhish S. ^{[1
]}

Punekar, Narayan S. ^{[1
]}

Bhaumik, Prasenjit ^{[1
]}

机构：

[1] Indian Inst Technol, Dept Biosci & Bioengn, Mumbai 400076, Maharashtra, India

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷

关键词：

CRYSTAL-STRUCTURE; ALLOSTERIC-REGULATION; MECHANISM; SPECIFICITY; COMPLEXES; FAMILY;

D O I：

10.1107/S2053230X14021499

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Glutamate dehydrogenase (GDH) catalyzes the NAD-dependent or NADP-dependent oxidative deamination of l-glutamate to 2-oxoglutarate and ammonia. This important reversible reaction establishes the link between carbon and nitrogen metabolism. In this study, Aspergillus niger NADP-GDH (AnGDH) has been overexpressed and purified. Purified AnGDH, with a high specific activity of 631.1 units per milligram of protein, was crystallized and the crystal diffracted to 2.9 angstrom resolution using a home X-ray source. Preliminary analysis of the X-ray diffraction data showed that the crystal belonged to space group R32, with unit-cell parameters a = b = 173.8, c = 241.5 angstrom, alpha = beta = 90, gamma = 120 degrees. The crystals exhibited an unusually high solvent content (83.0%) and had only one molecule in the asymmetric unit. Initial phases were obtained by molecular replacement, and model building and structure refinement of AnGDH are in progress.

引用

页码：1508 / 1512

页数：5

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