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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Crystallization and Preliminary X-Ray Diffraction Analysis of ARO9, an Aromatic Aminotransferase from Saccharomyces cerevisiae

Author(s): Hui Chen, Hua Huang, Xu Li, Shuilong Tong, Liwen Niu and Maikun Teng

Volume 16 , Issue 4 , 2009

Page: [450 - 453] Pages: 4

DOI: 10.2174/092986609787848036

Price: $65

Abstract

Saccharomyces cerevisae ARO9 protein, an aromatic aminotransferase II, catalyzes the transamination step of the catabolism of aromatic amino acids, mainly tryptophan. ARO9 also belongs to a novel subfamily of enzymes within the aminotransferase subgroup I. Crystals of ARO9 protein have been grown using the hanging-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 75.6 Å, b = 117.5 Å, c = 134.9 Å. Diffraction data were collected to a resolution of 2.6 Å using a rotating-anode X-ray source. Analysis indicates the presence of two molecules in an asymmetric unit.

Keywords: ARO9, aromatic aminotransferase, transamination, aminotransferase subgroup I, crystallization


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