NDLI: Crystal structure of Saccharomyces cerevisiae Aro8, a putative -aminoadipate aminotransferase.

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Crystal structure of Saccharomyces cerevisiae Aro8, a putative -aminoadipate aminotransferase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Bulfer, Stacie L. Trievel, Raymond C. Brunzelle, Joseph S.
Description	Author Affiliation: Bulfer SL ( Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, 48109.)
Abstract	-Aminoadipate aminotransferase (AAA-AT) catalyzes the amination of 2-oxoadipate to -aminoadipate in the fourth step of the -aminoadipate pathway of lysine biosynthesis in fungi. The aromatic aminotransferase Aro8 has recently been identified as an AAA-AT in Saccharomyces cerevisiae. This enzyme displays broad substrate selectivity, utilizing several amino acids and 2-oxo acids as substrates. Here we report the 1.91Å resolution crystal structure of Aro8 and compare it to AAA-AT LysN from Thermus thermophilus and human kynurenine aminotransferase II. Inspection of the active site of Aro8 reveals asymmetric cofactor binding with lysine-pyridoxal-5-phosphate bound within the active site of one subunit in the Aro8 homodimer and pyridoxamine phosphate and a HEPES molecule bound to the other subunit. The HEPES buffer molecule binds within the substrate-binding site of Aro8, yielding insights into the mechanism by which it recognizes multiple substrates and how this recognition differs from other AAA-AT/kynurenine aminotransferases.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1002/pro.2315
Journal	Protein Science
Issue Number	10
Volume Number	22
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2013-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	2-aminoadipate Transaminase Chemistry Protein Structure, Tertiary Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Enzymology Thermus Thermophilus Transaminases Metabolism Catalytic Domain Genetics Crystallography, X-ray Hepes Lysine Models, Molecular Pyridoxal Phosphate Pyridoxamine Analogs & Derivatives Substrate Specificity Research Support, U.s. Gov't, Non-p.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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