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

Author:

Bulfer Stacie L.1,Brunzelle Joseph S.2,Trievel Raymond C.1

Affiliation:

1. Department of Biological Chemistry; University of Michigan; Ann Arbor Michigan 48109

2. Northwestern Synchrotron Research Center; Life Sciences Collaborative Access Team; Northwestern University Center for Synchrotron Research; Argonne Illinois 60439

Funder

Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor research program (use of the LS-CAT Sector 21)

NIH CBTP Training

University of Michigan Rackham Graduate School through a Predoctoral Fellowship and a Graduate Student Research Grant

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference35 articles.

1. The alpha-aminoadipate pathway for lysine biosynthesis in fungi;Xu;Cell Biochem Biophys,2006

2. Enzymatic and physiological properties of the yeast glutamate-alpha-ketoadipate transaminase;Matsuda;J Biol Chem,1969

3. Separation and specificity of the yeast glutamate-alpha-ketoadipate transaminase;Matsuda;J Biol Chem,1969

4. The automation of science;King;Science,2009

5. Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding aromatic aminotransferases I and II reveals a new aminotransferase subfamily;Iraqui;Mol Gen Genet,1998

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