Crystallization of the catalytic subunit of Saccharomyces cerevisiae acetohydroxyacid synthase

Pang, S. S., Guddat, L. W. and Duggleby, R. G. (2001). Crystallization of the catalytic subunit of Saccharomyces cerevisiae acetohydroxyacid synthase. In: Acta crystallographica. Section D, Biological crystallography: Papers presented at COMBIO 2001. COMBIO 2001, Canberra, ACT, Australia, (1321-1323). 1-4 October, 2001. doi:10.1107/S0907444901011635

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Author Pang, S. S.
Guddat, L. W.
Duggleby, R. G.
Title of paper Crystallization of the catalytic subunit of Saccharomyces cerevisiae acetohydroxyacid synthase
Conference name COMBIO 2001
Conference location Canberra, ACT, Australia
Conference dates 1-4 October, 2001
Proceedings title Acta crystallographica. Section D, Biological crystallography: Papers presented at COMBIO 2001   Check publisher's open access policy
Journal name Acta Crystallographica Section D: Biological Crystallography   Check publisher's open access policy
Place of Publication Malden, MA, United States
Publisher Wiley-Blackwell
Publication Year 2001
Sub-type Fully published paper
DOI 10.1107/S0907444901011635
Open Access Status File (Publisher version)
ISSN 0907-4449
1399-0047
Volume 57
Issue 9
Start page 1321
End page 1323
Total pages 3
Language eng
Abstract/Summary Acetohydroxyacid synthase (AHAS; E.C. 4.1.3.18) is the first enzyme in the biosynthetic pathway of the branched-chain amino acids isoleucine, leucine and valine. It is a thiamin diphosphate-dependent enzyme which catalyses the decarboxylation of pyruvate and its condensation with either 2-ketobutyrate or a second molecule of pyruvate to give 2-aceto-2-hydroxybutyrate or 2-acetolactate, respectively. The enzyme is the target of sulfonylurea and imidazolinone herbicides, which act as potent and specific inhibitors. Here, the crystallization and preliminary X-ray diffraction analysis of the catalytic subunit of Saccharomyces cerevisiae AHAS is reported. Data to 2.7 Angstrom resolution have been collected using synchrotron radiation (Advanced Photon Source, Chicago). Crystals have unit-cell parameters a = 95.8, b = 110.0, c = 178.9 Angstrom and belong to the space group P2(1)2(1)2(1). Preliminary analysis indicates there is one dimer located in each asymmetric unit.
Subjects 03 Chemical Sciences
Keyword Biochemical Research Methods
Biochemistry & Molecular Biology
Biophysics
Crystallography
Diphosphate-dependent Enzyme
Site-directed Mutagenesis
Crystal-structure
Pyruvate Decarboxylase
Angstrom Resolution
Acid Synthase
Acetolactate Synthase
Escherichia-coli
Isozyme-iii
Reconstitution
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Conference Paper
Collection: School of Chemistry and Molecular Biosciences
 
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Created: Thu, 20 Sep 2007, 01:55:22 EST