Crystallization of the FAD-independent acetolactate synthase of Klebsiella pneumoniae

Pang, S. S., Guddat, L. W. and Duggleby, R.G. (2002) Crystallization of the FAD-independent acetolactate synthase of Klebsiella pneumoniae. Acta Crystallographica Section D - Biological Crystallography, D58 1237-1239. doi:10.1107/S0907444902008132

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Author Pang, S. S.
Guddat, L. W.
Duggleby, R.G.
Title Crystallization of the FAD-independent acetolactate synthase of Klebsiella pneumoniae
Journal name Acta Crystallographica Section D - Biological Crystallography   Check publisher's open access policy
ISSN 0907-4449
Publication date 2002
Sub-type Article (original research)
DOI 10.1107/S0907444902008132
Open Access Status File (Publisher version)
Volume D58
Start page 1237
End page 1239
Total pages 3
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell
Collection year 2002
Language eng
Subject C1
270108 Enzymes
780105 Biological sciences
Abstract Leucine and valine are formed in a common pathway from pyruvate in which the first intermediate is 2-acetolactate. In some bacteria, this compound also has a catabolic fate as the starting point for the butanediol fermentation. The enzyme (EC 4.1.3.18) that forms 2-acetolactate is known as either acetohydroxyacid synthase (AHAS) or acetolactate synthase (ALS), with the latter name preferred for the catabolic enzyme. A significant difference between AHAS and ALS is that the former requires FAD for catalytic activity, although the reason for this requirement is not well understood. Both enzymes require the cofactor thiamine diphosphate. Here, the crystallization and preliminary X-ray diffraction analysis of the Klebsiella pneumoniae ALS is reported. Data to 2.6 Angstrom resolution have been collected at 100 K using a rotating-anode generator and an R-AXIS IV++ detector. Crystals have unit-cell parameters a = 137.4, b = 143.9, c = 134.4 Angstrom, alpha = 90, beta = 108.4, gamma = 90degrees and belong to space group C2. Preliminary analysis indicates that there are four monomers located in each asymmetric unit.
Keyword Biochemical Research Methods
Biochemistry & Molecular Biology
Biophysics
Crystallography
Thaliana Acetohydroxyacid Synthase
Catalytic Subunit
Escherichia-coli
Isozyme-iii
Reconstitution
Purification
Expression
Decarboxylase
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
 
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Created: Tue, 14 Aug 2007, 17:35:06 EST