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Literature DB >> 16511150

Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus.

Kenichiro Suzuki¹, Sohei Ito, Akiko Shimizu-Ibuka, Hiroshi Sakai.

Abstract

Pyruvate kinase (PK) from a moderate thermophile, Bacillus stearothermophilus (BstPK), is an allosteric enzyme activated by AMP and ribose 5-phosphate but not by fructose 1,6-bisphosphate (FBP). However, almost all other PKs are activated by FBP. The wild-type and W416F/V435W mutant BstPKs were crystallized by the hanging-drop vapour-diffusion method. However, they were unsuitable for structural analysis because their data sets exhibited low completeness. A crystal suitable for structural analysis was obtained using C9S/C268S enzyme. The crystal belonged to space group P6(2)22, with unit-cell parameters a = b = 145.97, c = 118.03 A.

Entities: Chemical Mutation Species

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Year: 2005 PMID： 16511150 PMCID： PMC1952353 DOI： 10.1107/S1744309105021093

Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091

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References

21 in total

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Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus.

1. The allosteric regulation of pyruvate kinase.

2. Molecular cloning of the gene that codes for the pyruvate kinase of Bacillus subtilis: primary characterization of a strain carrying this gene insertionally inactivated.

3. Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli.

4. The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity.

5. Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs.

6. Leishmania pyruvate kinase: the crystal structure reveals the structural basis of its unique regulatory properties.

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9. Mutagenesis of the active site lysine 221 of the pyruvate kinase from Bacillus stearothermophilus.

10. Pyruvate kinase of the hyperthermophilic crenarchaeote Thermoproteus tenax: physiological role and phylogenetic aspects.