Literature DB >> 1400259

Crystallization and preliminary X-ray studies of a Bacillus subtilis and Thermus thermophilus HB8 chimeric 3-isopropylmalate dehydrogenase and thermostable mutants of it.

M Sakurai1, K Onodera, H Moriyama, O Matsumoto, N Tanaka, K Numata, K Imada, M Sato, Y Katsube, T Oshima.   

Abstract

A new type of chimeric 3-isopropylmalate dehydrogenase (2T2M6T) was produced by expressing the fused gene of Bacillus subtilis and Thermus thermophilus. The enzyme shows heat stability intermediate between those of the parents. The crystal of the enzyme belongs to the space group of P3(2)21, with cell dimensions of a = b = 78.9 A and c = 158.9 A. Two thermostable mutants of the chimeric enzyme were prepared by site-directed mutagenesis and then crystallized.

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Year:  1992        PMID: 1400259     DOI: 10.1093/oxfordjournals.jbchem.a123873

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  1 in total

1.  Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus.

Authors:  Angelo Merli; Karuppasamy Manikandan; Eva Gráczer; Linda Schuldt; Rajesh Kumar Singh; Péter Závodszky; Mária Vas; Manfred S Weiss
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-05-29
  1 in total

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