Hyperthermophilic Topoisomerase I from Thermotoga maritima
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چکیده
منابع مشابه
Characterization of acetohydroxyacid synthase from the hyperthermophilic bacterium Thermotoga maritima
Acetohydroxyacid synthase (AHAS) is the key enzyme in branched chain amino acid biosynthesis pathway. The enzyme activity and properties of a highly thermostable AHAS from the hyperthermophilic bacterium Thermotoga maritima is being reported. The catalytic and regulatory subunits of AHAS from T. maritima were over-expressed in Escherichia coli. The recombinant subunits were purified using a sim...
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The cel12B gene was cloned, optimized through directed evolution using error-prone polymerase chain reaction, and then expressed in the Escherichia coli BL21 (DE3) host strain. Five mutants promoting the enzyme activities were selected. The specific activity of the best-evolved Cel16 (L20R, D37V, I108T) was improved approximately 3-fold compared to the parental enzyme. The residual enzyme activ...
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An expressed sequence tag homologous to cheA was previously isolated by random sequencing of Thermotoga maritima cDNA clones (C. W. Kim, P. Markiewicz, J. J. Lee, C. F. Schierle, and J. H. Miller, J. Mol. Biol. 231: 960-981, 1993). Oligonucleotides complementary to this sequence tag were synthesized and used to identify a clone from a T. maritima lambda library by using PCR. Two partially overl...
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Fig 4 is incorrect. Fig 4 incorrectly appears a duplicate of Fig 5. The authors have provided a corrected version of Fig 4 here. Fig 4. Structures of site-directed amino acid residues with other vicinal residues by H-bond. Copyright: © 2015 Zhang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distrib...
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To meet the demand for the application of high activity and thermostable cellulases in the production of new-generation bioethanol from nongrain-cellulose sources, a hyperthermostable β-1,4-endoglucase Cel12B from Thermotoga maritima was selected for further modification by gene site-directed mutagenesis method in the present study, based on homology modeling and rational design. As a result, t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m107714200