Stabilization of Escherichia coli isopropylmalate dehydrogenase by single amino acid substitution
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چکیده
منابع مشابه
Aerobic activity of Escherichia coli alcohol dehydrogenase is determined by a single amino acid.
Expression of the alcohol dehydrogenase gene, adhE, in Escherichia coli is anaerobically regulated at both the transcriptional and the translational levels. To study the AdhE protein, the adhE(+) structural gene was cloned into expression vectors under the control of the lacZ and trp(c) promoters. Wild-type AdhE protein produced under aerobic conditions from these constructs was inactive. Const...
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The two isozymes of dihydrofolate reductase (Forms 1 and 2) from, a Trimethoprim-resistant strain of Escherichia coli (RT500) were separated and purified to homogeneity using a simple procedure based on differential elution from a Methotrexate affinity column. The complete amino acid sequence of the Form 2 isozyme was determined, and it differs from that of Form 1 in only one position. Residue ...
متن کاملAmino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.
Amino-acid sequences around two lipoic acid residues in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex of Escherichia coli were investigated. A single amino acid sequence of 13 residues was found. A repeated amino acid sequence in the lipoate acetyltransferase chain might explain this result.
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UNLABELLED Programmed cell death (PCD) is an important hallmark of multicellular organisms. Cells self-destruct through a regulated series of events for the benefit of the organism as a whole. The existence of PCD in bacteria has long been controversial due to the widely held belief that only multicellular organisms would profit from this kind of altruistic behavior at the cellular level. Howev...
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ژورنال
عنوان ژورنال: Protein Engineering Design and Selection
سال: 1997
ISSN: 1741-0126,1741-0134
DOI: 10.1093/protein/10.3.249