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Abstracts » Biological sciences

Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrate

Article Abstract:

Research has been conducted on the heterocyclic substrate 4-picoline. The oxidation of this substrate by toluene dioxygenase and improvement of the enzyme's activity via laboratory evolution in extending the dioxygenase-catalyzed biotransformations range are discussed.

Author: Sakamoto, Takeshi, Joern, John M., Arisawa, Akira, Arnold, Frances H.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
Heterocyclic compounds, Toluene, Microbiological research

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A C (sub)35 carotenoid biosynthetic pathway

Article Abstract:

Research has been conducted on C (sub)35 carotenoid biosynthetic pathway. The authors describe the construction of this pathway, and report that the pahtway has emerged when C (sub)30 carotene synthase from Staphylococcus aureus was suplied with natural substrate of C (sub)40 synthase.

Author: Arnold, Frances H., Umeno, Daisuke
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2003
Science & research, Environmental aspects, Genetic aspects, Staphylococcus aureus, Escherichia coli, Carotenoids, Microbiology, Gene expression, Biosynthesis, Microbial populations, Microbial ecology

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Electrochemical studies of a truncated laccase produced in Pichia pastoris

Article Abstract:

The cDNA that encodes a laccase isoform from Trametes versicolor (LCCI), and a truncated version (LCCIa), was subcloned and expressed using Pichia pastoris, a yeast and a heterologous host. The amino acid sequence of LCCIa is just like that of LCCI except that 11 amino acids at the end at the C terminus of LCCI are replaced with a cysteine residue. The change was made to improve kinetics of electron transfer between an electrode and a copper-containing active site. For the first time it has been shown that the rate of electron transfer between an oxidoreductase and an electrode can be improved by changes to the primary structure of a protein with site-directed mutagenesis.

Author: Gelo-Pujic, Mirjana, Kim, Hyug-Han, Butlin, Nathan G., Palmore, Tayhas R.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
Usage, Yeast, Yeast (Food product), Structure-activity relationships (Biochemistry), Binding sites (Biochemistry), Active sites (Biochemistry), Enzyme kinetics, Bioelectrochemistry, Molecular microbiology, Mutagenesis

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Subjects list: Statistical Data Included, United States, Analysis, Physiological aspects, Enzymes, Oxidation-reduction reaction, Oxidation-reduction reactions, Research
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