5-Aminolevulinate production by Escherichia coli containing the Rhodobacter sphaeroides hemA gene
Article Abstract:
Escherichia coli synthesizes the five-carbon amino acid, 5-aminolevulinate (ALA), via expression of the Rhodobacter sphaeroides hemA gene. The biosynthetic pathway involves the enzyme ALA synthase and the precursors succinate and glycine. Cloning and sequencing of the hemA gene expressed in a variety of E. coli strains reveal that production of ALA is regulated by the formation of ALA synthase. E. coli host strains with high levels of carbon produce high levels of ALA synthase activity, suggesting that ALA synthase production is dependent on carbon source.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
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Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme
Article Abstract:
Microbiological research shows that the gene encoding the anaerobic microorganism Pyrococcus furiosus hyperthermophilic enzyme amylopullulanase is a single 827-residue polypeptide with a 26-residue signal peptide. It is a mature protein which has a molecular weight of 89,000 and retains its three-dimensional shape at temperatures of up to 70 degrees centigrade. The substrate specificity, kinetic properties and hydrolysis product analysis are discussed.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
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Regulation and characterization of xylanolytic enzymes of Thermoanaerobacterium saccharolyticum B6A-RI
Article Abstract:
Xylanolytic enzymes were derived from Thermoanaerobacterium saccharolyticum B6A-RI. Enzymatic activity were subjected to sodium dodecyl sulfate- polyacrylamide gel electrophoresis and zymograms for analysis. Gel filtration was used to purify the endoxylanase The xylanolytic activities of T. saccharolyticum were effectively characterized by the coordination of production of complex hydrolyzing enzymes.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1993
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