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Sequence analysis of the cryptic plasmid pMG101 from Rhodopseudomonas palustris and construction of stable cloning vectors

Article Abstract:

The sequence and properties of a plasmid isolated from Rhodopseudomonas palustris is described. This bacterium belongs to the purple nonsulfur bacteria, which can fix CO(sub)2 in the presence or absence of light.

Author: Inui, Masayuki, Roh, Jung Hyeob, Zahn, Kenneth, Yukawa, Hideaki
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
Genetic aspects, Plasmids, Nucleotide sequence, Base sequence

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A periplasmic, alpha-type carbonic anhydrase from Rhodopseudomonas palustris is essential for bicarbonate uptake

Article Abstract:

Research reveals that the carbonic anhydrase produced by anaerobically growing Rhodopseudomonas palustris is an alpha-type enzyme whose activity is inhibited by acetazolamide in vitro and in culture under anaerobic conditions if bicarbonate is present. Data confirm that alpha-type carbonic anhydrase is not expressed under aerobic conditions.

Author: Inui, Masayuki, Zahn, Kenneth, Yukawa, Hideaki, Puskas, Laszlo G.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2000
United States, Japan, Statistical Data Included, Enzymes, Microbial enzymes, Anaerobic bacteria, Enzyme regulation, Bicarbonates, Carbonic anhydrase inhibitors

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Purification and characterization of a malic enzyme from the ruminal bacterium Streptococcus bovis ATCC 15352 and cloning and sequencing of its gene

Article Abstract:

The 2.9-kb fragment from the ruminal bacterium, Streptococcus bovis (S. bovis) ATCC 15352, is cloned to obtain malic enzyme, and the properties of this enzyme are determined and analyzed. The enzymatic properties are similar to those of the malic enzymes of Bacillus stearothermophilus and Haemophilus influenzae, and of the malolactic enzyme of Lactococcus lactis. S. bovis malic enzyme, however, catalyzes unknown enzymatic reactions, and the cations and the optimum pH required for these activities are different from those required for the L-malate oxidative decarboxylating activity.

Author: Inui, Masayuki, Yukawa, Hideaki, Suzuki, Hideyuki, Kumagai, Hidehiko, Kawai, Shigeyuki, Yamamoto, Kenji
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
Research, Streptococcus, Cloning, Enzyme kinetics

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Subjects list: Analysis, Physiological aspects
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