Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Regular Papers
Structure of Ribulose 1,5-bisphosphate Carboxylase/Oxygenase Gene Cluster from a Thermophilic Hydrogen-Oxidizing Bacterium, Hydrogenophilus thermoluteolus, and Phylogeny of the Fructose 1,6-Bisphosphate Aldolase Encoded by cbbA in the Cluster
Nobuhiro R. HAYASHIKoichi TERAZONOTohru KODAMAYasuo IGARASHI
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2000 年 64 巻 1 号 p. 61-71

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  Four genes, cbbO, cbbY, cbbA, and the pyruvate kinase gene (pyk), were found downstream of ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) genes, cbbLS, from a thermophilic hydrogen-oxidizing bacterium, Hydrogenophilus thermoluteolus (formerly Pseudomonas hydrogenothermophila). cbbO was similar to norD in the denitrification gene cluster, and cbbY was similar to cbbY from other autotrophic bacteria. cbbA encoded fructose 1,6-bisphosphate aldolase (FBP aldolase); however, CbbA was little similar to other CbbA proteins. When CbbA was overexpressed in Escherichia coli, overproduction of CbbA was detected by SDS-PAGE. However, the cell extract had slightly higher activity than a cell extract of E. coli without cbbA. Phylogenetic analysis showed class II FBP aldolase divided into classes IIA and IIB, and that CbbA from H. thermoluteolus was in class IIA. Activities of RubisCO and FBP aldolase were examined under autotrophic, mixotrophic, and heterotrophic conditions. The activities of the two enzymes were regulated independently.

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© 2000 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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