Cloning and sequencing of genes encoding malonate decarboxylase in Acinetobacter calcoaceticus |
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| Affiliation: | 1. Division of Microbiology, Department of Pathobiology, School of Public Health, Tehran University of Medical Sciences, Tehran, Iran;2. Food Microbiology Research Center, Tehran University of Medical Sciences, Tehran, Iran;3. Pediatrics Infectious Diseases Research Center, Department of Infectious Diseases, Children''s Medical Center, Tehran University of Medical Sciences, Tehran, Iran;4. Department of Microbiology, Reference Health Laboratories, Ministry of Health, Tehran, Iran;1. College of Environmental Science and Engineering, Taiyuan University of Technology, Shanxi 030024, China;2. Key Laboratory of Coal Science and Technology of Shanxi Province and Ministry of Education, Taiyuan University of Technology, Shanxi 030024, China;1. AGH University of Science and Technology, Faculty of Energy and Fuels, Al. A. Mickiewicza 30, 30-059 Cracow, Poland;2. Sorbonne Universités, UPMC, Univ. Paris 6, CNRS, UMR 7190, Institut Jean Le Rond d’Alembert, 2 place de la gare de ceinture, 78210 Saint-Cyr-L’Ecole, France;1. Department of Civil and Environmental Engineering, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong;2. Beijing Key Lab for Source Control Technology of Water Pollution, College of Environmental Science and Engineering, Beijing Forestry University, Beijing 100083, PR China;3. State Key Laboratory of Environmental Criteria and Risk Assessment, Chinese Research Academy of Environmental Sciences, Beijing 100012, PR China |
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| Abstract: | Malonate decarboxylase from Acinetobacter calcoaceticus was isolated and characterized (Kim, Y.S., Byun, H.S., J. Biol. Chem. 269 (1994) 29636–29641), and its subunits were reanalyzed recently to be α, β, γ, and δ. The genes for the subunits, MdcA (548 a.a.), B (295 a.a.), C (238 a.a.), and D (102 a.a.), of the enzyme have been cloned by using oligonucleotide primers deduced from amino acid sequences of peptides isolated from the purified enzyme, and sequenced to be clustered in an operon in the order of A-D-B-C. The operon was found to encode more genes than mdcABCD. The Escherichia coli, transformed with the vector containing the insert mdcADBC and about 1.7 kb of an upstream region, expressed the four subunits of the enzyme but the proteins did not show enzyme activity. It indicates that, like the enzymes from Malonomonas rubra and Klebsiella pneumoniae, more genes are needed for the formation of the functional malonate decarboxylase. |
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