Amino Acids

Kinoshita, Shukuo; Nakayama, Kiyoshi

doi:10.1016/b978-0-12-596552-1.50013-9

Cited by 33 publications

(12 citation statements)

References 91 publications

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“…amino acids (Liebl, 1991). The organism is able to grow on acetate and, accordingly, both isocitrate lyase and malate synthase activities are present in it (Kinoshita, 1985). It has been shown that acetate also serves as substrate for the production of amino acids such as glutamate, lysine and threonine (reviewed in Kinoshita & Tanaka, 1972).…”

Section: Introductionmentioning

confidence: 99%

Malate synthase from Corynebacterium glutamicum: sequence analysis of the gene and biochemical characterization of the enzyme

Reinscheid

Eikmanns²,

Sahm³

1994

Microbiology

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Malate synthase is one of the key enzymes of the glyoxylate cycle and is essential for growth on acetate as sole carbon source. The aceB gene from Corynebacterium glutamicum , encoding ma late sy n t hase, was is01 a ted, subcloned and expressed in Escherichia coli and C. glutamicum . Sequencing of a 3024 bp DNA fragment containing the aceB gene revealed that it is located close t o the isocitrate lyase gene aceA. The two genes are separated by 597 bp and are transcribed in divergent directions. The predicted aceB gene product consists of 739 amino acids with an M, of 82 362. Interestingly, this polypeptide shows only weak identity with malate synthase polypeptides from other organisms and possesses an extra N-terminal sequence of about 170 amino acid residues. Inactivation of the chromosomal aceB gene led to the absence of malate synthase activity and t o the inability to grow on acetate, suggesting that only one malate synthase is present in C. glutamicum. The malate synthase was purified from an aceB-overexpressing C. glutamicum strain and biochemically characterized. The native enzyme was shown to be a monomer migrating at an M, of about 80000. By sequencing the N-terminus of malate synthase the predicted translational start site of the enzyme was confirmed. The enzyme displayed K,,, values of 30 pM and 12 pM for the substrates glyoxylate and acetyl CoA, respectively. Oxalate, glycolate and ATP were found t o be inhibitors of malate synthase activity. The present study provides evidence that the malate synthase from C. glutamicum is functionally similar t o other malate synthase enzymes but is different both in size and primary structure.

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Section: Introductionmentioning

confidence: 99%

Malate synthase from Corynebacterium glutamicum: sequence analysis of the gene and biochemical characterization of the enzyme

Reinscheid

Eikmanns²,

Sahm³

1994

Microbiology

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“…Kinoshita et al (1957a) isolated a biotin-requiring, glutamate-producing organism, subsequently named Corynebacterium glutamicum, the permeability of which could be modified by the level of biotin. Provided that the level of biotin in the production medium was below 5 μ% dm -3 then the organism would excrete glutamate, but at concentrations of biotin optimum for growth the organism produced lactate (Kinoshita and Nakayama, 1978). Thus, the permeability of C. glutamicum may be controlled by the composition of the culture medium and, as such, is not an example of strain improvement in the sense that the term has been used in this chapter.…”

Section: Modification Of the Permeabilitymentioning

confidence: 99%

“…The mutant lacked homoserine dehydrogenase which allowed aspartic semi-aldehyde to be converted solely to lysine and the resulting lack of threonine removed the concerted feedback inhibition of aspartokinase. Kinoshita and Nakayama (1978) quoted the homoserine auxotroph, C. glutamicum 901, as producing 44 g dm -3…”

Section: Glutamicummentioning

confidence: 99%

The Isolation, Preservation and Improvement of Industrially Important Micro-organisms

Stanbury

1995

Principles of Fermentation Technology

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“…Non-pathogenic Gram-positive Corynebacterium glutamicum and related bacteria are industrially important micro-organisms, used in the production of various amino acids (Kinoshita & Nakayama, 1978). Aminoacid-producing strains of these bacteria have been constructed by random mutagenesis and screening procedures (Kinoshita & Nakayama, 1978).…”

Section: Introductionmentioning

confidence: 99%

“…Aminoacid-producing strains of these bacteria have been constructed by random mutagenesis and screening procedures (Kinoshita & Nakayama, 1978). The development of gene cloning systems for these bacteria (Katsumata et (Ikeda & Katsumata, 1992;Ikeda et al, 1993Ikeda et al, , 1994.…”

Section: Introductionmentioning

confidence: 99%

A novel system with positive selection for the chromosomal integration of replicative plasmid DNA in Corynebacterium glutamicum

Ikeda

Katsumata

1998

Microbiology

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A simple system has been developed for generating Corynebacterium glutamicum strains containing stable replicative plasmids integrated into the chromosome via homologous recombination. The system is based upon extremely strong incompatibility between two plasmids, which cannot be comaintained even under antibiotic selective pressure. Integration of the resident plasmid that contained the tqpD gene of C. glutamicum was achieved by introduction of a second plasmid and subsequent selection for the maintenance of both plasmids. Plasmid integrates positive for both plasmid markers were obtained at a frequency about transformation frequency with selection for the maintenance of only the second plasmid. Southern analysis revealed that the integration had occurred through a single-crossover homologous recombination between the tqpD regions of the host genome and the plasmid. On the basis of the Campbelltype integration, chromosome walking was attempted by using Escherichia coli replication origins that were also present in the integrated plasmid. The chromosomal DNA was digested, ligated, and used to transform E. coli, which enabled recovery of the expected adjacent genomic DNA regions. The plasmid integrate was stably maintained for 30 generations under non-selective culture conditions, suggesting that the integrated sequences carrying a replicon active in the host were maintained as a stable chromosomal insert in C. glutamicum . of the normal

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Amino Acids

Cited by 33 publications

References 91 publications

Malate synthase from Corynebacterium glutamicum: sequence analysis of the gene and biochemical characterization of the enzyme

Malate synthase from Corynebacterium glutamicum: sequence analysis of the gene and biochemical characterization of the enzyme

The Isolation, Preservation and Improvement of Industrially Important Micro-organisms

A novel system with positive selection for the chromosomal integration of replicative plasmid DNA in Corynebacterium glutamicum

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