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  • 1
    Electronic Resource
    Electronic Resource
    Purification and properties of oxaloacetate decarboxylase fromCorynebacterium glutamicum (1995)
    Springer
    Antonie van Leeuwenhoek 67 (1995), S. 221-227 
    Details
    ISSN: 1572-9699
    Keywords: lysine biosynthesis ; aspartate-derived amino acids ; oxaloacetate decarboxylase ; pyruvate kinase ; Corynebacterium glutamicum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Oxaloacetate (OAA) decarboxylase (E.C. 4.1.1.3) was isolated fromCorynebacterium glutamicum. In five steps the enzyme was purified 300-fold to apparent homogeneity. The molecular mass estimated by gel filtration was 118 ± 6 kDa. SDS-PAGE showed a single subunit of 31.7 KDa, indicating an α4 subunit structure for the native enzyme. The enzyme catalyzed the decarboxylation of OAA to pyruvate and CO2, but no other α-ketoacids were used as substrate. The cation Mn2+ was required for full activity, but could be substituted by Mg2+, Co2+, Ni2+ and Ca2+. Monovalent ions like Na+, K+ or NH 4 + were not required for activity. The enzyme was inhibited by Cu2+, Zn2+, ADP, coenzyme A and succinate. Avidin did not inhibit the enzyme activity, indicating that biotin is not involved in decarboxylation of OAA. Analysis of the kinetic properties revealed a K m for OAA of 2.1 mM and a K m of 1.2 mM for Mn2+. The V max was 158 µmol of OAA converted per min per mg of protein, which corresponds to an apparent k cat of 311 s−1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00871217
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  • 2
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of the lysA gene of Corynebacterium glutamicum and possible mechanisms for modulation of its expression (1988)
    Springer
    Molecular genetics and genomics 212 (1988), S. 112-119 
    Details
    ISSN: 1617-4623
    Keywords: Corynebacterium glutamicum ; lysA promoter(s) ; Weak expression ; Full expression ; Bacterial evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Sequence analysis localized the lysA gene of Corynebacterium glutamicum strain AS019 within a 1.35 kb open reading frame, potentially encoding a 445 amino acid product. Immediately downstream from this gene we found a potential ρ-independent transcription terminator, while the 5′ flanking region (300 bp) harbors unusual topological and structural features, located in the vicinity of a potential ribosome binding site. Within this upstream region, enzymatic and genetic analyses indicated the occurrence of a promoter responsible for significant, although weak, expression of the encoded enzymatic activity. The same significant expression level was observed with a plasmid harboring an additional 0.5 kb of genomic information upstream from lysA, while its full expression apparently requires 2 kb of additional genomic information located immediately upstream from the cloned gene. The upstream sequence requirement apparently associated with the full expression of the lysA gene of C. glutamicum shows some similarity with the Escherichia coli system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00322452
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  • 3
    Electronic Resource
    Electronic Resource
    General organization of the genes specifically involved in the diaminopimelate-lysine biosynthetic pathway of Corynebacterium glutamicum (1988)
    Springer
    Molecular genetics and genomics 212 (1988), S. 105-111 
    Details
    ISSN: 1617-4623
    Keywords: Corynebacterium glutamicum ; Diaminopimelate-lysine anabolic pathway ; Heterologous complementation ; Homologous expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We utilized diaminopimelate-lysine mutants of Escherichia coli K12 to clone the genes specifically involved in the Corynebacterium glutamicum diaminopimelate-lysine anabolic pathway. From a cosmid genomic bank of C. glutamicum strain AS019, we isolated cosmids pSM71, pSM61 and pSM531, that are respectively able to complement dapA/dapB, dapD, and lysA mutants of E. coli. DNA hybridization analysis indicates that these complementing genes are located on the chromosome of C. glutamicum in at least three separate transcription units. Subcloning of parental cosmids in dapA, dapD, and lysA mutants of E. coli localized these genes, respectively, within 1.4, 3.4, and 1.8 kb fragments, cloned in an E. coli/C. glutamicum shuttle vector. Enzymatic analysis in C. glutamicum identified the dapA-complementing gene as l-2,3-dihydrodipicolinate synthetase (dapA), and the lysA-complementing gene as meso-diaminopimelate decarboxylase (lysA). In contrast, complementation of E. coli dapD8, presumably lacking L-Δ1-tetrahydrodipicolinate synthetase (dapD), led us to clone a diaminopimelate-lysine anabolic gene of C. glutamicum which does not exist in E. coli: meso-diaminopimelate dehydrogenase. Although meso-diaminopimelate is crucial in lysine formation and in cell wall biosynthesis, expression of the genomic copies of the cloned genes, which encode activities involved at key branching points of the diaminopimelate-lysine pathway of C. glutamicum, appears constitutive with regard to the addition of diaminopimelate and/or lysine during cell growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00322451
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  • 4
    Electronic Resource
    Electronic Resource
    The phosphoenolpyruvate carboxylase gene of Corynebacterium glutamicum: Molecular cloning, nucleotide sequence, and expression (1989)
    Springer
    Molecular genetics and genomics 218 (1989), S. 330-339 
    Details
    ISSN: 1617-4623
    Keywords: Corynebacterium glutamicum ; Phosphoenolpyruvate carboxylase ; ppc gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The ppc gene of Corynebacterium glutamicum encoding phosphoenolpyruvate (PEP) carboxylase was isolated by complementation of a ppc mutant of Escherichia coli using a cosmid gene bank of chromosomal c. glutamicum DNA. By subsequent subcloning into the plasmid pUC8 and deletion analysis, the ppc gene could be located on a 3.3 kb SalI fragment. This fragment was able to complement the E. coli ppc mutant and conferred PEP carboxylase activity to the mutant. The complete nucleotide sequence of the ppc gene including 5′ and 3′ flanking regions has been determined and the primary structure of PEP carboxylase was deduced. The sequence predicts a 919 residue protein product (molecular weight of 103154) which shows 34% similarity with the respective E. coli enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331286
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