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  • 1
    Electronic Resource
    Electronic Resource
    Physical mapping and genome organization of mitochondrial DNA from Candida maltosa (1986)
    Springer
    Current genetics 10 (1986), S. 527-530 
    Details
    ISSN: 1432-0983
    Keywords: Candida maltosa ; mtDNA ; Physical and genetic map
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mitochondrial (mt) DNA of the ascomycetous yeast Candida maltosa was isolated and characterized. The mtDNA is circular and the size estimated from restriction analysis performed with 7 endonucleases was 52 kb pairs. A restriction map was constructed, using the cleavage data of four endonucleases. Using mt genes from Saccharomyces cerevisiae, six structural genes (large rRNA, apocytochrome b, cytochrome c oxidase subunit I and subunit 11, ATPase subunit 6 and subunit 9) were located on the C. maltosa chondriome by cross hybridization experiments. The comparison between the mt genomes of C. maltosa and six other yeasts showed differences in the overall genome organization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00447386
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Valine inhibition of β-isopropylmalate dehydrogenase takes part in the regulation of leucine biosynthesis inCandida maltosa (1991)
    Springer
    Antonie van Leeuwenhoek 60 (1991), S. 125-130 
    Details
    ISSN: 1572-9699
    Keywords: Candida maltosa ; β-isopropylmalate dehydrogenase ; leucine biosynthesis ; valine inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The β-isopropylmalate (IPM) dehydrogenase (EC 1.1.1.85) ofCandida maltosa, the third pathway-specific enzyme of leucine biosynthesis, was purified, some properties of the enzyme were studied and a novel regulatory pattern was found. The Km values of the enzyme were estimated to be 0.42 mM for β-IPM and 0.34 mM for NAD+. It is demonstrated that the enzyme can be regulated by L-valine. The inhibition was competitive with respect to β-IPM (Ki=1.84 mM) and non-competitive with respect to NAD+ (Ki=5.67 mM). Exogenous addition of L-valine toC. maltosa cells increased the intracellular pool of some intermediates of leucine biosynthesis (α-ketoisovalerate, α-IPM, β-IPM), but has hardly influence on the leucine pool.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00572702
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of a novel enzyme, N6-acetyl-L-lysine: 2-oxoglutarate aminotransferase, which catalyses the second step of lysine catabolism inCandida maltosa (1992)
    Springer
    Antonie van Leeuwenhoek 62 (1992), S. 285-290 
    Details
    ISSN: 1572-9699
    Keywords: Candida maltosa ; N6-acetyl-L-lysine: 2-oxoglutarate aminotransferase ; lysine degradation ; enzyme induction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A novel aminotransferase catalyzing the second step of lysine catabolism, the oxidative transamination of the α-group of N6-acetyllysine, was identified and characterized in the yeastCandida maltosa. The enzyme was strongly induced in cells grown on L-lysine as sole carbon source. Its activity was specific for both N6-acetyllysine and 2-oxoglutarate. The Km values were 14 mM for the donor, 4 mM for the acceptor and 1.7 μM for pyridoxal-5-phosphate. The enzyme had a maximum activity at pH 8.1 and 32°C. Its molecular mass estimated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis was 55 kDa. Since the native molecular mass determined by gel filtration was 120 kDa, the enzyme is probably a homodimer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00572596
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  • 4
    Electronic Resource
    Electronic Resource
    Lysine degradation in Candida maltosa: occurrence of a novel enzyme, acetyl-CoA: L-lysine N-acetyltransferase (1988)
    Springer
    Archives of microbiology 150 (1988), S. 215-218 
    Details
    ISSN: 1432-072X
    Keywords: Candida maltosa ; Lysine degradation ; Acetyl-CoA:L-lysine N-acetyltransferase ; Enzyme induction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The yeast Candida maltosa can utilize L-lysine as sole nitrogen and sole carbon source accompanied by accumulation of ε-N-acetyl-L-lysine, indicating that lysine is metabolized by way of N-acetylated intermediates. A novel lysine acetyltransferase catalyzing the first step in this pathway, the N-acetylation of the ε-amino group of L-lysine, was found in this yeast. The enzyme, acetyl-CoA:L-lysine N-acetyltransferase, is strongly induced in cells grown on L-lysine as sole carbon source. The enzyme is specific for both L-lysine and acetyl-CoA. The K m values are 10 mM for L-lysine and 0.33 mM for acetyl-CoA. The enzyme has a maximum activity at pH 8.1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00407782
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  • 5
    Electronic Resource
    Electronic Resource
    Mode of action of glyphosate in Candida maltosa (1984)
    Springer
    Archives of microbiology 140 (1984), S. 83-85 
    Details
    ISSN: 1432-072X
    Keywords: Candida maltosa ; Glyphosate ; Shikimate pathway ; 5-Enolpyruvylshikimate 3-phosphate synthase ; 5-Dehydroquinate synthase ; 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase ; Enzyme inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The broad-spectrum herbicide glyphosate inhibits the growth of Candida maltosa and causes the accumulation of shikimic acid and shikimate-3-phosphate. Glyphosate is a potent inhibitor of three enzymes of aromatic amino acid biosynthesis in this yeast. In relation to tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase and dehydroquinate synthase, the inhibitory effect appears at concentrations in the mM range, but 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase is inhibited by micromolar concentrations of glyphosate. Inhibition of partially purified EPSP synthase reaction by glyphosate is competitive with respect to phosphoenolpyruvate (PEP) with a K i -value of 12 μM. The app. K m for PEP is about 5-fold higher and was 62 μM. Furthermore, the presence of glyphosate leads to derepression of many amino acid biosynthetic enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409776
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    Paper (German National Licenses)
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