Mutants of Saccharomycopsis lipolytica defective in lysine catabolism

Gaillardin, C.; Fournier, P.; Sylvestre, G.; Heslot, H.

doi:10.1128/jb.125.1.48-57.1976

Cited by 38 publications

(7 citation statements)

References 27 publications

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“…Considerable genetic and biochemical diversity also exist in yeasts and molds for the use of lysine as the sole nitrogen source. Distinct pathways for the use of lysine as the sole nitrogen source are used by Rhodotorula glutinis (KINZEL et al 1983), Saccharomycopsis lipolytica (GAILLARDIN et al 1976), Candida maltosa (SCHMIDT et al 1988) and Pichia guilliermondii (SCHMIDT et al 1987). Results presented in this report indicate that C .…”

Section: Homoisocitrate Dehydrogenase Glutamate-a-ketoadipate Transamentioning

confidence: 79%

Use of α‐aminoadipate and lysine as sole nitrogen source by Schizosacharomyces pombe and selected pathogenic fungi

Garrad

Winston

et al. 1991

J. Basic Microbiol.

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alpha-Aminodipate, an intermediate of the lysine biosynthetic pathway of fungi, or lysine when used as the sole nitrogen source in the medium was growth inhibitory and toxic to Saccharomyces cerevisiae. The fission yeast Schizosaccharomyces pombe and pathogenic fungi Candida albicans, Filobasidiella neoformans and Aspergillus fumigatus grew in the medium containing alpha-aminoadipate as the sole nitrogen source. C. albicans, A. fumigatus, and one of the strains of F. neoformans also grew in the medium containing lysine as the sole nitrogen source. When grown in the alpha-aminoadipate medium, only S. pombe accumulated a significant amount of alpha-ketoadipate in the culture supernatant. Also, 14C-alpha-aminoadipate was converted to 14C-alpha-ketoadipate in vivo. In the ammonium sulfate medium, S. pombe cells converted 14C-alpha-aminoadipate to lysine. The levels of glutamate-alpha-ketoadipate transaminase, an enzyme responsible for the conversion of alpha-aminoadipate to alpha-ketoadipate, and alpha-aminoadipate reductase, an enzyme required for the conversion of alpha-aminoadipate to lysine, were similar in S. pombe cells grown in the alpha-aminoadipate or ammonium sulfate medium. However, the level of homoisocitrate dehydrogenase, an enzyme before the alpha-ketoadipate step, was twelvefold lower in S. pombe cells grown in the alpha-aminoadipate medium compared to the level in cells grown in the ammonium sulfate medium. Pathogenic fungi used in this study did not accumulate alpha-ketoadipate and alpha-aminoadipate-delta-semialdehyde when grown in medium containing alpha-aminoadipate and lysine, respectively, as sole nitrogen source. However, only pathogenic fungi used both lysine and alpha-aminoadipate as sole nitrogen source. This unique metabolic property could be useful for the identification of these pathogens.

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Section: Homoisocitrate Dehydrogenase Glutamate-a-ketoadipate Transamentioning

confidence: 79%

Use of α‐aminoadipate and lysine as sole nitrogen source by Schizosacharomyces pombe and selected pathogenic fungi

Garrad

Winston

et al. 1991

J. Basic Microbiol.

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“…Mutations affecting all 11 biosynthetic steps of lysine except one have been identified. A single locus, LYS1 encoding homocitrate synthase controls the first step [63, 64]. The existence of isoenzymes hitherto prevented characterization of such mutants in S. cerevisiae .…”

Section: Physiologymentioning

confidence: 99%

Physiology and genetics of the dimorphic fungusYarrowia lipolytica

Barth¹,

Gaillardin²

1997

FEMS Microbiol Rev

442

100

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The ascomycetous yeast Yarrowia lipolytica (formerly Candida, Endomycopsis, or Saccharomyces lipolytica) is one of the more intensively studied 'non-conventional' yeast species. This yeast is quite different from the well-studied yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe with respect to its phylogenetic evolution, physiology, genetics, and molecular biology. However, Y. lipolytica is not only of interest for fundamental research, but also for biotechnological applications. It secretes several metabolites in large amounts (i.e. organic acids, extracellular proteins) and the tools are available for overproduction and secretion of foreign proteins. This review presents a comprehensive overview on the available data on physiology, cell biology, molecular biology and genetics of Y. lipolytica.

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“…The next stages are oxidative decarboxylation of 2-oxo-6-acetamidohexanoate to 5-acetamidovalerate, deacetylation of the latter to 5-aminovalerate and transamination of this to glutarate semialdehyde, thereby removing the second amino group. Evidence for the occurrence of one or more of the enzymes of this route has been obtained in Williopsis (Hansenula) saturnus [6], Yarrowia lipolytica [7] and Candida maltosa [8], as well as in the filamentous fungus Rhizoctonia leguminicola [9].…”

Section: Introductionmentioning

confidence: 99%

The route of lysine breakdown in Candida tropicalis

Large

Robertson

1991

FEMS Microbiology Letters

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Candida tropicalis was found to contain high levels of the following enzymes after growth in defined medium on L-lysine as sole nitrogen source: L-lysine N6-acetyltransferase, N6-acetyl-lysine aminotransferase, and aminotransferase activity for 5-aminovalerate and 4-aminobutyrate. Extracts were also capable of converting 5-acetamidovalerate (and 4-acetamidobutyrate) to acetate. N6-Acetyllysine however, only gave rise to acetate in the presence of 2-oxoglutarate, NAD+ and thiamine pyrophosphate. These activities were undetectable or present in much lower concentrations in cells that had been grown on ammonium sulphate as sole nitrogen source. It is concluded that L-lysine is degraded in this organism via N6-acetyllysine, 5-acetamidovalerate and 5-aminovalerate, both nitrogen atoms being removed by transamination.

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Mutants of Saccharomycopsis lipolytica defective in lysine catabolism

Cited by 38 publications

References 27 publications

Use of α‐aminoadipate and lysine as sole nitrogen source by Schizosacharomyces pombe and selected pathogenic fungi

Use of α‐aminoadipate and lysine as sole nitrogen source by Schizosacharomyces pombe and selected pathogenic fungi

Physiology and genetics of the dimorphic fungusYarrowia lipolytica

The route of lysine breakdown in Candida tropicalis

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