Lack of triose phosphate isomerase activity (TIM) is of special interest because this enzyme works at an important branch point of glycolytic flux. In this paper, we report the cloning and sequencing of the Kluyveromyces lactis gene encoding TIM. Unlike Saccharomyces cerevisiae Delta TPI1 mutants, the K. lactis mutant strain was found to be able to grow on glucose. Preliminary bioconversion experiments indicated that, like the S. cerevisiae TIM-deficient strain, the K. lactis TIM-deficient strain is able to produce glycerol with high yield.

Compagno, C., Boschi, F., Daleffe, A., Porro, D., Ranzi, B. (1999). Isolation, nucleotide sequence, and physiological relevance of the gene encoding triose phosphate isomerase from Kluyveromyces lactis. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 65(9), 4216-4219.

Isolation, nucleotide sequence, and physiological relevance of the gene encoding triose phosphate isomerase from Kluyveromyces lactis

Porro, D;
1999

Abstract

Lack of triose phosphate isomerase activity (TIM) is of special interest because this enzyme works at an important branch point of glycolytic flux. In this paper, we report the cloning and sequencing of the Kluyveromyces lactis gene encoding TIM. Unlike Saccharomyces cerevisiae Delta TPI1 mutants, the K. lactis mutant strain was found to be able to grow on glucose. Preliminary bioconversion experiments indicated that, like the S. cerevisiae TIM-deficient strain, the K. lactis TIM-deficient strain is able to produce glycerol with high yield.
Articolo in rivista - Articolo scientifico
SACCHAROMYCES CEREVISIAE; TRANSCRIPTIONAL REGULATION; GLYCEROL PRODUCTION; DEFICIENT MUTANT; YEAST; GLUCOSE; METABOLISM
English
1999
65
9
4216
4219
none
Compagno, C., Boschi, F., Daleffe, A., Porro, D., Ranzi, B. (1999). Isolation, nucleotide sequence, and physiological relevance of the gene encoding triose phosphate isomerase from Kluyveromyces lactis. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 65(9), 4216-4219.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/33836
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