In yeast the utilization of lactate requires two enzymes, the D and L-lactate ferricytochrome c oxidoreductase (D and L-LCR), which stereospeci®cally oxidize D-and L-lactate to pyruvate. These enzymes are nuclearly encoded and localized in mitochondria. In the yeast Kluyveromyces lactis, a mutant de
Characterization of the histidine mutants ofKluyveromyces lactis
✍ Scribed by Zonneveld, B. J. M.; Tizzani, L.; Wésolowski-Louvel, M.
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 220 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0749-503X
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✦ Synopsis
Thirty-eight different histidine mutations of Kluyveromyces lactis were isolated and genetically characterized. All of the mutations were nuclear recessive alleles. They turned out to belong to seven different complementation groups, designated hisA1 to hisA7. Five of these genes have been cloned by in vivo complementation of the Klhis mutations. Their homology to some of the histidine genes of Saccharomyces cerevisiae was confirmed by heterologous complementation. However, one of these KlHIS genes did not complement any mutation in the seven known histidine biosynthetic enzymes encoding genes (his1-his7) of S. cerevisiae.
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