Kluyveromyces lactis toxin has an essential chitinase activity
نویسندگان
چکیده
منابع مشابه
Regulation of lactose transport in Kluyveromyces lactis
Kluyveromyces lactis is able to ferment lactose and it is considered as an alternative model for biochemical, physiological and genetic studies in nonSaccharomyces yeasts. Understanding the mechanisms of lactose uptake and the regulation involved in the transport is an important step towards better biotechnological applications. The transport of lactose in K. lactis is mediated by a membrane pe...
متن کاملKluyveromyces lactis γ-toxin, a ribonuclease that recognizes the anticodon stem loop of tRNA
Kluyveromyces lactis gamma-toxin is a tRNA endonuclease that cleaves Saccharomyces cerevisiae [see text] between position 34 and position 35. All three substrate tRNAs carry a 5-methoxycarbonylmethyl-2-thiouridine (mcm(5)s(2)U) residue at position 34 (wobble position) of which the mcm(5) group is required for efficient cleavage. However, the different cleavage efficiencies of mcm(5)s(2)U(34)-co...
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The overexpression of efflux pumps is an important mechanism leading to the development of multidrug resistance phenomenon. The transcription factor KlPdr1p, belonging to the Zn2Cys6 family, is a central regulator of efflux pump expression in Kluyveromyces lactis. To better understand how KlPDR1-mediated drug resistance is achieved in K. lactis, we used DNA microarrays to identify genes whose e...
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Saccharomyces cerevisiae and Kluyveromyces lactis are considered to be the prototypes of two distinct metabolic models of facultatively-aerobic yeasts: Crabtree-positive/fermentative and Crabtree-negative/respiratory, respectively. Our group had previously proposed that one of the molecular keys supporting this difference lies in the mechanisms involved in the reoxidation of the NADPH produced ...
متن کاملAn essential histidine residue for the activity of UDPglucose 4-epimerase from Kluyveromyces fragilis.
UDPglucose 4-epimerase from Kluyveromyces fragilis was completely inactivated by diethylpyrocarbonate following pseudo-first order reaction kinetics. The pH profile of diethylpyrocarbonate inhibition and reversal of inhibition by hydroxylamine suggested specific modification of histidyl residues. Statistical analysis of the residual enzyme activity and the extent of modification indicated modif...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1991
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1991.tb16147.x