Structural gene for the alkaline extracellular protease of Saccharomycopsis lipolytica
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چکیده
منابع مشابه
A novel location for dipeptidyl aminopeptidase processing sites in the alkaline extracellular protease of Yarrowia lipolytica.
A stretch of 10 consecutive dipeptides with the sequence -X-Ala- or -X-Pro-, possible cleavage sites for dipeptidyl aminopeptidase (DPAPase) activity, are located in the prepro-region of the alkaline extracellular protease (AEP) beginning at Leu14. Evidence for DPAPase processing of this dipeptide stretch was obtained by characterizing the polypeptide secreted by a strain carrying a xpr6 mutati...
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Six ethionine-resistant (Etr) regulatory mutants of Saccharomycopsis lipolytica Sl/1 overproducing methionine have been isolated. Five of them are also resistant to seleno-methionine. The activity of homocysteine synthase (O-acetyl-L-hormoserine-acetate lyase, adding hydrogen sulfide) is derepressed in these mutants and is not susceptible to the methionine-mediated repression. The pool of free ...
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XPR2 and AXP1, coding for alkaline (AEP) and acid (AXP) extracellular proteases, have been sequenced for several strains. For XPR2, the three sequenced strains are not closely related and produce significantly different levels of AEP, yet the coding sequences are identical, and there is only a single nucleotide difference in one promoter suggesting that host physiology, not promoter differences...
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The pH-regulated expression of the acid (AXP) and alkaline (AEP) extracellular proteases of the yeast Yarrowia lipolytica 148 was analysed. Expression in batch and continuous cultures was determined at the mRNA level by Northern blotting, and at the enzyme level by enzyme assays and Western blotting. Culture pH regulated AEP and AXP expression predominantly at the level of mRNA content. Highest...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1981
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.145.1.404-409.1981