Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have examined the pattern of synthesis of the glycoprotein form of invertase and of the smaller carbohydratefree from in synchronous culture to obtain further infromation concerning their biosynthetic relationship. Saccharomyces mutant 1710 was chosen since its invertase production is almost completely derepressed during growth in 0.1 M mannose medium. The large enzyme, unlike the small form, binds to concanavalin A-Sepharose, and on this basis the two types can conveniently be separated for analysis. Large invertase was produced throughout the cell cycle. Synthesis of the small invertase was periodic; the single burst occurred at or close to the budding stage. Tunicamycin, which inhibits the sypthesis of external glycoproteins, halted formation of the large enzyme but not of the small form, and there was no accumulation of invertase activity with the properties of the small enzyme. Hence, it is unlikely that the small form is a precursor of the large one. Despite marked differences in their amino acid compositions, the two enzymes have many similarities. They are probably, in part, the products of the same gene(s), and the differences between them may largely reflect differences in post-translational processing.
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PMID:Large and small invertases and the yeast cell cycle. Pattern of synthesis and sensitivity to tunicamycin. 32 Oct 22

Carboxypeptidase Y from Saccharomyces cerevisiae contains 14% mannose, the only neutral sugar present. An antiserum can be raised in rabbits which reacts with both the protein and the sugar moieties of the enzyme. This antiserum also precipitates yeast invertase and yeast cell wall mannan. Thus carboxypeptidase Y, which is known to be localized in yeast vacuoles, is very probably a mannoprotein. Tunicamycin inhibits the apparent formation of carboxypeptidase Y to a similar extent as that of the externally localized mannoprotein, invertase. No accumulation of an inactive nonglycosylated or partly glycosylated carboxypeptidase Y occurs as determined by the immunoprecipitation technique. Tunicamycin also inhibits the apparent formation of proteinase A, whereas it does not affect the increase in the activities of a number of other enzymes. It is suggested that in the synthesis of glycoproteins there exists a regulatory link between the synthesis of their polypeptide chains and the reactions involved in their glycosylation.
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PMID:Inhibition of the apparent rate of synthesis on the vacuolar glycoprotein carboxypeptidase Y and its protein antigen by turicamycin in Saccharomyces cerevisiae. 79 Oct 99

Tunicamycin apparently inhibited the biosynthesis of glucose, galactose, and maltose transport systems in Saccharomyces cerevisiae. Under the conditions used, the antibiotic also blocked the biosynthesis of invertase, a well-known yeast glycoprotein, as well as the glycosylation of a marker mannoprotein of the yeast cell wall. However, the antibiotic did not affect certain proteins which did not contain carbohydrate. It seems, therefore, that these sugar carriers are glycoproteins.
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PMID:Inhibition of biosynthesis of Saccharomyces cerevisiae sugar transport system by tunicamycin. 353 86