Characterization of fructose 1,6-bisphosphatase from bakers' yeast.
نویسندگان
چکیده
منابع مشابه
Phosphorylation and inactivation of yeast fructose-1,6-bisphosphatase by cyclic AMP-dependent protein kinase from yeast.
Purified fructose-1,6-bisphosphatase from Saccharomyces cerevisiae was phosphorylated in vitro by purified yeast cAMP-dependent protein kinase. Maximal phosphorylation was accompanied by an inactivation of the enzyme by about 60%. In vitro phosphorylation caused changes in the kinetic properties of fructose-1,6-bisphosphatase: 1) the ratio R(Mg2+/Mn2+) of the enzyme activities measured at 10 mM...
متن کاملInactivation and phosphorylation of yeast fructose 1,6-bisphosphatase.
FBPase* from Saccharomyces cerevisiae is a highly regulated enzyme. Repression of its synthesis by sugars (Gancedo et al., 1967) and allosteric inhibition by AMP (Gancedo et al., 1965) have been documented. Moreover, glucose can inactivate the enzyme. In certain conditions the loss of enzymic activity is paralleled by a loss of cross-reacting material against FBPase antibodies (Funayama et al.,...
متن کاملDNA polymerases from bakers' yeast.
Two DNA polymerases are present in extracts of commercial bakers' yeast and wild type Saccharomyces cerevisiae grown aerobically to late log phase. Yeast DNA polymerase I and yeast DNA polymerase II can be separated by DEAE-cellulose, hydroxylapatite, and denatured DNA-cellulose chromatography from the postmitochondrial supernatants of yeast lysates. The yeast polymerases are both of high molec...
متن کاملFormaldehyde dehydrogenase from bakers' yeast.
In the course of studies of formaldehyde metabolism in yeast (I), an enzyme was found that catalyzed the oxidation of formaldehyde in the presence of glutathione and diphosphopyridine nucleotide. A similar enzyme was discovered independently by Strittmatter and Ball in liver (2). This paper describes the partial purification and some of the properties of yeast formaldehyde dehydrogenase. Some e...
متن کاملCharacterization of the human liver fructose-1,6-bisphosphatase gene promoter.
Fructose-1,6-bisphosphatase (FBPase; EC 3.1.3.11), an important gluconeogenic enzyme, catalyses the hydrolysis of fructose 1, 6-bisphosphate to fructose 6-phosphate and P(i). Enzyme activity is mainly regulated by the allosteric inhibitors fructose 2, 6-bisphosphate and AMP. Although some observations about hormonal regulation of the enzyme have been published, the FBPase promoter has not been ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1984
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)39856-3