Studies on Yeast Enolase
نویسندگان
چکیده
منابع مشابه
Studies on the Enzyme Enolase*
Enolase catalyzes the interconversion of u-glyceric acid 2-phosphat,e and enolpyruvic acid phosphate,’ and, as a participant of Embden-Meyerhof glycolysis and fermentation, is widely distributed in living cells. The enzyme was first purified by Warburg and Christian (1)) who demonstrated its metal activation and made the initial studies of the kinetics and the thermodynamics of the enolase reac...
متن کاملStudies on the Enzyme Enolase*
Enolase catalyzes the interconversion of u-glyceric acid 2-phosphat,e and enolpyruvic acid phosphate,’ and, as a participant of Embden-Meyerhof glycolysis and fermentation, is widely distributed in living cells. The enzyme was first purified by Warburg and Christian (1)) who demonstrated its metal activation and made the initial studies of the kinetics and the thermodynamics of the enolase reac...
متن کاملStudies on yeast enolase. Quantitative end group analyses and the effect of exopeptidase digestion.
The structural model of yeast enolase has undergone substantial modification in recent years, and the quantitative end group analysis of the enzyme was undertaken as a means of establishing the most recent two-subunit model by a chemical method. Carboxypeptidase digestion and hydrazinolysis gave 1.95 and 1.85 moles, respectively, of carboxyl-terminal leucine per mole of enzyme, and aminotermina...
متن کاملThe amino acid sequence of yeast enolase.
Automatic sequencing of yeast enolase and of its chemically and enzymatically produced peptide fragments has established the sequence of 416 of the 436 residues in the enolase subunits. The missing segments have been provided from results from sequencing the DNA of the yeast enolase genes (Holland, M. J., Holland, J. P., Thill, G. P., and Jackson, K. A. (1981) J. Biol. Chem. 256, 1385-1395). Th...
متن کاملCalorimetric studies of the role of magnesium ions in yeast enolase catalysis.
The binding of magnesium ions and of the competitive inhibitor 3-phospho-D-glyceric acid to yeast enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) has been studied calorimetrically. Thermal titration of the apoprotein with magnesium ions provides evidence that two magnesium ions bind immeasurably tightly to the dimeric enzyme, either anticooperatively to interacting sites or to two indep...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)62268-9