BRENDA - Enzyme Database

A differential scanning calorimetric study of the effects of metal ions, substrate/product, substrate analogues and chaotropic anions on the thermal denaturation of yeast enolase 1

Brewer, J.M.; Wampler, J.E.; Int. J. Biol. Macromol. 28, 213-218 (2001)

Data extracted from this reference:

Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.11
Saccharomyces cerevisiae
-
isozyme 1
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.11
2-phospho-D-glycerate
-
651535
Saccharomyces cerevisiae
phosphoenolpyruvate
-
651535
Saccharomyces cerevisiae
r
Temperature Stability [C]
EC Number
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
4.2.1.11
additional information
-
thermal stability is increased by divalent metal ions and binding to substrate, enzyme dissociates before denaturation
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.11
2-phospho-D-glycerate
-
651535
Saccharomyces cerevisiae
phosphoenolpyruvate
-
651535
Saccharomyces cerevisiae
r
Temperature Stability [C] (protein specific)
EC Number
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
4.2.1.11
additional information
-
thermal stability is increased by divalent metal ions and binding to substrate, enzyme dissociates before denaturation
Saccharomyces cerevisiae