BRENDA - Enzyme Database

Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase

Poyner, R.R.; Larsen, T.M.; Wong, S.W.; Reed, G.H.; Arch. Biochem. Biophys. 401, 155-163 (2002)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
4.2.1.11
co-crystallization of the S39A mutant with Mg2+ and phosphonoacetohydroxamate, the active-site flap is opened
Saccharomyces cerevisiae
Engineering
EC Number
Amino acid exchange
Commentary
Organism
4.2.1.11
S39A
inactive mutant
Saccharomyces cerevisiae
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.11
Saccharomyces cerevisiae
-
-
-
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
-
649458
Saccharomyces cerevisiae
phosphoenolpyruvate
-
649458
Saccharomyces cerevisiae
r
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.2.1.11
co-crystallization of the S39A mutant with Mg2+ and phosphonoacetohydroxamate, the active-site flap is opened
Saccharomyces cerevisiae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
4.2.1.11
S39A
inactive mutant
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
-
649458
Saccharomyces cerevisiae
phosphoenolpyruvate
-
649458
Saccharomyces cerevisiae
r