BRENDA - Enzyme Database

Recognition of enolase in the Escherichia coli RNA degradosome

Chandran, V.; Luisi, B.F.; J. Mol. Biol. 358, 8-15 (2006)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
4.2.1.11
1.6 A resolution, co-crystallization of enolase with a synthetic peptide corresponding to residues 833 to 850 from RNase E determined, asymmetric binding of a single molecule of RNase E to a conserved cleft at the interface of the enolase dimer
Escherichia coli
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.11
Mg2+
coordinated in catalytic site of enolase
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.11
2-phospho-D-glycerate
Escherichia coli
-
phosphoenolpyruvate + H2O
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.11
Escherichia coli
P0A6P9
-
-
Purification (Commentary)
EC Number
Commentary
Organism
4.2.1.11
-
Escherichia coli
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.2.1.11
additional information
-
additional and independent function beyond glycolytic enzyme function, association of enolase to the RNA degrasome, role in RNA metabolism predicted
Escherichia coli
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
-
681381
Escherichia coli
phosphoenolpyruvate + H2O
-
-
-
r
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
4.2.1.11
additional information
interaction with RNase E of the RNA degradasome, enolase recognition site for RNase E conserved in gamma-proteobacteria
Escherichia coli
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
4.2.1.11
additional information
interaction with RNase E of the RNA degradasome, enolase recognition site for RNase E conserved in gamma-proteobacteria
Escherichia coli
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.2.1.11
1.6 A resolution, co-crystallization of enolase with a synthetic peptide corresponding to residues 833 to 850 from RNase E determined, asymmetric binding of a single molecule of RNase E to a conserved cleft at the interface of the enolase dimer
Escherichia coli
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.11
Mg2+
coordinated in catalytic site of enolase
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.11
2-phospho-D-glycerate
Escherichia coli
-
phosphoenolpyruvate + H2O
-
-
r
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.2.1.11
-
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.2.1.11
additional information
-
additional and independent function beyond glycolytic enzyme function, association of enolase to the RNA degrasome, role in RNA metabolism predicted
Escherichia coli
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
-
681381
Escherichia coli
phosphoenolpyruvate + H2O
-
-
-
r