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Literature summary for 4.2.1.11 extracted from

  • Chandran, V.; Luisi, B.F.
    Recognition of enolase in the Escherichia coli RNA degradosome (2006), J. Mol. Biol., 358, 8-15.
    View publication on PubMed
Search for more literature for 4.2.1.11

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Metals/Ions Comment Organism Structure
Mg2+ coordinated in catalytic site of enolase Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-phospho-D-glycerate Escherichia coli
-
 phosphoenolpyruvate + H2O
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6P9
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phospho-D-glycerate
-
 Escherichia coli phosphoenolpyruvate + H2O
-
 r

Synonyms

Synonyms Comment Organism
enolase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
additional information interaction with RNase E of the RNA degradasome, enolase recognition site for RNase E conserved in gamma-proteobacteria Escherichia coli