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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | coordinated in catalytic site of enolase | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-phospho-D-glycerate | Escherichia coli | - |
phosphoenolpyruvate + H2O | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6P9 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-phospho-D-glycerate | - |
Escherichia coli | phosphoenolpyruvate + H2O | - |
r |
Synonyms | Comment | Organism |
---|---|---|
enolase | - |
Escherichia coli |
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 |