Literature summary extracted from
Stenta, M.; Calvaresi, M.; Altoè, P.; Spinelli, D.; Garavelli, M.; Galeazzi, R.; Bottoni, A.
Catalytic mechanism of diaminopimelate epimerase: A QM/MM investigation (2009), J. Chem. Theory Comput., 5, 1915-1930.
Application
EC Number |
Application |
Comment |
Organism |
---|
5.1.1.7 |
drug development |
enzyme represents a promising target for rational drug design aimed to develop new selective antibacterial therapeutic agents |
Haemophilus influenzae |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
5.1.1.7 |
DL-aziridino-diaminopimelate |
product-like inhibitor, inhibitor mimics the natural substrate, the methylene carbon of the aziridine ring of the 2 diastereomeric inhibitors is covalently bonded to the sulfur atom of Cys73 or Cys217 after the nucleophilic attack of the sulfur on the aziridine ring that irreversibly inhibits the enzyme |
Haemophilus influenzae |
|
5.1.1.7 |
LL-aziridino-diaminopimelate |
reactant-like inhibitor, inhibitor mimics the natural substrate, the methylene carbon of the aziridine ring of the 2 diastereomeric inhibitors is covalently bonded to the sulfur atom of Cys73 or Cys217 after the nucleophilic attack of the sulfur on the aziridine ring that irreversibly inhibits the enzyme |
Haemophilus influenzae |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
5.1.1.7 |
LL-2,6-diaminoheptanedioate |
Haemophilus influenzae |
stereo-conversion, the product complex (Enzyme/meso-diaminopimelate) is less stable than the reactant complex (Enzyme/LL-diaminopimelate) |
meso-diaminopimelate |
- |
r |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.1.1.7 |
Haemophilus influenzae |
P44859 |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
5.1.1.7 |
LL-2,6-diaminoheptanedioate |
stereo-conversion, the product complex (Enzyme/meso-diaminopimelate) is less stable than the reactant complex (Enzyme/LL-diaminopimelate) |
Haemophilus influenzae |
meso-diaminopimelate |
- |
r |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
5.1.1.7 |
diaminopimelate epimerase |
- |
Haemophilus influenzae |
Turnover Number [1/s]
EC Number |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Comment |
Organism |
Structure |
---|
5.1.1.7 |
128 |
- |
LL-2,6-Diaminoheptanedioate |
forward reaction |
Haemophilus influenzae |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
5.1.1.7 |
physiological function |
enzyme belongs to the group of isomerases which are capable of inverting the absolute configuration of a carbon atom in substrates containing one (racemases) or more stereocenters |
Haemophilus influenzae |