Literature summary for 5.1.1.7 extracted from

Pillai, B.; Cherney, M.M.; Diaper, C.M.; Sutherland, A.; Blanchard, J.S.; Vederas, J.C.; James, M.N.
Structural insights into stereochemical inversion by diaminopimelate epimerase: an antibacterial drug target (2006), Proc. Natl. Acad. Sci. USA, 103, 8668-8673.

Application

Application	Comment	Organism
drug development	bacterial racemase, including glutamate racemase and DAP epimerase, are potential targets for the development of new agents effective against organisms resistant to conventional antibiotics	Haemophilus influenzae

Crystallization (Commentary)

Crystallization (Comment)	Organism
co-crystals of the inhibitors LL- and DL-aziridino diaminopimelic acid with diaminopimelate epimerase from Haemophilus influenzae are grown at room temperature by the hanging-drop vapor-diffusion method. Crystals of both complexes are obtained in 2.8 M sodium acetate /0.1 M Hepes (pH 7.0) at a protein concentration of approx. 10 mg/ml in 25 mM Hepes, 5 mM DTT (pH 8.0)	Haemophilus influenzae
crystal structures of diaminopimelate epimerase from Haemophilus influenzae with two different isomers of the irreversible inhibitor and substrate mimic aziridino diaminopimelic acid at 1.35- and 1.70-A resolution are analysed. These structures permit a detailed description of this pyridoxal 5-phosphate-independent amino acid racemase active site and delineate the electrostatic interactions that control the exquisite substrate selectivity of DAP epimerase. Moreover, the active site shows how deprotonation of the substratesnonacidic hydrogen at the alpha-carbon by a seemingly weakly basic cysteine residue is facilitated by interactions with two buried alpha-helices	Haemophilus influenzae

Crystallization (Comment)

Organism

co-crystals of the inhibitors LL- and DL-aziridino diaminopimelic acid with diaminopimelate epimerase from Haemophilus influenzae are grown at room temperature by the hanging-drop vapor-diffusion method. Crystals of both complexes are obtained in 2.8 M sodium acetate /0.1 M Hepes (pH 7.0) at a protein concentration of approx. 10 mg/ml in 25 mM Hepes, 5 mM DTT (pH 8.0)

Haemophilus influenzae

crystal structures of diaminopimelate epimerase from Haemophilus influenzae with two different isomers of the irreversible inhibitor and substrate mimic aziridino diaminopimelic acid at 1.35- and 1.70-A resolution are analysed. These structures permit a detailed description of this pyridoxal 5-phosphate-independent amino acid racemase active site and delineate the electrostatic interactions that control the exquisite substrate selectivity of DAP epimerase. Moreover, the active site shows how deprotonation of the substratesnonacidic hydrogen at the alpha-carbon by a seemingly weakly basic cysteine residue is facilitated by interactions with two buried alpha-helices

Haemophilus influenzae

Inhibitors

Inhibitors	Comment	Organism	Structure
DL-aziridino analogues of diaminoheptanedioate	DL-aziridino diaminopimelic acid, irreversible inhibitor	Haemophilus influenzae
LL-aziridino analogues of diaminoheptanedioate	LL-aziridino diaminopimelic acid, irreversible inhibitor	Haemophilus influenzae

Organism

Organism	UniProt	Comment	Textmining
Haemophilus influenzae	P44859	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
LL-oxa-diaminopimelic acid	-	Haemophilus influenzae	meso-oxa-diaminopimelic acid	-	?

Synonyms

Synonyms	Comment	Organism
DAP epimerase	-	Haemophilus influenzae
diaminopimelate epimerase	-	Haemophilus influenzae