Ubiquitously present in most bacteria, the enzyme metallohydrolase N-succinyl diaminopimelate desuccinylase (DapE) is required for the biosynthesis of meso-diaminopimelate (mDAP) and lysine, both essential components of bacterial peptidoglycan. DapE activity has been recognized as critical for bacterial ...
S. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of succinyl-diaminopimelate desuccinylase (Rv1202, DapE) from Mycobacterium tuberculosis. Acta. Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68, 1089–1093 (2012). 17. Gillner, D. M. et al. ...
Scott RA & Holz RC (2003) The dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae is a dinuclear metallohydrolase. ... Nathaniel,J.,Cosper,... - 《Journal of the American Chemical Society》 被引量: 23发表: 2003年 PROCESS FOR PRODUCTION OF L-AMINO ACID...
In the case of the homologous dimeric DapE, a succinyl-diaminopimelate desuccinylase, a histidine (H194) from the dimerization domain enters the active site of the opposing monomer [31]. This histidine is also conserved in MsAA as H226 (Fig. 1). From the predicted dimeric protein structure ...
Hydrolysis of N-succinyl-l,l-diaminopimelic acid by the dapE-encoded desuccinylase is required for the bacterial synthesis of lysine and meso-diaminopimelic acid. We have investigated the catalytic mechanism of the recombinant enzyme from Haemophilus influenzae. The desuccinylase was overexpressed in Esch...
N-succinyl-diaminopimelate desuccinylaseDapE is an enzyme that belongs to the meso-diaminopimelate/Lysine pathway. It is recognized as an antimicrobial target, hence compounds that inhibit its catalytic activity are required. The principal features considered in the selection of potential inhibitors for ...