UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase
UDP-N-acetylmuramoyl-L-alanine:glutamate ligase (ADP-forming)
UDP-N-acetylmuramoylalanine---D-glutamate ligase
SER 116;GLU 157(Magnesium-2);HIS 183(Magnesium-1)
Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli.
Large-scale preparation, purification, and crystallization of UDP-N-acetylmuramoyl-L-alanine: D-glutamate ligase from Escherichia coli.
Determination of the MurD mechanism through crystallographic analysis of enzyme complexes.
"Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase.
Structural and functional similarities in the ADP-forming amide bond ligase superfamily: implications for a substrate-induced conformational change in folylpolyglutamate synthetase.
Crystal structure of Escherichia coli UDPMurNAc-tripeptide d-alanyl-d-alanine-adding enzyme (MurF) at 2.3 A resolution.
Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-diaminopimelate ligase from Escherichia coli.
This enzyme catalyzes two successive transfer reactions, according to the literature [1] & [3]. Firstly, it transfers phosphate group from ATP to the carboxyl group of the second substrate, UDP-MurNAc (UMA), forming an acyl-phosphate intermediate. Secondly, it transfers acyl group (UMA) to the amine group of the other substrate, D-glutamate, releasing the inorganic phosphate. The first reaction (phosphate transfer) occurs as follows (see [3]): (1) The acceptor group, carboxyl oxygen atom of UMA, makes a nucleophilic attack on the transferred group, the phosphorus atom of the gamma-phosphate group of ATP. The reaction proceeds through an SN2-mechanism. (2) Lys115 and Mg2+ at site-2 stabilize the transition-state by neutralizing the transferred and leaving group, which are the beta- and gamma-phosphate groups of ATP. (3) Mg2+ at site-1 activates the acceptor group, the carboxyl group of UMA, and stabilizes the transferred group, the gamma-phosphate group of ATP. The second reaction (acyl transfer) occurs as follows (see [3]): (1') The first base, probably the gamma-phosphate group of the substrate, may abstract the proton from the second acceptor group, the amine group of D-Glu. (2') After the third substrate, D-Glu, was bound to the active site, the acceptor group, the amine group of D-Glu, would make a nucleophilic attack on the second transferred group, the carbonyl carbon of phosphorylated-UMA, forming the tetrahedral intermediate. (3') The second base, probably His183, may abstract the proton from the amine of the tetrahedral intermediate, facilitating the transformation of the intermediate into the final product and the release of the phosphate.