@article {4448,
	title = {A phosphinate inhibitor of the meso-diaminopimelic acid-adding enzyme (MurE) of peptidoglycan biosynthesis},
	journal = {Journal of Organic Chemistry},
	volume = {63},
	number = {26},
	year = {1998},
	note = {ISI Document Delivery No.: 153LPTimes Cited: 37Cited Reference Count: 50},
	month = {Dec},
	pages = {10081-10085},
	type = {Article},
	keywords = {AMINO-ACIDS, COLI GLUTAMINE-SYNTHETASE, D-ALANINE LIGASE, ESCHERICHIA-COLI, GLUTATHIONE SYNTHETASE, INACTIVATION, KINETIC MECHANISM, MECHANISM-BASED, N-ACETYLMURAMATE, RAPID-QUENCH, VANCOMYCIN RESISTANCE},
	isbn = {0022-3263},
	url = {<Go to ISI>://000077834800087},
	author = {Zeng, B. Q. and Kwong, K. and Pompliano, D. L. and Reddy, S. and Tanner, M. E.}
}
@article {3832,
	title = {Phosphinate inhibitors of the D-glutamic acid-adding enzyme of peptidoglycan biosynthesis},
	journal = {Journal of Organic Chemistry},
	volume = {61},
	number = {5},
	year = {1996},
	note = {ISI Document Delivery No.: TZ997Times Cited: 66Cited Reference Count: 31},
	month = {Mar},
	pages = {1756-1760},
	type = {Article},
	abstract = {We report the synthesis and initial evaluation of the first effective inhibitors of the D-glutamic acid-adding enzyme (UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase or MurD). This enzyme plays a key role in bacterial peptidoglycan biosynthesis and is therefore a target for antibiotic design. Phosphinic acid 3 is a dipeptide analog linked to uridine diphosphate by a hydrophobic spacer. It is a good inhibitor of the enzyme (IC50 = 0.68 mu M) as it closely resembles the tetrahedral intermediate that is presumed to form in the ligation reaction. Compound 4 lacks the terminal UMP group, and compound 5 lacks both the linker and UDP functionalities. These are less effective inhibitors of the enzyme with IC50 values of 29 mu M and > 1 mM, respectively. Preincubation of the enzyme in the presence of inhibitor 3 and ATP does not result in irreversible inhibition or in the formation of a slowly decomplexing species, suggesting that the phosphinic acid is not phosphorylated in the active site.},
	keywords = {(AMINOALKYL)PHOSPHINATE, ATP, D-ALANINE LIGASE, ESCHERICHIA-COLI, INACTIVATION, MECHANISM, PHOSPHINOTHRICIN, PURIFICATION, RAPID-QUENCH, SYNTHETASE},
	isbn = {0022-3263},
	url = {<Go to ISI>://A1996TZ99700030},
	author = {Tanner, M. E. and Vaganay, S. and vanHeijenoort, J. and Blanot, D.}
}
