@article {4273,
	title = {Covalent adduct formation with a mutated enzyme: Evidence for a thioester intermediate in the reaction catalyzed by UDP-glucose dehydrogenase},
	journal = {Journal of the American Chemical Society},
	volume = {120},
	number = {26},
	year = {1998},
	note = {ISI Document Delivery No.: ZZ420Times Cited: 15Cited Reference Count: 23},
	month = {Jul},
	pages = {6613-6614},
	type = {Article},
	keywords = {ALDEHYDE DEHYDROGENASE, biosynthesis, GENE, GROUP-A, HYALURONIC-ACID SYNTHESIS, INSERTION, MOLECULAR CHARACTERIZATION, MUTATIONS, PNEUMONIAE, STREPTOCOCCI, TYPE-3 CAPSULAR POLYSACCHARIDE},
	isbn = {0002-7863},
	url = {<Go to ISI>://000074727600028},
	author = {Ge, X. and Campbell, R. E. and van de Rijn, I. and Tanner, M. E.}
}
@article {3922,
	title = {Properties and kinetic analysis of UDP-glucose dehydrogenase from group a streptococci - Irreversible inhibition by UDP-chloroacetol},
	journal = {Journal of Biological Chemistry},
	volume = {272},
	number = {6},
	year = {1997},
	note = {ISI Document Delivery No.: WG192Times Cited: 39Cited Reference Count: 48},
	month = {Feb},
	pages = {3416-3422},
	type = {Article},
	abstract = {UDP-glucuronic acid is used by many pathogenic bacteria in the construction of an antiphagocytic capsule that is required for virulence. The enzyme UDP-glucose dehydrogenase catalyzes the NAD(+)-dependent 2-fold oxidation of UDP-glucose and provides a source of the acid. In the present study the recombinant dehydrogenase from group A streptococci has been purified and found to be active as a monomer. The enzyme contains no chromophoric cofactors, and its activity is unaffected by the presence of EDTA or carbonyl-trapping reagents. Initial velocity and product inhibition kinetic patterns are consistent with a bi-uni-uni-bi ping-pong mechanism in which UDP-glucose is bound first and UDP-glucuronate is released last. UDP-xylose was found to be a competitive inhibitor (K-i, 2.7 mu M) of the enzyme. The enzyme is irreversibly inactivated by uridine 5{\textquoteright}-diphosphate chloroacetol due to the alkylation of an active site cysteine thiol. The apparent second order rate constant for the inhibition (k(i)/K-i) was found to be 2 x 10(3) mM(-1) min(-1). Incubation with the truncated compound, chloroacetol phosphate, resulted in no detectable inactivation when tested under comparable conditions. This supports the notion that uridine 5{\textquoteright}-diphosphate-chloroacetol is bound in the place of UDP-glucose and is not simply acting as a nonspecific alkylating agent.},
	keywords = {ALDEHYDE DEHYDROGENASE, BOVINE LIVER, CAPSULE, CONSERVED CYSTEINE RESIDUES, GROUP-A STREPTOCOCCI, HISTIDINOL DEHYDROGENASE, HYALURONIC-ACID SYNTHESIS, MOLECULAR CHARACTERIZATION, MUTAGENESIS, PNEUMONIAE, SITE-DIRECTED},
	isbn = {0021-9258},
	url = {<Go to ISI>://A1997WG19200045},
	author = {Campbell, R. E. and Sala, R. F. and vandeRijn, I. V. and Tanner, M. E.}
}
