|1.||Yew, Wen Shan: 1 article (08/2007)|
|2.||Fedorov, Elena V: 1 article (08/2007)|
|3.||Gerlt, John A: 1 article (08/2007)|
|4.||Almo, Steven C: 1 article (08/2007)|
|5.||Fedorov, Alexander A: 1 article (08/2007)|
|1.||Dehydration (Water Stress)
08/21/2007 - "The dehydration of l-talarate is accompanied by competing epimerization to galactarate; little epimerization to l-talarate is observed in the dehydration of galactarate. "
08/21/2007 - "The epimerization of l-talarate to galactarate that competes with dehydration can be rationalized by partitioning of the enolate intermediate between dehydration (departure of the 3-OH group catalyzed by the conjugate acid of His 328) and epimerization (protonation on C2 by the conjugate acid of Lys 197). "
08/21/2007 - "We discovered the function of STM3697 by screening a library of acid sugars; it catalyzes the efficient dehydration of both l-talarate (kcat = 2.1 s-1, kcat/Km = 9.1 x 10(3) M-1 s-1) and galactarate (kcat = 3.5 s-1, kcat/Km = 1.1 x 10(4) M-1 s-1). "
08/21/2007 - "On the basis of (1) structures of the wild type enzyme complexed with l-lyxarohydroxamate, an analogue of the enolate intermediate, and of the K197A mutant complexed with l-glucarate, a substrate for exchange of the alpha-proton, and (2) incorporation of solvent deuterium into galactarate in competition with dehydration, we conclude that Lys 197 functions as the galactarate-specific base and His 328 functions as the l-talarate-specific base. "