Mechanistic studies of a C-C bond hydrolase
This project exemplifies our contribution to mechanistic enzymology. Homologs of this enzyme occur in cholesterol catabolism (HsaD) and the catabolism of aromatic compounds (BphD).
Ruzzini AC, Bhowmik S, Ghosh S, Yam KC, Bolin JT, Eltis LD. 2013. Insight into the tautomerization reaction catalyzed by the meta-cleavage product hydrolases. Biochemistry. 52, 7428-38.
Ruzzini AC, Bhowmik S, Yam KC, Ghosh S, Bolin JT, Eltis LD. 2013. The lid domain of the MCP hydrolase DxnB2 contributes to an increased specificity for recalcitrant PCB metabolites. Biochemistry. 52, 5685-95.
Ruzzini AC, Horsman GP, Eltis LD. 2012. The catalytic serine of MCP hydrolases is activated differently for C-O bond cleavage than for C-C bond cleavage. Biochemistry. 51, 5831-40.
Ruzzini AC, Ghosh S, Horsman GP, Foster LJ, Bolin JT, Eltis LD. 2012. Identification of an acyl-enzyme intermediate in a meta-cleavage product hydrolase reveals the versatility of the catalytic triad. J. Am. Chem Soc. 134, 4615-24.
Bhowmik S, Horsman GP, Bolin JT, Eltis LD. 2007. The molecular basis for inhibition of BphD, a C-C bond hydrolase involved in PCB degradation: large 3-substituents prevent tautomerization. J. Biol. Chem. 282, 36377-85.
Horsman GP, Bhowmik S, Seah SYK, Kumar P, Bolin JT, Eltis LD. 2007. The tautomeric half-reaction of BphD, a C-C bond hydrolase: kinetic and structural evidence supporting a key role for histidine 265 of the catalytic triad. J. Biol. Chem. 282, 19894-904.