the enzyme is able to catalyse carbon-carbon bond formation. In addition to its natural substrate 2-hydroxy-6-oxonona-1,9-dienedioic acid, enzyme MhpC also hydrolyses various analogues and also the hydrolysis of ester bonds of monoethyl adipate and 4-nitrophenyl valerate. The H114A mutant of the enzyme also hydrolyses 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, HOPDA, a substrate of enzyme BphD, EC 126.96.36.199. Incubation of monomethyl succinate and ethyl 2-hydroxypentadienoate with the wild-type freeze-dried MhpC in hexane result in C-C bond formation product
hanging-drop vapour-diffusion method. The 2.1 A resolution X-ray structure of the native enzyme determined from orthorhombic crystals confirms that it is a member of the alpha/beta hydrolase fold family, comprising eight beta-strands interconnected by loops and helices. The 2.8 A resolution structure of the enzyme cocrystallized with the non-hydrolysable substrate analogue 2,6-diketo-nona-1,9-dioic acid confirms the location of the active site in a buried channel including Ser110, His263 and Asp235, postulated contributors to a serine protease-like catalytic triad in homologous enzymes
shows twofold-reduced catalytic efficiency, ruling out a catalytic role, but shows a fivefold-reduced KM for the natural substrate, and an ability to process an aryl-containing substrate, implying a role for His114 in positioning of the substrate
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3-(3-hydroxyphenyl)propionic acid, 3-(2-hydroxyphenyl)propionic acid, 3-(2,3-dihydroxyphenyl)propionic acid or hydrocinnamic acid or cis-3-(3-carboxyethyl)-3,5-cyclohexadiene-1,2-diol are poor inducers