Article
Analyzing the catalytic role of active site residues in the Fe-type nitrile hydratase from Comamonas testosteroni Ni1.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Jul 2015
Martinez Salette, Wu Rui, Krzywda Karoline, Opalka Veronika, Chan Hei, Liu Dali, Holz Richard C
Abstract excerpt
A strictly conserved active site arginine residue (αR157) and two histidine residues (αH80 and αH81) located near the active site of the Fe-type nitrile hydratase from Comamonas testosteroni Ni1 (CtNHase), were mutated. These mutant enzymes were examined for their ability to bind iron and hydrate acrylonitrile. For the αR157A mutant, the residual activity (k cat = 10 ± 2 s(-1)) accounts for less than 1% of the...
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