RT Journal Article SR Electronic(1) A1 Bui, Kien A1 Fradet, Hugues A1 Arnaud, Alain A1 Galzy, PierreYR 1984 T1 A Nitrile Hydratase with a Wide Substrate Spectrum Produced by a Brevibacterium sp JF Microbiology, VO 130 IS 1 SP 89 OP 93 DO https://doi.org/10.1099/00221287-130-1-89 PB Microbiology Society, SN 1465-2080, AB A mutant stain, Brevibacterium 19, defective for the enzyme nitrile hydratase but retaining all the amidase activity of the wild-type Brevibacterium R312, was isolated. This is genetic evidence in favour of the hypothesis that all the nitrile-hydratase activity of the wild-type was due to a single enzyme, the structural gene of which was lost in the mutant strain 19. The specific activities and K m of the nitrile hydratase were determined for 12 different substrates. The affinity of the enzyme increased as the number of hydrogen-bonding positions of the substrate increased, and decreased with more spatial crowding of the hydrocarbon chain. The specific activity of the enzyme for a substrate was enhanced by the nucleophilic and hydrophilic properties of the hydrocarbon side chain of that substrate., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-130-1-89