title: A point mutation in the N-terminus of ribulose-1,5-bisphosphate carboxylase affects ribulose-1,5-bisphosphate binding.
abstract: Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) from Anacystis nidulans was used to generate novel enzymes. Two conserved residues, threonine 4 and lysine 11 in the N-terminus were changed. The substitution of threonine 4 with serine or valine had little effect on the kinetic parameters. The substitution of lysine 11 with leucine, which is non-polar, increased the K m for ribulose-1,5-bisphosphate from 82 to 190 μM but its replacement with glutamine, which has polar properties, had no appreciable effect.
authors.affiliation: AFRC Institute of Arable Crops Research, Rothamsted Experimental Station, AL5 2JQ, Harpenden, Herts, UK.
authors.forename: C A
authors.initials: CA
authors.lastname: Kettleborough
authors.forename: A L
authors.initials: AL
authors.lastname: Phillips
authors.forename: A J
authors.initials: AJ
authors.lastname: Keys
authors.forename: M A
authors.initials: MA
authors.lastname: Parry