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A point mutation in the N-terminus of ribulose-1,5-bisphosphate carboxylase affects ribulose-1,5-bisphosphate binding

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<mark>Journal publication date</mark>1/04/1991
<mark>Journal</mark>Planta
Issue number1
Volume184
Number of pages5
Pages (from-to)35-39
Publication StatusPublished
<mark>Original language</mark>English

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 Km for ribulose-1,5-bisphosphate from 82 to 190 μM but its replacement with glutamine, which has polar properties, had no appreciable effect.