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

✍ Scribed by C. A. Kettleborough; A. L. Phillips; A. J. Keys; M. A. Parry

Publisher
Springer-Verlag
Year
1991
Tongue
English
Weight
750 KB
Volume
184
Category
Article
ISSN
0032-0935

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✦ Synopsis

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 ΞΌM but its replacement with glutamine, which has polar properties, had no appreciable effect.

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