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

Kettleborough, C. A. and Phillips, A. L. and Keys, A. J. and Parry, M. A. (1991) A point mutation in the N-terminus of ribulose-1,5-bisphosphate carboxylase affects ribulose-1,5-bisphosphate binding. Planta, 184 (1). pp. 35-39. ISSN 0032-0935

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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.

Item Type: Article
Journal or Publication Title: Planta
Uncontrolled Keywords: 1,5-bisphosphate carboxylase ; Gene mutation (N-terminus) ; Ribulose ; Substrate affinity (ribulose-1,5-bisphosphate)
Subjects:
Departments: Faculty of Science and Technology > Lancaster Environment Centre
ID Code: 76054
Deposited By: ep_importer_pure
Deposited On: 21 Oct 2015 06:04
Refereed?: Yes
Published?: Published
Last Modified: 30 Aug 2017 14:51
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/76054

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