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Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity

Parry, M. A. J. and Madgwick, P. and Parmar, S. and Cornelius, M. J. and Keys, A. J. (1992) Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity. Planta, 187 (1). pp. 109-112. 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 nidulansSynechococcus PCC 6301) was used to generate novel enzymes in Escherichia coli. Residues in C-terminal loop 6 of the β/α barrel structure of the large subunit were changed. Replacement of valine 331 with alanine caused a 90% reduction in Vmax but did not alter the enzyme's relative specificity towards either of its gaseous substrates, CO2 and O2. However replacement of alanine 340 with glutamate decreased the enzyme's specificity for CO2 but had no significant effect on either the Km for ribulose-1,5-bisphosphate or CO2 or on Vmax. In contrast replacing a small cassette of residues 338-341 produced a small increase in the specificity factor.

Item Type: Article
Journal or Publication Title: Planta
Uncontrolled Keywords: Gene mutation ; Ribulose-1,5-bisphosphate carboxylase ; Specificity factor
Subjects:
Departments: Faculty of Science and Technology > Lancaster Environment Centre
ID Code: 76051
Deposited By: ep_importer_pure
Deposited On: 21 Oct 2015 06:04
Refereed?: Yes
Published?: Published
Last Modified: 20 Sep 2017 02:20
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/76051

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