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

Full text not available from this repository.

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:
Journal Article
Journal or Publication Title:
Planta
Uncontrolled Keywords:
/dk/atira/pure/subjectarea/asjc/1100/1110
Subjects:
?? 1,5-bisphosphate carboxylasegene mutation (n-terminus)ribulosesubstrate affinity (ribulose-1,5-bisphosphate)plant sciencegenetics ??
ID Code:
76054
Deposited By:
Deposited On:
21 Oct 2015 05:04
Refereed?:
Yes
Published?:
Published
Last Modified:
13 Sep 2024 08:51