Effect of mutations of residue 340 in the large subunit polypeptide of Rubisco from Anacystis nidulans

Madgwick, Pippa J. and Parmar, Saroj and Parry, Martin A J (1998) Effect of mutations of residue 340 in the large subunit polypeptide of Rubisco from Anacystis nidulans. European Journal of Biochemistry, 253 (2). pp. 476-479. ISSN 0014-2956

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Abstract

Residues 338-342 at the C-terminal end of loop 6 in the large subunit β/α barrel structure of Rubisoo influence specificity towards CO2 and O2. In Anacystis nidulans Rubisco, replacement of alanine 340 by tyrosine or histidine increased the specificity factor by 12-13%, accompanied by a 25- 33% fall in V(c), the rate of carboxylation, while replacement by asparagine increased the specificity factor by 9% and V(c) by 19%. Other mutations did not significantly alter specificity. Alanine 340 does not interact directly with the bisphosphate substrate, thus replacing it with other residues must have indirect effects on the specificity factor and rate of carboxylation.

Item Type:
Journal Article
Journal or Publication Title:
European Journal of Biochemistry
Uncontrolled Keywords:
/dk/atira/pure/subjectarea/asjc/1300/1303
Subjects:
ID Code:
76035
Deposited By:
Deposited On:
21 Oct 2015 05:04
Refereed?:
Yes
Published?:
Published
Last Modified:
07 Jan 2020 04:36