title: Effect of mutations of residue 340 in the large subunit polypeptide of Rubisco from Anacystis nidulans.
abstract: Residues 338-342 at the C-terminal end of loop 6 in the large subunit beta/alpha barrel structure of Rubisco 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 Vc, the rate of carboxylation, while replacement by asparagine increased the specificity factor by 9% and Vc 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.
authors.affiliation: Biochemistry and Physiology Department, IACR-Rothamsted, Harpenden, UK. pippa.madgwick@bbsrc.ac.uk
authors.forename: P J
authors.initials: PJ
authors.lastname: Madgwick
authors.forename: S
authors.initials: S
authors.lastname: Parmar
authors.forename: M A
authors.initials: MA
authors.lastname: Parry
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D000458:Cyanobacteria / Q000201:enzymology* / Q000235:genetics; D016297:Mutagenesis, Site-Directed; D012273:Ribulose-Bisphosphate Carboxylase / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D012273:Ribulose-Bisphosphate Carboxylase