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The values of molecular carboxylase activity kcat and carboxylation specificity factor τ for mutant ribulose 1,5‐bisphosphate carboxylase (rubisco) from Anacystis nidulans decreased as compared to those of the wild type recombinant rubisco. The substitution of five amino acid residues in rubisco large subunit Lys,AIa,Ser, Thr, Leu(339‐343)Phe,Leu,Met,Ile,Lys had kcat decreased by 90% and τ by 36.3%. The same parameters for mutants with the single replacements decreased: for Thr342Ile kcat by 40.5% and τ by16.7%, and for mutant Leu343Lys kcat by 48.1% and τ by 18.5%. Mutant rubisco with three amino acid resudues changed Val,Asp,Leu(346‐348)Tyr,His,Thr was inactive. The substitution Leu326Ile decreased kcat by 54.4% and τ by 34.2%; and change Ser328Ala decreased kcat only by 5.6% but τ by 41.5%. Replacement Asn123His decreased kcat by 16.5%. Significance of the non conservative amino acid residues for carboxylase activity and ribulose‐l,5‐bisphosphate partition is discussed.
IUBMB Life – Wiley
Published: Jun 1, 1997
Keywords: recombinant ribulose‐l,5‐bisphopsphate carboxylase; cyanobacteriurn; mutant large subunit; carboxylation efficiency
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