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Results 1 - 10 of 11 > >>
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EC Number Protein Variants Commentary Reference
Display the reaction diagram Show all sequences 2.1.1.259247H/Ins254A/R259W mutant is able to methylate both Rubisco and fructose 1,6-bisphosphate aldolase with similar efficiency 757705
Display the reaction diagram Show all sequences 2.1.1.259I242V mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT 757705
Display the reaction diagram Show all sequences 2.1.1.259Ins254A enzyme is able to methylate Rubisco in addition to fructose 1,6-bisphosphate aldolase 757705
Display the reaction diagram Show all sequences 2.1.1.259Ins254A/R259W mutation enhances methylation of Rubisco without altering fructose 1,6-bisphosphate aldolase methylation 757705
Display the reaction diagram Show all sequences 2.1.1.259more construction of chimera between Pisum sativum and Arabidopsis thaliana enzymes to localize regions of the enzymes responsible for the observed difference in substrate specificity. Contrary to the Pisum sativum enzyme, Arabidopsis thaliana LSMT is not able to trimethylate Rubisco 757705
Display the reaction diagram Show all sequences 2.1.1.259more identification of an LSMT region important for RBCL methylation by domain swapping, Arabidopsis thaliana AtLSMT and Pisum sativum PsLSMT are selected as representatives of monofunctional and bifunctional enzymes, respectively. An initial set of chimeric enzymes (chimera 1 and 2) is constructed in which the N-terminal portion of one parental mature enzyme, i.e. devoid of its amino terminal sequence for targeting to plastids, is replaced by the equivalent of the second parental enzyme, and vice versa. The exchanged peptide fragment comprises the nSET domain, the N-terminal part of the SET domain, and the entire iSET domain of both model enzymes. Chimera 1, bearing the N-terminal portion from PsLSMT, displays an AtLSMT-like activity, methylating only FBA2, while its reciprocal counterpart, chimera 2, displays a PsLSMT-like profile, methylating both FBA2 and RBCL. For chimera 2, measured activities are somewhat impaired compared with those of the PsLSMT parent enzyme. Chimera 1 and 2 confirm that the iSET domain is not critical for LSMT substrate selectivity. Phenotypes overview 757705
Display the reaction diagram Show all sequences 2.1.1.259P240A mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT 757705
Display the reaction diagram Show all sequences 2.1.1.259R259W mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT 757705
Display the reaction diagram Show all sequences 2.1.1.259S299P mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT 757705
Display the reaction diagram Show all sequences 2.1.1.259V269L mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT 757705
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