2.1.1.259: [fructose-bisphosphate aldolase]-lysine N-methyltransferase
This is an abbreviated version!
For detailed information about [fructose-bisphosphate aldolase]-lysine N-methyltransferase, go to the full flat file.
Reaction
3 S-adenosyl-L-methionine + = 3 S-adenosyl-L-homocysteine +
Synonyms
chloroplastic protein methyltransferase, large subunit of Rubisco methyltransferase, large subunit Rubisco methyltransferase, LSMT, LSMT-L, protein-lysine methyltransferase-like, PsLSMT, rbcMT, Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilonN-methyltransferase, Ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase, Rubisco methyltransferase, S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase
ECTree
Advanced search results
Engineering
Engineering on EC 2.1.1.259 - [fructose-bisphosphate aldolase]-lysine N-methyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
247H/Ins254A/R259W
mutant is able to methylate both Rubisco and fructose 1,6-bisphosphate aldolase with similar efficiency
I242V
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
Ins254A
enzyme is able to methylate Rubisco in addition to fructose 1,6-bisphosphate aldolase
Ins254A/R259W
mutation enhances methylation of Rubisco without altering fructose 1,6-bisphosphate aldolase methylation
P240A
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
R259W
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
S299P
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
V269L
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
Y247H
mutant is not able to methylate Rubisco, activity is severely impaired
additional information
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
additional information
-
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
additional information
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
additional information
-
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
additional information
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
additional information
-
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
additional information
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
additional information
-
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