Literature summary for 2.1.1.259 extracted from

Ma, S.; Martin-Laffon, J.; Mininno, M.; Gigarel, O.; Brugiere, S.; Bastien, O.; Tardif, M.; Ravanel, S.; Alban, C.
Molecular evolution of the substrate specificity of chloroplastic aldolases/Rubisco lysine methyltransferases in plants (2016), Mol. Plant, 9, 569-581 .

Search for more literature for 2.1.1.259

Cloned(Commentary)

Cloned (Comment)	Organism
sequence comparisons and phylogenetic tree, recombinant expression of His-tagged chimeric enzyme mutants in Escherichia coli	Pisum sativum
sequence comparisons and phylogenetic tree, recombinant expression of His-tagged chimeric enzyme mutants in Escherichia coli	Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
247H/Ins254A/R259W	mutant is able to methylate both Rubisco and fructose 1,6-bisphosphate aldolase with similar efficiency	Arabidopsis thaliana
I242V	mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT	Arabidopsis thaliana
Ins254A	enzyme is able to methylate Rubisco in addition to fructose 1,6-bisphosphate aldolase	Arabidopsis thaliana
Ins254A/R259W	mutation enhances methylation of Rubisco without altering fructose 1,6-bisphosphate aldolase methylation	Arabidopsis thaliana
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	Pisum sativum
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	Arabidopsis thaliana
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	Pisum sativum
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	Arabidopsis thaliana
P240A	mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT	Arabidopsis thaliana
R259W	mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT	Arabidopsis thaliana
S299P	mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT	Arabidopsis thaliana
V269L	mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT	Arabidopsis thaliana
Y247H	mutant is not able to methylate Rubisco, activity is severely impaired	Arabidopsis thaliana

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chloroplast	-	Pisum sativum	9507	-
chloroplast	-	Arabidopsis thaliana	9507	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
3 adenosyl-L-methionine + [Rubisco large subunit]-L-lysine	Pisum sativum	-	3 S-adenosyl-L-homocysteine + [Rubisco large subunit]-N6,N6,N6-trimethyl-L-lysine	-	?
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine	Pisum sativum	-	3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine	-	?
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine	Arabidopsis thaliana	-	3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine	-	?

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9XI84	-	-
Pisum sativum	Q43088	-	-
Pisum sativum	Q43088	cf. EC 2.1.1.127	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged chimeric enzyme mutants from Escherichia coli by nickel affinity chromatography	Pisum sativum
recombinant His-tagged chimeric enzyme mutants from Escherichia coli by nickel affinity chromatography	Arabidopsis thaliana

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Pisum sativum	-
leaf	-	Arabidopsis thaliana	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3 adenosyl-L-methionine + [Rubisco large subunit]-L-lysine	-	Pisum sativum	3 S-adenosyl-L-homocysteine + [Rubisco large subunit]-N6,N6,N6-trimethyl-L-lysine	-	?
3 adenosyl-L-methionine + [Rubisco large subunit]-L-lysine	i.e. RBCL	Pisum sativum	3 S-adenosyl-L-homocysteine + [Rubisco large subunit]-N6,N6,N6-trimethyl-L-lysine	-	?
3 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine394	-	Arabidopsis thaliana	3 S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine394	-	?
3 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase]-L-lysine	-	Pisum sativum	3 S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine	-	?
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine	-	Pisum sativum	3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine	-	?
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine	-	Arabidopsis thaliana	3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine	-	?
3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-lysine	-	Pisum sativum	3 S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6,N6,N6-trimethyl-L-lysine	-	?
additional information	no trimethylation of the Rubisco large subunit by the enzyme from Arabidosis thaliana	Arabidopsis thaliana	?	-	-

Synonyms

Synonyms	Comment	Organism
chloroplastic protein methyltransferase	-	Pisum sativum
chloroplastic protein methyltransferase	-	Arabidopsis thaliana
large subunit Rubisco methyltransferase	-	Pisum sativum
LSMT	-	Pisum sativum
LSMT	-	Arabidopsis thaliana
PsLSMT	-	Pisum sativum
rbcMT	-	Pisum sativum
rbcMT	-	Arabidopsis thaliana

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	-	Pisum sativum
S-adenosyl-L-methionine	-	Arabidopsis thaliana

General Information

General Information	Comment	Organism
evolution	molecular evolution of the substrate specificity of chloroplastic aldolases/Rubisco lysine methyltransferases in plants, overview. The His-Ala/Pro-Trp triad located in the central part of LSMT enzymes is the key motif to confer the capacity to trimethylate Rubisco. Two of the critical residues are located on a surface loop outside the methyltransferase catalytic site. A strict correlation between the presence of the triad motif and the in vivo methylation status of Rubisco is observed, distribution of the motif into a phylogenetic tree, overview. Chloroplastic fructose-1,6-bisphosphate aldolases (FBAs) are naturally trimethylated in both Pisum sativum and Arabidopsis thaliana, whereas the Rubisco large subunit is trimethylated only in the former species. The distribution of the motif into a phylogenetic tree further suggests that the ancestral function of LSMT was FBA trimethylation. In a recent event during higher plant evolution, this function evolved in ancestors of Fabaceae, Cucurbitaceae, and Rosaceae to include Rubisco as an additional substrate to the archetypal enzyme	Pisum sativum
evolution	molecular evolution of the substrate specificity of chloroplastic aldolases/Rubisco lysine methyltransferases in plants, overview. The His-Ala/Pro-Trp triad located in the central part of LSMT enzymes is the key motif to confer the capacity to trimethylate Rubisco. Two of the critical residues are located on a surface loop outside the methyltransferase catalytic site. A strict correlation between the presence of the triad motif and the in vivo methylation status of Rubisco is observed, distribution of the motif into a phylogenetic tree, overview. Chloroplastic fructose-1,6-bisphosphate aldolases (FBAs) are naturally trimethylated in both Pisum sativum and Arabidopsis thaliana, whereas the Rubisco large subunit is trimethylated only in the former species. The distribution of the motif into a phylogenetic tree further suggests that the ancestral function of LSMT was FBA trimethylation. In a recent event during higher plant evolution, this function evolved in ancestors of Fabaceae, Cucurbitaceae, and Rosaceae to include Rubisco as an additional substrate to the archetypal enzyme	Arabidopsis thaliana
additional information	structure of PsLSMT enzyme in complex with the AdoMet structural analogue aza-adenosyl-Lmethionine (PDB ID 2H2E), overview	Pisum sativum

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Release 2023.1 (January 2023)