Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.127
Description:[Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase.
Alternative Name: RuBisCO methyltransferase.
RuBisCO LSMT.
Ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase.
Cath: 3.90.1410.10; 3.90.1420.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.127
BRENDA Enzyme Link: BRENDA 2.1.1.127
KEGG Enzyme Link: KEGG2.1.1.127
BioCyc Enzyme Link: BioCyc 2.1.1.127
ExPASy Enzyme Link: ExPASy2.1.1.127
EC2PDB Enzyme Link: EC2PDB 2.1.1.127
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.127
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.127
IntEnz Enzyme Link: IntEnz 2.1.1.127
MEDLINE Enzyme Link: MEDLINE 2.1.1.127
MSA:

2.1.1.127;

Phylogenetic Tree:

2.1.1.127;

Uniprot:
M-CSA:
RHEA:50996 [ribulose-1,5-bisphosphate carboxylase]-L-lysine + 3 S-adenosyl-L-methionine = [ribulose-1,5-bisphosphate carboxylase]-N(6),N(6),N(6)-trimethyl-L-lysine + 3 H(+) + 3 S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6].[*:7]-[S+;H0:8](-[*:9])-[CH3;+0:10].[*:11]-[S+;H0:12](-[*:13])-[CH3;+0:14]>>[*:1]-[N+;H0:2](-[CH3;+0:10])(-[CH3;+0:14])-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5].[*:7]-[S;H0;+0:8]-[*:9].[*:11]-[S;H0;+0:12]-[*:13]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Organization and characterization of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilon N-methyltransferase gene in tobacco.Ying Z, Janney N, Houtz RL1996 Nov8980518
Affinity purification of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilon N-methyltransferase.Wang P, Royer M, Houtz RL1995 Aug8527940
Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants.Mininno M, Brugière S, Pautre V, Gilgen A, Ma S, Ferro M, Tardif M, Alban C, Ravanel S2012 Jun 1522547063
Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase.Magnani R, Nayak NR, Mazarei M, Dirk LM, Houtz RL2007 Sep 2117635932
Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases.Dirk LM, Flynn EM, Dietzel K, Couture JF, Trievel RC, Houtz RL2007 Mar 2717338551