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Search The CSA
PDB ID
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Catalytic Site Atlas

CSA LITERATURE entry for 1mlv

E.C. name[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase
SpeciesPisum sativum (Garden pea)
E.C. Number (IntEnz) 2.1.1.127
CSA Homologues of 1mlv1ozv,1p0y,2h21,2h23,2h2e,2h2j,
CSA Entries With UniProtID Q43088
CSA Entries With EC Number 2.1.1.127
PDBe Entry 1mlv
PDBSum Entry 1mlv
MACiE Entry 1mlv

Literature Report

IntroductionRibulose-1,5-bisphosphate carboxylase-oxygenase large subunit N-methyltransferase enzymes (LSMTs) uses S-adenosyl methionine to methylate Lys 14 of the Rubisco large subunit. Lys 14 is situated in the flexible N-terminal tail of the large subunit, and the precise role of its methylation is not clear. It does not affect the activity of Rubisco but may be involved in targeting other proteins to interact with the tail.
MechansimThe ionised form of Tyr 287 deprotonates the -NH3+ group of Lys 14 (on the large subunit of Rubisco). The resulting Lys-NH2 group can then attack the methyl group of the AdoMet sulphonium cation. It is proposed that the pKa of Tyr 287 is depressed (so allowing it to be present in the ionised form which can act as a general base) by the proximity of two positively charged groups: the AdoMet sulfonium cation and the epsilon-ammonium group of the substrate lysine.
Reaction

Catalytic Sites for 1mlv

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrA287287macie:sideChainRemoves proton from Lys14-NH3+ to generate the nucleophilic species Lys14-NH2.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrB287287macie:sideChainRemoves proton from Lys14-NH3+ to generate the nucleophilic species Lys14-NH2.

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrC287287macie:sideChainRemoves proton from Lys14-NH3+ to generate the nucleophilic species Lys14-NH2.

Literature References

Notes:
Trievel RC
Structure and catalytic mechanism of a SET domain protein methyltransferase.
Cell 2002 111 91-103
PubMed: 12372303
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