KEGG   ENZYME: 2.1.1.127Help
Entry
EC 2.1.1.127                Enzyme                                 

Name
[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase;
rubisco methyltransferase;
ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase;
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilonN-methyltransferase;
S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase;
RuBisCO methyltransferase;
RuBisCO LSMT
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine N6-methyltransferase
Reaction(IUBMB)
3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-L-lysine = 3 S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6,N6,N6-trimethyl-L-lysine [RN:R05179]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
[ribulose-1,5-bisphosphate carboxylase]-L-lysine
Product
S-adenosyl-L-homocysteine [CPD:C00021];
[ribulose-1,5-bisphosphate carboxylase]-N6,N6,N6-trimethyl-L-lysine
Comment
The enzyme catalyses three successive methylations of Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39). Only the three methylated form is observed [3]. The enzyme from pea (Pisum sativum) also three-methylates a specific lysine in the chloroplastic isoforms of fructose-bisphosphate aldolase (EC 4.1.2.13) [5].
History
EC 2.1.1.127 created 1999, modified 2012
Orthology
K00592  
[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase
Genes
ATH: 
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
CAM: 
FVE: 
PPER: 
CSV: 
RCU: 
POP: 
VVI: 
SLY: 
SOT: 
DOSA: 
Os09t0411650-01(Os09g0411650)
OBR: 
BDI: 
SBI: 
SORBI_02g024510(SORBIDRAFT_02g024510)
ZMA: 
SITA: 
ATR: 
s00010p00267610(AMTR_s00010p00267610)
SMO: 
PPP: 
CRE: 
VCN: 
MIS: 
MPP: 
BPG: 
CSL: 
CVR: 
GSL: 
CCP: 
PIF: 
NGD: 
EHX: 
GTT: 
 » show all
Taxonomy
Reference
1  [PMID:8527940]
  Authors
Wang P, Royer M, Houtz RL.
  Title
Affinity purification of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilon N-methyltransferase.
  Journal
Protein. Expr. Purif. 6 (1995) 528-36.
  Organism
Pisum sativum, Spinacia oleracea
Reference
2  [PMID:8980518]
  Authors
Ying Z, Janney N, Houtz RL.
  Title
Organization and characterization of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilon N-methyltransferase gene in tobacco.
  Journal
Plant. Mol. Biol. 32 (1996) 663-71.
  Organism
Nicotiana tabacum
  Sequence
[up:P94026]
Reference
3  [PMID:17338551]
  Authors
Dirk LM, Flynn EM, Dietzel K, Couture JF, Trievel RC, Houtz RL
  Title
Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases.
  Journal
Biochemistry. 46 (2007) 3905-15.
Reference
4  [PMID:17635932]
  Authors
Magnani R, Nayak NR, Mazarei M, Dirk LM, Houtz RL
  Title
Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase.
  Journal
J. Biol. Chem. 282 (2007) 27857-64.
Reference
5  [PMID:22547063]
  Authors
Mininno M, Brugiere S, Pautre V, Gilgen A, Ma S, Ferro M, Tardif M, Alban C, Ravanel S
  Title
Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants.
  Journal
J. Biol. Chem. 287 (2012) 21034-44.
  Organism
Pisum sativum
  Sequence
[up:Q43088]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
139171-98-5

DBGET integrated database retrieval system