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Literature summary for 2.1.1.127 extracted from

  • Houtz, R.L.; Royer, M.; Salvucci, M.E.
    Partial purification and characterization of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilonN-methyltransferase (1991), Plant Physiol., 97, 913-920.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
S-adenosyl-L-methionine
-
Nicotiana sp.
0.018
-
ribulose-1,5-bisphosphate carboxylase
-
Nicotiana sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Nicotiana sp. 9507
-

Organism

Organism UniProt Comment Textmining
Nicotiana sp.
-
Nicotiana rustica
-

Purification (Commentary)

Purification (Comment) Organism
partial Nicotiana sp.

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Nicotiana sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Nicotiana sp.

Storage Stability

Storage Stability Organism
-80°C, 300 mM KCl, 5 mM DTT, stable for at least 1 month Nicotiana sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + ribulose-1,5-bisphosphate carboxylase ribulose-1,5-bisphosphate carboxylase from Spinacia sp. Nicotiana sp. ?
-
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine the enzyme does not distinguish between the enzyme form activated by Mg2+ and CO2 and the unactivated enzyme form Nicotiana sp. S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
-
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine inactive on ribulose-bisphosphate-carboxylases that contain trimethyllysyl residues at position 14 in the large subunit Nicotiana sp. S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
-
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine catalyzes methylation of the epsilon-amino group of Lys-14 in the large subunit of ribulose-bisphosphate-carboxylase from Spinacia oleracea Nicotiana sp. S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5 10
-
Nicotiana sp.