Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.100 extracted from

  • Boivin, D.; Potier, M.; Beliveau, R.
    Functional size of C-terminal protein carboxyl methyltransferase from kidney basolateral plasma membranes (1994), Biochim. Biophys. Acta, 1207, 114-119.
    View publication on PubMed
Search for more literature for 2.1.1.100

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0038
-
 S-adenosyl-L-methionine
-
 Rattus norvegicus
0.03
-
 N-acetyl-S-(E,E)-farnesyl-L-cysteine
-
 Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
basolateral plasma membrane
-
 Rattus norvegicus 16323
-
membrane
-
 Saccharomyces cerevisiae 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
 radiation inactivation Saccharomyces cerevisiae
98000
-
 radiation inactivation Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-
Saccharomyces cerevisiae
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosylmethionine + N-acetyl-S-(E,E)-farnesyl-L-cysteine
-
 Rattus norvegicus S-adenosylhomocysteine + N-acetyl-S-(E,E)-farnesyl-L-cysteine methyl ester
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 24000, deduced from nucleotide sequence Saccharomyces cerevisiae
More enzyme may be a homotetramer Rattus norvegicus