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Literature summary for 2.1.1.100 extracted from

  • Lu, Q.; Harrington, E.O.; Hai, C.M.; Newton, J.; Garber, M.; Hirase, T.; Rounds, S.
    Isoprenylcysteine carboxyl methyltransferase modulates endothelial monolayer permeability: involvement of RhoA carboxyl methylation (2004), Circ. Res., 94, 306-315.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
adenosine plus homocysteine Bos taurus
N-acetyl-S-geranylgeranyl-L-cysteine
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Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + (RhoAA) C-terminal S-farnesyl-L-cysteine Bos taurus the enzyme modulates endothelial monolayer per meability by altering RhoA carboxyl methylation and activation, thus changing the organization of intercellular junctions. Carboxy methylation of RhoA may modulate endothelial barrier function S-adenosyl-L-homocysteine + (RhoA) C-terminal S-farnesyl-L-cysteine methyl ester
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?

Organism

Organism UniProt Comment Textmining
Bos taurus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
pulmonary artery endothelial cell stably overexpressing isoprenylcysteine carboxyl methyltransferase/GFP cDNA Bos taurus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + (RhoAA) C-terminal S-farnesyl-L-cysteine
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Bos taurus S-adenosyl-L-homocysteine + (RhoA) C-terminal S-farnesyl-L-cysteine methyl ester
-
?
S-adenosyl-L-methionine + (RhoAA) C-terminal S-farnesyl-L-cysteine the enzyme modulates endothelial monolayer per meability by altering RhoA carboxyl methylation and activation, thus changing the organization of intercellular junctions. Carboxy methylation of RhoA may modulate endothelial barrier function Bos taurus S-adenosyl-L-homocysteine + (RhoA) C-terminal S-farnesyl-L-cysteine methyl ester
-
?

Synonyms

Synonyms Comment Organism
Icmt
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Bos taurus
isoprenylcysteine carboxyl methyltransferase
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Bos taurus