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Results 1 - 8 of 8
EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.58farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate both subunits would appear to have a role in binding and orienting the leaving group of farnesyl diphosphate approximately for catalysis 637521
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.58farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate enzyme constitutes the protein prenyltransferase family of enzymes 636537, 637503, 637507, 637523
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.58farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate farnesyl diphosphate binds exclusively to the beta subunit 637505
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.58farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate farnesyl diphosphate binds the enzyme in a two step process that may involve an enzyme conformational change, the enzyme-substrate complex then rapidly reacts with the peptide substrate to form a product, and product release is the rate-limiting step in catalysis 636537, 637499
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.58farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate kinetic mechanism 636537, 637499, 637502, 637503, 637513, 637514, 637523
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.58farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate leucine makes the protein a substrate for EC 2.5.1.59. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Substrates of prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heteotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. A zinc metalloenzyme that requires Mg2+ for activity -
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.58farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate The enzyme preferentially farnesylates CaaX sequences ending in methionine, cysteine or serine. Enzyme also attaches geranylgeraniol to some CaaX sequences ending in methionine, leucine and cysteine. Substrate overlap may occur between the Saccharomyces cerevisae farnesyl transferase and geranylgeranyltransferase types I in vivo 637507
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.58farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate This enzyme, along with geranylgeranyltransferase types I, EC 2.5.1.59 and II, EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine -
Results 1 - 8 of 8