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Results 1 - 10 of 13 > >>
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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the reaction diagram Show all sequences 6.2.1.46ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] during the biosynthesis of the cyclopropyl amino acid coronamic acid from L-allo-Ile by the phytotoxic Pseudomonas syringae, the aminoacyl group covalently attached to the pantetheinyl arm of CmaA is shuttled to the HS-pantetheinyl arm of the protein CmaD by the aminoacyltransferase CmaE, reversible shuttling process Pseudomonas syringae AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein] - r
Display the reaction diagram Show all sequences 6.2.1.46ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] CmaE will only recognize deacylated CmaA for initial complexation. The aminoacyl group becomes covalently attached to the active site Cys of CmaE and can then be transferred out to the holo pantetheinylated form of CmaD, reversible shuttling process Pseudomonas syringae AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein] - r
Display the reaction diagram Show all sequences 6.2.1.46ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine the didomain protein contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyzes the adenylation of L-allo-isoleucine and the attachment of L-allo-isoleucine to the CmaA T domain. The enzyme-bound L-allo-isoleucine serves as the substrate for the later stages of the biosdynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease Pseudomonas syringae AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine - ?
Display the reaction diagram Show all sequences 6.2.1.46ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine the didomain protein contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyzes the adenylation of L-allo-isoleucine and the attachment of L-allo-isoleucine to the CmaA T domain. The enzyme-bound L-allo-isoleucine serves as the substrate for the later stages of the biosdynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease Pseudomonas syringae pv. glycinea PG4180 AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine - ?
Display the reaction diagram Show all sequences 6.2.1.46ATP + L-allo-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine Pseudomonas syringae AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine - ?
Display the reaction diagram Show all sequences 6.2.1.46ATP + L-allo-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine Pseudomonas syringae pv. glycinea PG4180 AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine - ?
Display the reaction diagram Show all sequences 6.2.1.46ATP + L-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine Pseudomonas syringae AMP + diphosphate + S-L-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine - ?
Display the reaction diagram Show all sequences 6.2.1.46ATP + L-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine Pseudomonas syringae pv. glycinea PG4180 AMP + diphosphate + S-L-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine - ?
Display the reaction diagram Show all sequences 6.2.1.46ATP + L-leucine + [CmaA-protein-T-domain]-4'-phosphopantetheine the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine Pseudomonas syringae AMP + diphosphate + S-L-leucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine - ?
Display the reaction diagram Show all sequences 6.2.1.46ATP + L-leucine + [CmaA-protein-T-domain]-4'-phosphopantetheine the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine Pseudomonas syringae pv. glycinea PG4180 AMP + diphosphate + S-L-leucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine - ?
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