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Literature summary extracted from

  • Strieter, E.R.; Vaillancourt, F.H.; Walsh, C.T.
    CmaE: a transferase shuttling aminoacyl groups between carrier protein domains in the coronamic acid biosynthetic pathway (2007), Biochemistry, 46, 7549-7557.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.28 C105A inactive mutant enzyme Pseudomonas syringae pv. tomato

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.46 Mg2+ required Pseudomonas syringae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.28 S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheinyl-L-allo-isoleucyl thioester + [CmaD -protein]-4'-phosphopantetheine Pseudomonas syringae pv. tomato the enzyme is involved in the biosynthesis of the toxin coronatine by the bacterium Pseudomonas syringae. The 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 symptoms [CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[CmaD-protein]-4'-phosphopantetheine
-
 ?
2.3.2.28 S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheinyl-L-allo-isoleucyl thioester + [CmaD -protein]-4'-phosphopantetheine Pseudomonas syringae pv. tomato DC3000 the enzyme is involved in the biosynthesis of the toxin coronatine by the bacterium Pseudomonas syringae. The 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 symptoms [CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[CmaD-protein]-4'-phosphopantetheine
-
 ?
6.2.1.46 ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] Pseudomonas syringae 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 AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.28 Pseudomonas syringae pv. tomato Q87W57
-
-
2.3.2.28 Pseudomonas syringae pv. tomato DC3000 Q87W57
-
-
6.2.1.46 Pseudomonas syringae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.28 L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine + [CmaD-protein]-4'-phosphopantetheine 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. CmaE catalyzes the reverse reaction, in which the aminoacyl group is transferred from CmaD back to CmaA Pseudomonas syringae pv. tomato [CmaA-protein-T-domain]-4'-phosphopantetheine + L-valyl-[CmaD-protein]-4'-phosphopantetheine
-
 r
2.3.2.28 L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine + [CmaD-protein]-4'-phosphopantetheine 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. CmaE catalyzes the reverse reaction, in which the aminoacyl group is transferred from CmaD back to CmaA Pseudomonas syringae pv. tomato DC3000 [CmaA-protein-T-domain]-4'-phosphopantetheine + L-valyl-[CmaD-protein]-4'-phosphopantetheine
-
 r
2.3.2.28 additional information CmaD can be loaded with other amino acids, for example, L-Leu and L-Thr, by the action of heterologous donor T domains containing alternative aminoacyl groups. Additionally, CmaE is able to accept L-Phe as a substrate when presented on CmaD and is able to load this aminoacyl moiety onto heterologous T domains Pseudomonas syringae pv. tomato ?
-
 ?
2.3.2.28 additional information CmaD can be loaded with other amino acids, for example, L-Leu and L-Thr, by the action of heterologous donor T domains containing alternative aminoacyl groups. Additionally, CmaE is able to accept L-Phe as a substrate when presented on CmaD and is able to load this aminoacyl moiety onto heterologous T domains Pseudomonas syringae pv. tomato DC3000 ?
-
 ?
2.3.2.28 S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine + [CmaD-protein]-4'-phosphopantetheine 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. CmaE catalyzes the reverse reaction, in which the aminoacyl group is transferred from CmaD back to CmaA Pseudomonas syringae pv. tomato [CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[CmaD-protein]-4'-phosphopantetheine
-
 r
2.3.2.28 S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine + [CmaD-protein]-4'-phosphopantetheine 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. CmaE catalyzes the reverse reaction, in which the aminoacyl group is transferred from CmaD back to CmaA Pseudomonas syringae pv. tomato DC3000 [CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[CmaD-protein]-4'-phosphopantetheine
-
 r
2.3.2.28 S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheinyl-L-allo-isoleucyl thioester + [CmaD -protein]-4'-phosphopantetheine the enzyme is involved in the biosynthesis of the toxin coronatine by the bacterium Pseudomonas syringae. The 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 symptoms Pseudomonas syringae pv. tomato [CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[CmaD-protein]-4'-phosphopantetheine
-
 ?
2.3.2.28 S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheinyl-L-allo-isoleucyl thioester + [CmaD -protein]-4'-phosphopantetheine the enzyme is involved in the biosynthesis of the toxin coronatine by the bacterium Pseudomonas syringae. The 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 symptoms Pseudomonas syringae pv. tomato DC3000 [CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[CmaD-protein]-4'-phosphopantetheine
-
 ?
6.2.1.46 ATP + 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
6.2.1.46 ATP + 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
6.2.1.46 additional information aminoacylated-S-CmaE will transfer the L-Val moiety to the HS-pantetheinyl arm of other T domains, including CytC2, BarA, and ArfA C2-A2-T2 but not to free HS-pantetheine. CmaD can be loaded with other amino acids, for example, L-Leu and L-Thr, by the action of heterologous donor T domains containing alternative aminoacyl groups. Additionally, CmaE is able to accept L-Phe as a substrate when presented on CmaD and is able to load this aminoacyl moiety onto heterologous T domains Pseudomonas syringae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.28 CmaE
-
 Pseudomonas syringae pv. tomato
6.2.1.46 CmaE
-
 Pseudomonas syringae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.28 24
-
 assay at Pseudomonas syringae pv. tomato

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.28 7.5
-
 assay at Pseudomonas syringae pv. tomato

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.46 ATP
-
 Pseudomonas syringae

General Information

EC Number General Information Comment Organism
2.3.2.28 physiological function the enzyme is involved in the biosynthesis of the toxin coronatine by the bacterium Pseudomonas syringae. The 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 symptoms Pseudomonas syringae pv. tomato
6.2.1.46 physiological function the transferase shuttles aminoacyl groups between carrier protein domains in the coronamic acid biosynthetic pathway, overview Pseudomonas syringae