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Literature summary for 2.3.2.28 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
Search for more literature for 2.3.2.28

Protein Variants

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
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 ?
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
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 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas syringae pv. tomato Q87W57
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Pseudomonas syringae pv. tomato DC3000 Q87W57
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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 r
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
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 r
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 ?
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 ?
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 ?
-
 ?
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
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
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
-
 ?
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
-
 ?

Synonyms

Synonyms Comment Organism
CmaE
-
 Pseudomonas syringae pv. tomato

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information Comment Organism
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