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L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine + [CmaD-protein]-4'-phosphopantetheine
[CmaA-protein-T-domain]-4'-phosphopantetheine + L-valyl-[CmaD-protein]-4'-phosphopantetheine
S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine + [CmaD-protein]-4'-phosphopantetheine
[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
[CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[CmaD-protein]-4'-phosphopantetheine
additional information
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L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine + [CmaD-protein]-4'-phosphopantetheine
[CmaA-protein-T-domain]-4'-phosphopantetheine + L-valyl-[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
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r
L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine + [CmaD-protein]-4'-phosphopantetheine
[CmaA-protein-T-domain]-4'-phosphopantetheine + L-valyl-[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
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S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine + [CmaD-protein]-4'-phosphopantetheine
[CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[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
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S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine + [CmaD-protein]-4'-phosphopantetheine
[CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[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
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S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheinyl-L-allo-isoleucyl thioester + [CmaD -protein]-4'-phosphopantetheine
[CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[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
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S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheinyl-L-allo-isoleucyl thioester + [CmaD -protein]-4'-phosphopantetheine
[CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[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
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additional information
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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
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additional information
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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
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S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheinyl-L-allo-isoleucyl thioester + [CmaD -protein]-4'-phosphopantetheine
[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
[CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[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
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?
S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheinyl-L-allo-isoleucyl thioester + [CmaD -protein]-4'-phosphopantetheine
[CmaA-protein-T-domain]-4'-phosphopantetheine + S-L-allo-isoleucyl-[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
-
-
?
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physiological function
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the enzyme is involved in the biosynthesis of coronatine
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
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
-
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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
Biochemistry
46
7549-7557
2007
Pseudomonas syringae pv. tomato (Q87W57), Pseudomonas syringae pv. tomato DC3000 (Q87W57)
brenda
Vaillancourt, F.H.; Yeh, E.; Vosburg, D.A.; O'Connor, S.E.; Walsh, C.T.
Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis
Nature
436
1191-1194
2005
Pseudomonas syringae
brenda
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History
2.3.2.28 L-allo-isoleucyltransferase
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