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Enzyme Nomenclature
Information on EC 2.3.2.28 - L-allo-isoleucyltransferase
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The expected taxonomic range for this enzyme is: Pseudomonas syringae group
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EC NUMBER 
COMMENTARY 
2.3.2.28
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RECOMMENDED NAME
GeneOntology No.
L-allo-isoleucyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein] + holo-[CmaD peptidyl-carrier protein] = L-allo-isoleucyl-S-[CmaD peptidyl-carrier protein] + holo-[CmaA peptidyl-carrier protein]
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SYSTEMATIC NAME
IUBMB Comments
L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]:holo-[CmaD peptidyl-carrier protein] L-allo-isoleucyltransferase
The enzyme, characterized from the bacterium Pseudomonas syringae, is involved in the biosynthesis of the toxin coronatine.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
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the enzyme is involved in the biosynthesis of coronatine
physiological function
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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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r
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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r
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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r
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
Q87W57
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
Q87W57
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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?
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C105A
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.2.28)
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