Information on EC 6.2.1.46 - L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase

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The expected taxonomic range for this enzyme is: Pseudomonas syringae

EC NUMBER
COMMENTARY hide
6.2.1.46
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RECOMMENDED NAME
GeneOntology No.
L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] = AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase (AMP-forming)
This two-domain protein from the bacterium Pseudomonas syringae contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyses the adenylation of L-allo-isoleucine and its attachment to the T domain. The enzyme is involved in the biosynthesis of the toxin coronatine, which mimics the plant hormone jasmonic acid isoleucine. Coronatine promotes opening of the plant stomata allowing bacterial invasion, which is followed by bacterial growth in the apoplast, systemic susceptibility, and disease.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein]
AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
show the reaction diagram
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
show the reaction diagram
ATP + L-allo-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
show the reaction diagram
ATP + L-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
show the reaction diagram
ATP + L-leucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-leucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
show the reaction diagram
ATP + L-valine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
show the reaction diagram
additional information
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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
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein]
AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
show the reaction diagram
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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
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r
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
L-allo-isoleucine
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.5
L-isoleucine
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
1.5
L-leucine
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
1.2
L-valine
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0015
L-allo-isoleucine
Pseudomonas syringae
Q6TNA5
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.012
L-isoleucine
Pseudomonas syringae
Q6TNA5
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.03
L-leucine
Pseudomonas syringae
Q6TNA5
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.023
L-valine
Pseudomonas syringae
Q6TNA5
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0375
L-allo-isoleucine
Pseudomonas syringae
Q6TNA5
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
11201
0.024
L-isoleucine
Pseudomonas syringae
Q6TNA5
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
311
0.02
L-leucine
Pseudomonas syringae
Q6TNA5
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
127
0.019
L-valine
Pseudomonas syringae
Q6TNA5
pH 7.5, 25C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
246
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Pseudomonas syringae pv. syringae FF5 as a FLAG-tagged protein
expression in Escherichia coli
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