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Information on EC 2.3.2.28 - L-allo-isoleucyltransferase
for references in articles please use BRENDA:EC2.3.2.28
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.2 Aminoacyltransferases
2.3.2.28 L-allo-isoleucyltransferase
IUBMB Comments
The enzyme, characterized from the bacterium Pseudomonas syringae, is involved in the biosynthesis of the toxin coronatine.
The expected taxonomic range for this enzyme is: Pseudomonas syringae group
Reaction Schemes
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holo-[CmaD peptidyl-carrier protein]
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L-allo-isoleucyl-[CmaD peptidyl-carrier protein]
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Synonyms
CmaE, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CmaE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-allo-isoleucyl-[CmaA peptidyl-carrier protein] + holo-[CmaD peptidyl-carrier protein] = L-allo-isoleucyl-[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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
Substrates: 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
Products: -
Products: -
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
Substrates: 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
Products: -
Products: -
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
Substrates: 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
Products: -
Products: -
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
Substrates: 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
Products: -
Products: -
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
Substrates: 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
Products: -
Products: -
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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
Substrates: 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
Products: -
Products: -
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additional information
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Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
Substrates: 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
Products: -
Products: -
?
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
Substrates: 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
Products: -
Products: -
?
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q87W57_PSESM
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
282
0
31765
TrEMBL
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C105A
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
EXTERNAL LINKS (specific for EC-Number 2.3.2.28)
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