Information on EC 2.1.1.145 - trans-aconitate 3-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.145
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RECOMMENDED NAME
GeneOntology No.
trans-aconitate 3-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate 3'-O-methyltransferase
Also catalyses the formation of the methyl monoester of cis-aconitate, isocitrate and citrate, but more slowly. While the enzyme from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate as the product, that from Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.144, trans-aconitate 2-methyltransferase)
CAS REGISTRY NUMBER
COMMENTARY hide
235107-12-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + (2R,3R)/(2S,3S)-3-isopropylmalate
S-adenosyl-L-homocysteine + ?
show the reaction diagram
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poor substrate
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-
?
S-adenosyl-L-methionine + (2R,3S)-3-isopropylmalate
S-adenosyl-L-homocysteine + ?
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + (2S,3R)-3-isopropylmalate
S-adenosyl-L-homocysteine + ?
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + 2-(1-methylethylidine)succinate
S-adenosyl-L-homocysteine + ?
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + 3-butylmalate
S-adenosyl-L-homocysteine + ?
show the reaction diagram
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-
-
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?
S-adenosyl-L-methionine + cis-aconitate
S-adenosyl-L-homocysteine + (Z)-2-(methoxycarbonylmethyl)butenedioate
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + isopropylfumarate
S-adenosyl-L-homocysteine + ?
show the reaction diagram
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poor substrate
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-
?
S-adenosyl-L-methionine + isopropylmaleate
S-adenosyl-L-homocysteine + ?
show the reaction diagram
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-
-
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?
S-adenosyl-L-methionine + itaconate
S-adenosyl-L-homocysteine + ?
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + trans-aconitate
S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate
show the reaction diagram
additional information
?
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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
S-adenosyl-L-methionine + trans-aconitate
S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate
show the reaction diagram
additional information
?
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the enzyme may work in two different pathways in two different ways: for detoxification in the citric acid cycle and for a possibly novel biosynthetic branch reaction of the leucine biosynthetic pathway
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
trans-aconitate
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0.5-1 mM, when cis-aconitate is used as substrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.428
(2R,3R)/(2S,3S)-3-isopropylmalate
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0.127
(2R,3S)-3-isopropylmalate
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0.341
(2S,3R)-3-isopropylmalate
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0.019
2-(1-methylethylidine)succinate
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0.045
3-butylmalate
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74
cis-aconitate
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1.67
isopropylfumarate
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0.323
isopropylmaleate
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44
Itaconate
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0.053 - 0.66
trans-aconitate
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcription level of trans-aconitate 3-methyltransferase is enhanced by almost 3fold during riboflavin production comparing to that during its growth phase