Information on EC 2.3.1.232 - methanol O-anthraniloyltransferase

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The expected taxonomic range for this enzyme is: Vitis labrusca

EC NUMBER
COMMENTARY hide
2.3.1.232
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RECOMMENDED NAME
GeneOntology No.
methanol O-anthraniloyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
anthraniloyl-CoA + methanol = CoA + O-methyl anthranilate
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
anthraniloyl-CoA:methanol O-anthraniloyltransferase
The enzyme from Concord grape (Vitis labrusca) is solely responsible for the production of O-methyl anthranilate, an important aroma and flavor compound in the grape. The enzyme has a broad substrate specificity, and can use a range of alcohols with substantial activity, the best being butanol, benzyl alcohol, iso-pentanol, octanol and 2-propanol. It can use benzoyl-CoA and acetyl-CoA as acyl donors with lower efficiency. In addition to O-methyl anthranilate, the enzyme might be responsible for the production of ethyl butanoate, methyl-3-hydroxy butanoate and ethyl-3-hydroxy butanoate, which are present in large quantities in the grapes. Also catalyses EC 2.3.1.196, benzyl alcohol O-benzoyltransferase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
anthraniloyl-CoA + methanol
CoA + O-methyl anthranilate
show the reaction diagram
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
anthraniloyl-CoA + methanol
CoA + O-methyl anthranilate
show the reaction diagram
Q3ZPN4
the enzyme is solely responsible for the production of O-methyl anthranilate, an important aroma and flavor compound in the grape. In addition to O-methyl anthranilate, the enzyme might be responsible for the production of ethyl butanoate, methyl-3-hydroxy butanoate and ethyl-3-hydroxy butanoate, which are present in large quantities in the Washington Concord grape (Vitis labrusca)
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 5070% at 5 mM
K+
the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 5070% at 5 mM
Mg2+
the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 5070% at 5 mM
Mn2+
the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 5070% at 5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00251 - 0.00478
anthraniloyl-CoA
0.015 - 0.032
methanol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.022
anthraniloyl-CoA
0.0035 - 0.0058
methanol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.07 - 8.9
anthraniloyl-CoA
6397
0.18 - 0.24
methanol
83
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 22
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp
Manually annotated by BRENDA team
the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 50000, SDS-PAGE; x * 50200, calculated from sequence
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
stable
726171
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
30 min, stable
45
5 min, 80% loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli