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Information on EC 2.3.1.232 - methanol O-anthraniloyltransferase and Organism(s) Vitis labrusca and UniProt Accession Q3ZPN4
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EC Tree
2.3.1.232 methanol O-anthraniloyltransferaseIUBMB Comments
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.
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The taxonomic range for the selected organisms is: Vitis labrusca
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
anthraniloyl-coenzyme a (coa):methanol acyltransferase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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.
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
anthraniloyl-CoA + methanol
CoA + O-methyl anthranilate
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)
-
-
?
anthraniloyl-CoA + methanol
CoA + O-methyl anthranilate
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. The enzyme also shows benzyl alcohol O-benzoyltransferase activity, EC 2.3.1.196
-
-
?
NATURAL SUBSTRATE
NATURAL 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
anthraniloyl-CoA + methanol
CoA + O-methyl anthranilate
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)
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00251
anthraniloyl-CoA
pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme
0.00478
anthraniloyl-CoA
pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme
0.015
methanol
pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme
0.032
methanol
pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
anthraniloyl-CoA
pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme
0.022
anthraniloyl-CoA
pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme
0.0035
methanol
pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme
0.0058
methanol
pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.07
anthraniloyl-CoA
pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme
8.9
anthraniloyl-CoA
pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme
0.18
methanol
pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme
0.24
methanol
pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp
the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp
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). ACMAT_VITLA
449
0
50182
Swiss-Prot
Chloroplast (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
three anthranilate derivatives, N-methylanthranilate, methyl anthranilate, and methyl N-methylanthranilate are synthesized using metabolically engineered stains of Escherichia coli. NMT encoding N-methyltransferase from Ruta graveolens, AMAT encoding anthraniloyl-coenzyme A (CoA):methanol acyltransferase from Vitis labrusca, and pqsA encoding anthranilate coenzyme A ligase from Pseudomonas aeruginosa are cloned and Eschetrichia coli strains harboring these genes were used to synthesize the three desired compounds. Escherichia coli mutants (metJ, trpD, tyrR mutants), which provide more anthranilate and/or S-adenosyl methionine, are used to increase the production of the synthesized compounds. 0.1853 mM N-methylanthranilate and 0.0952 mM methyl N-methylanthranilate are synthesized
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, J.; De Luca, V.
The biosynthesis and regulation of biosynthesis of Concord grape fruit esters, including foxy methylanthranilate
Plant J.
44
606-619
2005
Vitis labrusca (Q3ZPN4)
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Release 2023.1 (January 2023)
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