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Literature summary extracted from

  • Wang, J.; De Luca, V.
    The biosynthesis and regulation of biosynthesis of Concord grape fruit esters, including ’foxy’ methylanthranilate (2005), Plant J., 44, 606-619.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.196 expression in Escherichia coli Vitis labrusca
2.3.1.232 expression in Escherichia coli Vitis labrusca

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.196 Cu2+
-
 Vitis labrusca
2.3.1.196 Zn2+
-
 Vitis labrusca
2.3.1.232 Cu2+
-
 Vitis labrusca
2.3.1.232 Zn2+
-
 Vitis labrusca

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.196 0.00842
-
 benzoyl-CoA pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme Vitis labrusca
2.3.1.196 0.0118
-
 benzoyl-CoA pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme Vitis labrusca
2.3.1.232 0.00251
-
 anthraniloyl-CoA pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme Vitis labrusca
2.3.1.232 0.00478
-
 anthraniloyl-CoA pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme Vitis labrusca
2.3.1.232 0.015
-
 methanol pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme Vitis labrusca
2.3.1.232 0.032
-
 methanol pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme Vitis labrusca

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.196 Ca2+ the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM Vitis labrusca
2.3.1.196 K+ the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM Vitis labrusca
2.3.1.196 Mg2+ the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM Vitis labrusca
2.3.1.196 Mn2+ the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM Vitis labrusca
2.3.1.232 Ca2+ the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM Vitis labrusca
2.3.1.232 K+ the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM Vitis labrusca
2.3.1.232 Mg2+ the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM Vitis labrusca
2.3.1.232 Mn2+ the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM Vitis labrusca

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.196 50000
-
 x * 50000, SDS-PAGE Vitis labrusca
2.3.1.232 50000
-
 x * 50000, SDS-PAGE Vitis labrusca
2.3.1.232 50200
-
 x * 50200, calculated from sequence Vitis labrusca

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.232 anthraniloyl-CoA + methanol Vitis labrusca 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) CoA + O-methyl anthranilate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.196 Vitis labrusca Q3ZPN4
-
-
2.3.1.232 Vitis labrusca Q3ZPN4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.196
-
 Vitis labrusca
2.3.1.232
-
 Vitis labrusca

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.196 berry the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp Vitis labrusca
-
2.3.1.196 mesocarp the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp Vitis labrusca
-
2.3.1.232 berry the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp Vitis labrusca
-
2.3.1.232 mesocarp the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp Vitis labrusca
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.196 benzoyl-CoA + benzyl alcohol
-
 Vitis labrusca CoA + benzyl benzoate
-
 ?
2.3.1.232 anthraniloyl-CoA + methanol 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) Vitis labrusca CoA + O-methyl anthranilate
-
 ?
2.3.1.232 anthraniloyl-CoA + methanol 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 Vitis labrusca CoA + O-methyl anthranilate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.196 ? x * 50000, SDS-PAGE Vitis labrusca
2.3.1.232 ? x * 50000, SDS-PAGE Vitis labrusca
2.3.1.232 ? x * 50200, calculated from sequence Vitis labrusca

Synonyms

EC Number Synonyms Comment Organism
2.3.1.232 AMAT
-
 Vitis labrusca
2.3.1.232 anthraniloyl-coenzyme A (CoA):methanol acyltransferase
-
 Vitis labrusca

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.196 20 22 assay at Vitis labrusca
2.3.1.232 20 22 assay at Vitis labrusca

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.1.196 35
-
 30 min, stable Vitis labrusca
2.3.1.196 45
-
 5 min, 80% loss of activity Vitis labrusca
2.3.1.232 35
-
 30 min, stable Vitis labrusca
2.3.1.232 45
-
 5 min, 80% loss of activity Vitis labrusca

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.196 0.045
-
 benzoyl-CoA pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme Vitis labrusca
2.3.1.196 0.045
-
 benzoyl-CoA pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme Vitis labrusca
2.3.1.232 0.0035
-
 methanol pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme Vitis labrusca
2.3.1.232 0.0058
-
 methanol pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme Vitis labrusca
2.3.1.232 0.01
-
 anthraniloyl-CoA pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme Vitis labrusca
2.3.1.232 0.022
-
 anthraniloyl-CoA pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme Vitis labrusca

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.196 7.5
-
 assay at Vitis labrusca
2.3.1.232 7.5
-
 assay at Vitis labrusca

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.3.1.196 7 9 stable Vitis labrusca
2.3.1.232 7 9 stable Vitis labrusca

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.196 2.85
-
 benzoyl-CoA pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme Vitis labrusca
2.3.1.196 3.81
-
 benzoyl-CoA pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme Vitis labrusca
2.3.1.232 0.18
-
 methanol pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme Vitis labrusca
2.3.1.232 0.24
-
 methanol pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme Vitis labrusca
2.3.1.232 2.07
-
 anthraniloyl-CoA pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme Vitis labrusca
2.3.1.232 8.9
-
 anthraniloyl-CoA pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme Vitis labrusca