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Literature summary for 2.3.1.232 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
Search for more literature for 2.3.1.232

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Vitis labrusca

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
 Vitis labrusca
Zn2+
-
 Vitis labrusca

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00251
-
 anthraniloyl-CoA pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme Vitis labrusca
0.00478
-
 anthraniloyl-CoA pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme Vitis labrusca
0.015
-
 methanol pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme Vitis labrusca
0.032
-
 methanol pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme Vitis labrusca

Metals/Ions

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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Vitis labrusca Q3ZPN4
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Vitis labrusca

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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

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

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20 22 assay at Vitis labrusca

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Vitis labrusca

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 9 stable Vitis labrusca

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.18
-
 methanol pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme Vitis labrusca
0.24
-
 methanol pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme Vitis labrusca
2.07
-
 anthraniloyl-CoA pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme Vitis labrusca
8.9
-
 anthraniloyl-CoA pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme Vitis labrusca