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Enzyme Nomenclature
Information on EC 2.3.1.196 - benzyl alcohol O-benzoyltransferase
for references in articles please use BRENDA:EC2.3.1.196
Word Map on EC 2.3.1.196
- 2.3.1.196
- benzoate
-
salicylic
- tobacco
- petunia
-
mitchell
- cinnamoyl-coa
- flowers
- salicaceae
- ethylene
-
wound-induced
-
benzenoid
- corolla
-
phenylethyl
- solanacearum
-
benzoylation
-
volatile
-
mitogen-activated
- populus
- jasmonate
- benzaldehyde
-
benzoic
- salicin
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.3.1.196
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RECOMMENDED NAME
GeneOntology No.
benzyl alcohol O-benzoyltransferase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
benzoyl-CoA + benzyl alcohol = CoA + benzyl benzoate
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
benzoyl-CoA:benzyl alcohol O-benzoyltransferase
The enzyme is involved in volatile benzenoid and benzoic acid biosynthesis. The enzyme from Petunia hybrida also catalyses the formation of 2-phenylethyl benzoate from benzoyl-CoA and 2-phenylethanol. The apparent catalytic efficiency of the enzyme from Petunia hybrida with benzoyl-CoA is almost 6-fold higher than with acetyl-CoA [1].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
generation of transgenic petunia plants in which the expression of BPBT, the gene encoding the enzyme that uses benzoyl-CoA and benzyl alcohol to make benzyl benzoate, is reduced or eliminated. Elimination of benzyl benzoate formation decreases the endogenous pool of benzoic acid and methyl benzoate emission but increases emission of benzyl alcohol and benzaldehyde, confirming the contribution of benzyl benzoate to benzoic acid formation. Suppression of BPBT activity also affects the overall morphology of petunia plants, resulting in larger flowers and leaves, thicker stems, and longer internodes, which is consistent with the increased auxin transport in transgenic plants
physiological function
physiological function
-
it is hypothesized that PhBPBT and subsequent benzyl benzoate production is involved in defencerelated processes in the corolla prior to pollination in the ovary immediately following fertilization, and in vegetative tissue in response to wounding
physiological function
the enzyme catalyzes the formation of benzyl benzoate, a minor constituent of the Clarkia breweri floral aroma
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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
acetyl-CoA + 3-hydroxybenzyl alcohol
3-hydroxybenzyl acetate + CoA
A0A0B4VSM7, B9I6S9
41% of the activity with benzoyl-CoA
-
-
?
acetyl-CoA + benzyl alcohol
acetyl benzoate + CoA
turnover number for acetyl is 5-8% of that with benzoyl-CoA
-
-
?
acetyl-CoA + salicyl alcohol
salicyl acetate + CoA
A0A0B4VSM7, B9I6S9
43.5% of the activity with benzoyl-CoA
-
-
?
benzoyl-CoA + coniferyl alcohol
coniferyl benzoate + CoA
A0A0B4VSM7, B9I6S9
71% of the activity with salicyl alcohol
-
-
?
cinnamoyl-CoA + 3-benzyl alcohol
benzyl cinnamate + CoA
A0A0B4VSM7, B9I6S9
28.6% of the activity with benzoyl-CoA
-
-
?
cinnamoyl-CoA + benzyl alcohol
? + CoA
the Km-value for cinnamoyl-CoA (0.464 mM) strongly suggests that acetyl-CoA is not commonly used by BEBT as the acyl donor in vivo
-
-
?
cinnamoyl-CoA + salicyl alcohol
salicyl cinnamoate + CoA
A0A0B4VSM7, B9I6S9
11.5% of the activity with benzoyl-CoA
-
-
?
acetyl-CoA + benzyl alcohol
benzyl acetate + CoA
the Km-value for acetyl-CoA (0.818 mM) strongly suggests that acetyl-CoA is not commonly used by BEBT as the acyl donor in vivo
-
-
?
acetyl-CoA + benzyl alcohol
benzyl acetate + CoA
A0A0B4VSM7, B9I6S9
13% of the activity with benzoyl-CoA
-
-
?
acetyl-CoA + benzyl alcohol
benzyl acetate + CoA
A0A0B4VSM7, B9I6S9
51% of the activity with benzoyl-CoA
-
-
?
benzoyl-CoA + 2-phenylethanol
2-phenylethyl benzoate + CoA
-
PhBPBT is responsible for the biosynthesis of both benzyl benzoate and 2-phenylethyl benzoate from benzyl alcohol and phenylethanol, respectively
-
-
?
benzoyl-CoA + 2-phenylethanol
2-phenylethyl benzoate + CoA
the enzyme is most likely responsible for the formation of both 2-phenylethyl benzoate and benzyl benzoate in vivo
-
-
?
benzoyl-CoA + 3-hydroxybenzyl alcohol
3-hydroxybenzyl benzoate + CoA
A0A0B4VSM7, B9I6S9
112% of the activity with benzyl alcohol
-
-
?
benzoyl-CoA + 3-hydroxybenzyl alcohol
3-hydroxybenzyl benzoate + CoA
A0A0B4VSM7, B9I6S9
97% of the activity with salicyl alcohol
-
-
?
benzoyl-CoA + benzyl alcohol
benzyl benzoate + CoA
the enzyme catalyzes the formation of benzyl benzoate, a minor constituent of the Clarkia breweri floral aroma
-
-
?
benzoyl-CoA + benzyl alcohol
benzyl benzoate + CoA
-
PhBPBT is responsible for the biosynthesis of both benzyl benzoate and 2-phenylethyl benzoate from benzyl alcohol and phenylethanol, respectively
-
-
?
benzoyl-CoA + benzyl alcohol
benzyl benzoate + CoA
the enzyme is most likely responsible for the formation of both 2-phenylethyl benzoate and benzyl benzoate in vivo
-
-
?
benzoyl-CoA + cinnamyl alcohol
cinnamyl benzoate + CoA
A0A0B4VSM7, B9I6S9
44% of the activity with salicyl alcohol
-
-
?
additional information
?
-
coumaroyl-CoA does not act as substrate
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-
-
additional information
?
-
no activity with acetyl-CoA at concentrations below 1 mM
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-
-
additional information
?
-
no substrates: cinnamoyl-CoA, coumaroyl-CoA, or caffeoyl-CoA
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-
-
additional information
?
-
B9I6S9
no substrates: cinnamoyl-CoA, coumaroyl-CoA, or caffeoyl-CoA
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-
-
additional information
?
-
-
no substrates: cinnamoyl-CoA, coumaroyl-CoA, or caffeoyl-CoA
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-
-
additional information
?
-
no substrates: coumaroyl-CoA, or caffeoyl-CoA
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-
-
additional information
?
-
B9I6S9
no substrates: coumaroyl-CoA, or caffeoyl-CoA
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-
-
additional information
?
-
-
no substrates: coumaroyl-CoA, or caffeoyl-CoA
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
benzoyl-CoA + 2-phenylethanol
2-phenylethyl benzoate + CoA
-
PhBPBT is responsible for the biosynthesis of both benzyl benzoate and 2-phenylethyl benzoate from benzyl alcohol and phenylethanol, respectively
-
-
?
benzoyl-CoA + 2-phenylethanol
2-phenylethyl benzoate + CoA
Q6E593
the enzyme is most likely responsible for the formation of both 2-phenylethyl benzoate and benzyl benzoate in vivo
-
-
?
benzoyl-CoA + benzyl alcohol
benzyl benzoate + CoA
Q8GT21
the enzyme catalyzes the formation of benzyl benzoate, a minor constituent of the Clarkia breweri floral aroma
-
-
?
benzoyl-CoA + benzyl alcohol
benzyl benzoate + CoA
-
PhBPBT is responsible for the biosynthesis of both benzyl benzoate and 2-phenylethyl benzoate from benzyl alcohol and phenylethanol, respectively
-
-
?
benzoyl-CoA + benzyl alcohol
benzyl benzoate + CoA
Q6E593
the enzyme is most likely responsible for the formation of both 2-phenylethyl benzoate and benzyl benzoate in vivo
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM
K+
the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM
Mg2+
the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM
Mn2+
the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50–70% at 5 mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00842
benzoyl-CoA
pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme
0.0118
benzoyl-CoA
pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme
0.063
benzoyl-CoA
A0A0B4VSM7, B9I6S9
cosubstrate 3-hydroxybenzyl alcohol, pH 7.0, 30°C; cosubstrate 3-hydroxybenzyl alcohol, pH 7.0, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045
benzoyl-CoA
pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme; pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.85
benzoyl-CoA
pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme
3.81
benzoyl-CoA
pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
pH 6.5: 39% of maximal activity, pH 9.0: 69% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp
BPBT mRNA transcripts predominante in the limb of petunia corollas, the parts of the flower that are primarily responsible for scent production and emission in petunia. The steady-state BPBT mRNA level in corolla limbs is developmentally regulated, peaking 1 to 2 d after anthesis and changing rhythmically during a daily light/dark cycle closely correlating with the pattern of BPBT activity and benzylbenzoate accumulation
the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp
the BEBT gene is expressed in different parts of the flowers with maximal RNA transcript levels in the stigma
the BEBT gene is expressed in different parts of the flowers with maximal RNA transcript levels in the stigma
no expression in the leaves under normal conditions. BEBT expression is induced in damaged leaves, reaching a maximum 6 h after damage occurres
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complete, non-fusion BEBT enzyme from the crude Escherichia coli extract
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
A0A0B4VSM7, B9I6S9
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PhBPBT is regulated by both light and an endogenous circadian rhythm, while it is also differentially regulated in response to ethylene in a tissue-specific manner. 24 hours following pollination of flowers, expression of PhBPBT decreases in the corolla, while it increases in the ovary after 48 h. This is caused by ethylene that is emitted from the flower coinciding with fertilization as this is not observed in transgenic ethylene-insensitive plants (CaMV35S::etr1-1, 44568). Ethylene is also emitted from vegetative tissue of petunia following mechanical wounding, resulting in an increase in PhBPBT expression in the leaves where expression is normally below detection levels
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.196)
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