Information on EC 2.3.1.196 - benzyl alcohol O-benzoyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.196
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RECOMMENDED NAME
GeneOntology No.
benzyl alcohol O-benzoyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
benzoyl-CoA + benzyl alcohol = CoA + benzyl benzoate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
benzoate biosynthesis I (CoA-dependent, beta-oxidative)
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salicortin biosynthesis
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volatile benzenoid biosynthesis I (ester formation)
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volatile esters biosynthesis (during fruit ripening)
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + 3-hydroxybenzyl alcohol
3-hydroxybenzyl acetate + CoA
show the reaction diagram
41% of the activity with benzoyl-CoA
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?
acetyl-CoA + benzyl alcohol
acetyl benzoate + CoA
show the reaction diagram
turnover number for acetyl is 5-8% of that with benzoyl-CoA
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?
acetyl-CoA + benzyl alcohol
benzyl acetate + CoA
show the reaction diagram
acetyl-CoA + salicyl alcohol
salicyl acetate + CoA
show the reaction diagram
43.5% of the activity with benzoyl-CoA
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?
benzoyl-CoA + 2-phenylethanol
2-phenylethyl benzoate + CoA
show the reaction diagram
benzoyl-CoA + 3-hydroxybenzyl alcohol
3-hydroxybenzyl benzoate + CoA
show the reaction diagram
benzoyl-CoA + benzyl alcohol
benzyl benzoate + CoA
show the reaction diagram
benzoyl-CoA + benzyl alcohol
CoA + benzyl benzoate
show the reaction diagram
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-
-
?
benzoyl-CoA + cinnamyl alcohol
cinnamyl benzoate + CoA
show the reaction diagram
benzoyl-CoA + coniferyl alcohol
coniferyl benzoate + CoA
show the reaction diagram
71% of the activity with salicyl alcohol
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?
benzoyl-CoA + salicyl alcohol
salicyl benzoate + CoA
show the reaction diagram
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?
cinnamoyl-CoA + 3-benzyl alcohol
benzyl cinnamoate + CoA
show the reaction diagram
28.6% of the activity with benzoyl-CoA
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?
cinnamoyl-CoA + benzyl alcohol
? + CoA
show the reaction diagram
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
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?
cinnamoyl-CoA + salicyl alcohol
salicyl cinnamoate + CoA
show the reaction diagram
11.5% of the activity with benzoyl-CoA
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?
additional information
?
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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
benzoyl-CoA + 2-phenylethanol
2-phenylethyl benzoate + CoA
show the reaction diagram
benzoyl-CoA + benzyl alcohol
benzyl benzoate + CoA
show the reaction diagram
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
Ca2+
5 mM, strong inhibition
Co2+
5 mM, strong inhibition
Mg2+
5 mM, strong inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.686
2-phenylethanol
pH 7.7, 22C, cosubstrate: 2-phenylethanol
0.057 - 0.067
3-Hydroxybenzyl alcohol
0.246 - 0.818
acetyl-CoA
0.00842 - 1.56
benzoyl-CoA
0.019 - 0.444
benzyl alcohol
0.464
cinnamoyl-CoA
pH 7.7, 22C, cosustrate: benzyl alcohol
0.0978
cinnamyl alcohol
pH 7.7, 22C, cosustrate: benzoyl-CoA
0.044 - 0.339
salicyl alcohol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
35.8
2-phenylethanol
Petunia x hybrida
Q6E593
pH 7.7, 22C, cosubstrate: 2-phenylethanol
1.42 - 1.97
3-Hydroxybenzyl alcohol
0.32 - 21.5
acetyl-CoA
0.045 - 124
benzoyl-CoA
0.4 - 85.2
benzyl alcohol
0.9
cinnamoyl-CoA
Clarkia breweri
Q8GT21
pH 7.7, 22C, cosustrate: benzyl alcohol
47.2
cinnamyl alcohol
Clarkia breweri
Q8GT21
pH 7.7, 22C, cosustrate: benzoyl-CoA
0.35 - 2.06
salicyl alcohol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
52.8
2-phenylethanol
Petunia x hybrida
Q6E593
pH 7.7, 22C, cosubstrate: 2-phenylethanol
1667
30.4 - 32.6
3-Hydroxybenzyl alcohol
7114
0.9 - 17.5
acetyl-CoA
29
2.5 - 92.2
benzoyl-CoA
394
1 - 83.1
benzyl alcohol
260
0.4
cinnamoyl-CoA
Clarkia breweri
Q8GT21
pH 7.7, 22C, cosustrate: benzyl alcohol
1321
4.6
cinnamyl alcohol
Clarkia breweri
Q8GT21
pH 7.7, 22C, cosustrate: benzoyl-CoA
936
1 - 46.6
salicyl alcohol
6025
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
at least 50% of maximum activity; at least 50% of maximum activity
6.5 - 9
pH 6.5: 39% of maximal activity, pH 9.0: 69% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 22
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.12
calculated from sequence
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
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
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
30% of the activity in stigma
Manually annotated by BRENDA team
30% of the activity in stigma
Manually annotated by BRENDA team
30% of the activity in stigma
Manually annotated by BRENDA team
the BEBT gene is expressed in different parts of the flowers with maximal RNA transcript levels in the stigma
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000 - 49500
gel filtration
50650
calculated from sequence
51010
calculated from sequence
51040
calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 50650, calculated from sequence; 1 * 55000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
stable
726171
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
30 min, stable
35
30 min, stable
37
30 min, 20% loss of activity
45
5 min, 80% loss of activity
50
30 min, complete inactivation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complete, non-fusion BEBT enzyme from the crude Escherichia coli extract
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
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 hide
LITERATURE
H166A
HTMSD motif altered to ATMSD. 97% loss of activity