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Information on EC 2.3.1.196 - benzyl alcohol O-benzoyltransferase
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2.3.1.196 benzyl alcohol O-benzoyltransferaseIUBMB Comments
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 .
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Word Map
- 2.3.1.196
- benzoate
- petunia
-
phenylethyl
- flowers
- jasmonate
- salicin
- solanacearum
-
benzoic
-
benzenoid
-
mitchell
- corolla
- salicaceae
- populus
- cinnamoyl-coa
-
wound-induced
- benzaldehyde
- ethylene
-
benzoylation
The enzyme appears in viruses and cellular organisms
Synonyms
ACT47, ACT49, BEBT, BEBT1, benzoyl CoA:benzyl alcohol/phenylethanol benzoyltransferase, benzoyl-CoA: salicyl alcohol O-benzoyltransferase, benzoyl-CoA:benzyl alcohol benzoyl transferase, benzoyl-CoA:benzyl alcohol/phenylethanol benzoyltransferase, benzoyl-coenzyme A:benzyl alcohol benzoyl transferase, BPBT, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BEBT
BPBT
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
benzoyl-CoA + benzyl alcohol = CoA + benzyl benzoate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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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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
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
43.5% of the activity with benzoyl-CoA
-
-
?
benzoyl-CoA + coniferyl alcohol
coniferyl benzoate + CoA
71% of the activity with salicyl alcohol
-
-
?
benzoyl-CoA + salicyl alcohol
salicyl benzoate + CoA
-
-
-
?
cinnamoyl-CoA + 3-benzyl alcohol
benzyl cinnamate + CoA
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
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
13% of the activity with benzoyl-CoA
-
-
?
acetyl-CoA + benzyl alcohol
benzyl acetate + CoA
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
112% of the activity with benzyl alcohol
-
-
?
benzoyl-CoA + 3-hydroxybenzyl alcohol
3-hydroxybenzyl benzoate + CoA
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
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
-
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
-
-
-
?
benzoyl-CoA + cinnamyl alcohol
cinnamyl benzoate + CoA
44% of the activity with salicyl alcohol
-
-
?
additional information
?
-
coumaroyl-CoA does not act as substrate
-
-
?
additional information
?
-
no activity with acetyl-CoA at concentrations below 1 mM
-
-
?
additional information
?
-
no substrates: cinnamoyl-CoA, coumaroyl-CoA, or caffeoyl-CoA
-
-
?
additional information
?
-
no substrates: cinnamoyl-CoA, coumaroyl-CoA, or caffeoyl-CoA
-
-
?
additional information
?
-
-
no substrates: cinnamoyl-CoA, coumaroyl-CoA, or caffeoyl-CoA
-
-
?
additional information
?
-
no substrates: coumaroyl-CoA, or caffeoyl-CoA
-
-
?
additional information
?
-
no substrates: coumaroyl-CoA, or caffeoyl-CoA
-
-
?
additional information
?
-
-
no substrates: coumaroyl-CoA, or caffeoyl-CoA
-
-
?
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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
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 + 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
-
-
?
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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 50â70% at 5 mM
K+
the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50â70% at 5 mM
Mg2+
the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50â70% at 5 mM
Mn2+
the monovalent and divalent cations K+, Ca2+, Mg2+ and Mn2+ can increase enzyme activity by 50â70% at 5 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
The Ectopic Expression of CaRop1 Modulates the Response of Tobacco Plants to Ralstonia solanacearum and Aphids.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057
3-Hydroxybenzyl alcohol
cosubstrate benzoyl-CoA, pH 7.0, 30°C
0.067
3-Hydroxybenzyl alcohol
cosubstrate benzoyl-CoA, pH 7.0, 30°C
0.246
acetyl-CoA
cosubstrate salicyl alcohol, pH 7.0, 30°C
0.365
acetyl-CoA
cosubstrate benzyl alcohol, pH 7.0, 30°C
0.063
benzoyl-CoA
cosubstrate 3-hydroxybenzyl alcohol, pH 7.0, 30°C
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
0.052
benzoyl-CoA
cosubstrate benzyl alcohol, pH 7.0, 30°C
0.046
benzoyl-CoA
cosubstrate salicyl alcohol, pH 7.0, 30°C
0.395
benzyl alcohol
cosubstrate acetyl-CoA, pH 7.0, 30°C
0.044
salicyl alcohol
cosubstrate benzoyl-CoA, pH 7.0, 30°C
0.339
salicyl alcohol
cosubstrate acetyl-CoA, pH 7.0, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.42
3-Hydroxybenzyl alcohol
cosubstrate benzoyl-CoA, pH 7.0, 30°C
1.97
3-Hydroxybenzyl alcohol
cosubstrate benzoyl-CoA, pH 7.0, 30°C
0.43
acetyl-CoA
cosubstrate salicyl alcohol, pH 7.0, 30°C
0.32
acetyl-CoA
cosubstrate benzyl alcohol, pH 7.0, 30°C
2.25
benzoyl-CoA
cosubstrate 3-hydroxybenzyl alcohol, pH 7.0, 30°C
2.01
benzoyl-CoA
cosubstrate 3-hydroxybenzyl alcohol, pH 7.0, 30°C
2.25
benzoyl-CoA
cosubstrate 3-hydroxybenzyl alcohol, pH 7.0, 30°C
0.045
benzoyl-CoA
pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme
0.045
benzoyl-CoA
pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme
1.72
benzoyl-CoA
cosubstrate benzyl alcohol, pH 7.0, 30°C
0.4
benzyl alcohol
cosubstrate acetyl-CoA, pH 7.0, 30°C
0.35
salicyl alcohol
cosubstrate acetyl-CoA, pH 7.0, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
32.6
3-Hydroxybenzyl alcohol
cosubstrate benzoyl-CoA, pH 7.0, 30°C
30.4
3-Hydroxybenzyl alcohol
cosubstrate benzoyl-CoA, pH 7.0, 30°C
2.85
benzoyl-CoA
pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme
45
benzoyl-CoA
cosubstrate salicyl alcohol, pH 7.0, 30°C
35.5
benzoyl-CoA
cosubstrate 3-hydroxybenzyl alcohol, pH 7.0, 30°C
33.2
benzoyl-CoA
cosubstrate benzyl alcohol, pH 7.0, 30°C
32.1
benzoyl-CoA
cosubstrate 3-hydroxybenzyl alcohol, pH 7.0, 30°C
3.81
benzoyl-CoA
pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme
30.4
benzyl alcohol
cosubstrate benzoyl-CoA, pH 7.0, 30°C
46.6
salicyl alcohol
cosubstrate benzoyl-CoA, pH 7.0, 30°C
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
brenda
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
brenda
the majority of the enzyme in grape tissues is localized to the outer fruit mesocarp
brenda
the BEBT gene is expressed in different parts of the flowers with maximal RNA transcript levels in the stigma
brenda
the BEBT gene is expressed in different parts of the flowers with maximal RNA transcript levels in the stigma
brenda
no expression in the leaves under normal conditions. BEBT expression is induced in damaged leaves, reaching a maximum 6 h after damage occurres
brenda
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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
metabolism
the enzyme is involved in benzenoid biosynthetic pathway
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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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)
BEBT1_PETHY
460
0
51042
Swiss-Prot
other Location (Reliability: 2)
BEBT_CLABR
456
0
50650
Swiss-Prot
other Location (Reliability: 2)
BEBT_TOBAC
460
0
51014
Swiss-Prot
other Location (Reliability: 3)
A0A5B7ARG0_DAVIN
459
0
50959
TrEMBL
Mitochondrion (Reliability: 5)
A0A396HC61_MEDTR
528
0
60090
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6PB83_ROSCH
526
1
58487
TrEMBL
other Location (Reliability: 2)
A0A2P6PRD1_ROSCH
463
0
51070
TrEMBL
other Location (Reliability: 5)
A0A5B6ZKD1_DAVIN
99
0
11008
TrEMBL
Chloroplast (Reliability: 5)
A0A5B7AR44_DAVIN
223
0
25187
TrEMBL
other Location (Reliability: 4)
A0A5B7B7N2_DAVIN
491
0
54042
TrEMBL
Mitochondrion (Reliability: 4)
A0A396JP14_MEDTR
112
0
12801
TrEMBL
Chloroplast (Reliability: 4)
G7I7F5_MEDTR
452
0
49682
TrEMBL
other Location (Reliability: 5)
A0A2P6PB55_ROSCH
462
0
51420
TrEMBL
Mitochondrion (Reliability: 2)
G7LGU8_MEDTR
130
0
14712
TrEMBL
other Location (Reliability: 5)
A0A2G9HPK0_9LAMI
176
0
19873
TrEMBL
other Location (Reliability: 2)
A0A396JM46_MEDTR
147
0
16587
TrEMBL
other Location (Reliability: 4)
A0A072VH86_MEDTR
461
0
51644
TrEMBL
other Location (Reliability: 5)
A0A072UW71_MEDTR
181
0
20417
TrEMBL
Mitochondrion (Reliability: 5)
A0A396HDK3_MEDTR
151
0
17190
TrEMBL
other Location (Reliability: 5)
A0A072VG31_MEDTR
458
0
51065
TrEMBL
other Location (Reliability: 3)
A0A5B7C4L0_DAVIN
161
0
17924
TrEMBL
other Location (Reliability: 4)
A0A396HEP6_MEDTR
833
1
94370
TrEMBL
Mitochondrion (Reliability: 3)
A0A2P6PB66_ROSCH
462
0
51403
TrEMBL
Mitochondrion (Reliability: 3)
A0A5B7ATJ3_DAVIN
472
0
52918
TrEMBL
Mitochondrion (Reliability: 5)
A0A5B7AR16_DAVIN
448
0
49709
TrEMBL
Mitochondrion (Reliability: 4)
A0A5B7APY3_DAVIN
119
0
13130
TrEMBL
other Location (Reliability: 3)
A0A396H7Y3_MEDTR
174
0
19136
TrEMBL
Mitochondrion (Reliability: 3)
I3SUK4_MEDTR
98
0
11287
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6PB78_ROSCH
435
0
48511
TrEMBL
Mitochondrion (Reliability: 5)
A0A2G9HPC7_9LAMI
181
0
20498
TrEMBL
other Location (Reliability: 3)
A0A396HK92_MEDTR
270
0
29895
TrEMBL
other Location (Reliability: 1)
A0A396H7Z0_MEDTR
478
0
54009
TrEMBL
other Location (Reliability: 4)
A0A396HGQ8_MEDTR
65
1
7297
TrEMBL
other Location (Reliability: 3)
A0A396JQE5_MEDTR
477
0
52639
TrEMBL
Secretory Pathway (Reliability: 1)
A0A513ZRY2_POLTB
123
0
13722
TrEMBL
other Location (Reliability: 2)
A0A2P6PB74_ROSCH
435
0
48497
TrEMBL
Mitochondrion (Reliability: 5)
G7KFS5_MEDTR
460
0
51711
TrEMBL
other Location (Reliability: 5)
A0A5B7ASR6_DAVIN
254
0
28710
TrEMBL
other Location (Reliability: 5)
A0A396H7X8_MEDTR
492
0
55441
TrEMBL
other Location (Reliability: 3)
A0A2P6PB85_ROSCH
462
0
51146
TrEMBL
Mitochondrion (Reliability: 5)
A0A396HEF2_MEDTR
232
0
26591
TrEMBL
Mitochondrion (Reliability: 5)
A0A396JJM0_MEDTR
117
0
12560
TrEMBL
other Location (Reliability: 3)
G7L0S9_MEDTR
462
0
51661
TrEMBL
other Location (Reliability: 5)
A0A072VH91_MEDTR
417
0
46375
TrEMBL
other Location (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H166A
HTMSD motif altered to ATMSD. 97% loss of activity
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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
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dexter, R.J.; Verdonk, J.C.; Underwood, B.A.; Shibuya, K.; Schmelz, E.A.; Clark, D.G.
Tissue-specific PhBPBT expression is differentially regulated in response to endogenous ethylene
J. Exp. Bot.
59
609-618
2008
Petunia x hybrida
brenda
Orlova, I.; Marshall-Colon, A.; Schnepp, J.; Wood, B.; Varbanova, M.; Fridman, E.; Blakeslee, J.J.; Peer, W.A., Murphy, A.S.; Rhodes, D.; Pichersky, E.; Dudareva, N.
Reduction of benzenoid synthesis in petunia flowers reveals multiple pathways to benzoic acid and enhancement in auxin transport
Plant Cell
18
3458-3475
2006
Petunia x hybrida
brenda
D'Auria, J.C.; Chen, F.; Pichersky, E.
Characterization of an acyltransferase capable of synthesizing benzyl benzoate and other volatile esters in flowers and damaged leaves of Clarkia breweri
Plant Physiol.
130
466-476
2002
Clarkia breweri (Q8GT21), Nicotiana tabacum (Q8GT20)
brenda
Boatright, J.; Negre, F.; Chen, X.; Kish, C.M.; Wood, B.; Peel, G.; Orlova, I.; Gang, D.; Rhodes, D.; Dudareva, N.
Understanding in vivo benzenoid metabolism in petunia petal tissue
Plant Physiol.
135
1993-2011
2004
Petunia x hybrida (Q6E593)
brenda
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)
brenda
Chedgy, R.J.; Koellner, T.G.; Constabel, C.P.
Functional characterization of two acyltransferases from Populus trichocarpa capable of synthesizing benzyl benzoate and salicyl benzoate, potential intermediates in salicinoid phenolic glycoside biosynthesis
Phytochemistry
113
149-159
2015
Populus trichocarpa (A0A0B4VSM7), Populus trichocarpa (B9I6S9), Populus trichocarpa
brenda
Park, S.B.; Kim, J.Y.; Han, J.Y.; Ahn, C.H.; Park, E.J.; Choi, Y.E.
Exploring genes involved in benzoic acid biosynthesis in the Populus davidiana transcriptome and their transcriptional activity upon methyl jasmonate treatment
J. Chem. Ecol.
43
1097-1108
2017
Populus davidiana (A0A1Z1G6V7), Populus davidiana
brenda
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