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Information on EC 2.3.1.196 - benzyl alcohol O-benzoyltransferase and Organism(s) Clarkia breweri and UniProt Accession Q8GT21

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IUBMB 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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This record set is specific for:
Clarkia breweri
UNIPROT: Q8GT21
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Word Map
The taxonomic range for the selected organisms is: Clarkia breweri
The enzyme appears in selected viruses and cellular organisms
Synonyms
phbpbt, hsr201, benzoyl-coa:benzyl alcohol/phenylethanol benzoyltransferase, benzyl alcohol o-benzoyltransferase, benzoyl-coa:benzyl alcohol o-benzoyltransferase, benzoyl coa:benzyl alcohol/phenylethanol benzoyltransferase, benzoyl-coa salicyl alcohol o-benzoyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
benzoyl-CoA:benzyl alcohol benzoyl transferase
-
benzoyl-coenzyme A:benzyl alcohol benzoyl transferase
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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].
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 + benzyl alcohol
benzyl acetate + CoA
show the reaction diagram
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
-
-
?
benzoyl-CoA + benzyl alcohol
benzyl benzoate + CoA
show the reaction diagram
benzoyl-CoA + cinnamyl alcohol
cinnamyl benzoate + CoA
show the reaction diagram
-
-
-
?
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
-
-
?
additional information
?
-
coumaroyl-CoA does not act as substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
benzoyl-CoA + benzyl alcohol
benzyl benzoate + CoA
show the reaction diagram
the enzyme catalyzes the formation of benzyl benzoate, a minor constituent of the Clarkia breweri floral aroma
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
5 mM, strong inhibition
Co2+
5 mM, strong inhibition
Cu2+
5 mM, strong inhibition
Mg2+
5 mM, strong inhibition
Zn2+
5 mM, strong inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.818
acetyl-CoA
pH 7.7, 22°C, cosustrate: benzyl alcohol
0.0205
benzoyl-CoA
pH 7.7, 22°C, cosustrate: benzyl alcohol
0.0468
benzyl alcohol
pH 7.7, 22°C, cosustrate: benzoyl-CoA
0.464
cinnamoyl-CoA
pH 7.7, 22°C, cosustrate: benzyl alcohol
0.0978
cinnamyl alcohol
pH 7.7, 22°C, cosustrate: benzoyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.5
acetyl-CoA
pH 7.7, 22°C, cosustrate: benzyl alcohol
124
benzoyl-CoA
pH 7.7, 22°C, cosustrate: benzyl alcohol
85.2
benzyl alcohol
pH 7.7, 22°C, cosustrate: benzoyl-CoA
0.9
cinnamoyl-CoA
pH 7.7, 22°C, cosustrate: benzyl alcohol
47.2
cinnamyl alcohol
pH 7.7, 22°C, cosustrate: benzoyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17.5
acetyl-CoA
pH 7.7, 22°C, cosustrate: benzyl alcohol
2.5
benzoyl-CoA
pH 7.7, 22°C, cosustrate: benzyl alcohol
4
benzyl alcohol
pH 7.7, 22°C, cosustrate: benzoyl-CoA
0.4
cinnamoyl-CoA
pH 7.7, 22°C, cosustrate: benzyl alcohol
4.6
cinnamyl alcohol
pH 7.7, 22°C, cosustrate: benzoyl-CoA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
pH 6.5: 39% of maximal activity, pH 9.0: 69% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the BEBT gene is expressed in different parts of the flowers with maximal RNA transcript levels in the stigma
Manually annotated by BRENDA team
no expression in the leaves under normal conditions. BEBT expression is induced in damaged leaves, reaching a maximum 6 h after damage occurres
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme catalyzes the formation of benzyl benzoate, a minor constituent of the Clarkia breweri floral aroma
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BEBT_CLABR
456
0
50650
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000 - 49500
gel filtration
50650
calculated from sequence
55000
1 * 55000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
30 min, stable
37
30 min, 20% 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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team