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Information on EC 2.3.1.195 - (Z)-3-hexen-1-ol acetyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SRQ2

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IUBMB Comments
The enzyme is resonsible for the production of (3Z)-hex-3-en-1-yl acetate, the major volatile compound released upon mechanical wounding of the leaves of Arabidopsis thaliana .
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9SRQ2
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Arabidopsis thaliana
Synonyms
at3g03480, acetyl coa:(z)-3-hexen-1-ol acetyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyl CoA:(Z)-3-hexen-1-ol acetyltransferase
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:(3Z)-hex-3-en-ol acetyltransferase
The enzyme is resonsible for the production of (3Z)-hex-3-en-1-yl acetate, the major volatile compound released upon mechanical wounding of the leaves of Arabidopsis thaliana [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 + (3Z)-hex-3-en-ol
(3Z)-hex-3-en-1-yl acetate + CoA
show the reaction diagram
acetyl-CoA + (3Z)-hex-3-en-ol
(Z)-3-hexen-1-yl acetate + coenzyme A
show the reaction diagram
-
-
-
?
acetyl-CoA + 1-octanol
octanyl acetate + CoA
show the reaction diagram
the enzyme has the ability to accept several medium-chain-length aliphatic and benzyl-derived alcohols, but has highest catalytic efficiency with (Z)-3-hexen-1-ol. The catalytic efficiency with 1-octanol is 0.2% of the catalytic efficiency with (Z)-3-hexen-1-ol
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-
?
additional information
?
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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
acetyl-CoA + (3Z)-hex-3-en-ol
(3Z)-hex-3-en-1-yl acetate + CoA
show the reaction diagram
the major volatile released upon mechanical wounding of the leaves is (Z)-3-hexen-1-yl acetate
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-
?
acetyl-CoA + (3Z)-hex-3-en-ol
(Z)-3-hexen-1-yl acetate + coenzyme A
show the reaction diagram
-
-
-
?
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
0.126 - 0.251
(3Z)-hex-3-en-ol
0.174
1-Octanol
pH 7.7, 25°C, recombinant His6-tagged enzyme
0.0105 - 0.0385
acetyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.3
(3Z)-hex-3-en-ol
pH 7.7, 25°C, recombinant His6-tagged enzyme
0.125
1-Octanol
pH 7.7, 25°C, recombinant His6-tagged enzyme
23
acetyl-CoA
pH 7.7, 25°C, recombinant His6-tagged enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
45
(3Z)-hex-3-en-ol
pH 7.7, 25°C, recombinant His6-tagged enzyme
0.072
1-Octanol
pH 7.7, 25°C, recombinant His6-tagged enzyme
597
acetyl-CoA
pH 7.7, 25°C, recombinant His6-tagged enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 9
pH 6.3: 89% of maximal activity, pH 9.0: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
enzyme activity in the leaves following wounding increases over time, but this response lagges significantly behind (Z)-3-hexen-1-yl acetate release. A maximum specific activity is reached 12 h after the initial wounding event. CHAT enzyme activity declines by 35% over the course of the next 12 h
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
RNAi transgenic plants exhibiting a severe reduction in At3g03480 transcript levels emitt no (Z)-3-hexen-1-yl acetate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CHAT_ARATH
454
0
50290
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
native plant protein, gel filtration
50290
calculated from sequence
50400
1 * 50400, native plant protein, calculated from sequence
51000
His-tagged protein, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 50290, calculated from sequence
monomer
1 * 50400, native plant protein, calculated from sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
30 min, stable
37
30 min, 13% loss of activity
50
30 min, complete loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli, the coding region of At3g03480 is cloned into a vector that introduces an N-terminal 6His tag
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
D'Auria, J.C.; Pichersky, E.; Schaub, A.; Hansel, A.; Gershenzon, J.
Characterization of a BAHD acyltransferase responsible for producing the green leaf volatile (Z)-3-hexen-1-yl acetate in Arabidopsis thaliana
Plant J.
49
194-207
2007
Arabidopsis thaliana (Q9SRQ2), Arabidopsis thaliana
Manually annotated by BRENDA team
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
Arabidopsis thaliana (Q9SRQ2)
Manually annotated by BRENDA team