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Information on EC 3.1.2.14 - oleoyl-[acyl-carrier-protein] hydrolase and Organism(s) Ricinus communis and UniProt Accession A9XK92

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.14 oleoyl-[acyl-carrier-protein] hydrolase
IUBMB Comments
Acts on acyl-carrier-protein thioesters of fatty acids from C12 to C18, but the derivative of oleic acid is hydrolysed much more rapidly than any other compound tested.
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Ricinus communis
UNIPROT: A9XK92
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Word Map
The taxonomic range for the selected organisms is: Ricinus communis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
acyl-acp thioesterase, fatb1, acyl-acyl carrier protein (acp) thioesterase, fatb2, acyl-acyl carrier protein thioesterase, acyl-acp te, fatty acyl-acp thioesterase, oleoyl-acp thioesterase, mlfatb, lcfatb, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acyl-ACP thioesterase
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acyl-acyl carrier protein (ACP) thioesterase
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12:0-ACP thioesterase
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-
-
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12:0-acyl-carrier protein thioesterase
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-
-
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14:0-ACP thioesterase
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-
-
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14:0-acyl-carrier protein thioesterase
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-
-
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16:0-ACP thioesterase
-
-
-
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16:0-acyl-carrier protein thioesterase
-
-
-
-
18:0-ACP thioesterase
-
-
-
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18:0-acyl-carrier protein thioesterase
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-
-
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acyl-ACP-hydrolase
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-
-
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acyl-acyl carrier protein hydrolase
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-
-
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Acyl-[acyl-carrier protein] hydrolase
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-
-
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acyl-[acyl-carrier-protein] hydrolase
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-
-
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acyl–ACP thioesterase
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acyl–acyl carrier protein (ACP) thioesterase
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AH
-
-
-
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BTE
-
-
-
-
C12:0 ACP TE
-
-
-
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C18:1-ACP thioesterase
-
-
-
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Deubiquitinating enzyme 14
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-
-
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hydrolase, oleoyl-[acyl carrier protein]
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-
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oleoyl-ACP thioesterase
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-
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oleoyl-acyl carrier protein thioesterase
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-
-
-
OTE
-
-
-
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PATE
-
-
-
-
STE
-
-
-
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Ubiquitin thiolesterase 14
-
-
-
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Ubiquitin-specific processing protease 14
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
oleoyl-[acyl-carrier protein] hydrolase
Acts on acyl-carrier-protein thioesters of fatty acids from C12 to C18, but the derivative of oleic acid is hydrolysed much more rapidly than any other compound tested.
CAS REGISTRY NUMBER
COMMENTARY hide
105669-84-9
-
68009-83-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
oleoyl-[acyl-carrier protein] + H2O
oleic acid + acyl-carrier protein
show the reaction diagram
maximum catalytic efficiency of FatA
-
-
?
palmitoleoyl-[acyl-carrier protein] + H2O
palmitoleate + acyl-carrier protein
show the reaction diagram
high catalytic efficiency of FatA
-
-
?
palmitoyl-[acyl-carrier protein] + H2O
palmitate + acyl-carrier protein
show the reaction diagram
-
-
-
?
stearoyl-[acyl-carrier protein] + H2O
stearate + acyl-carrier protein
show the reaction diagram
-
-
-
?
oleoyl-[acyl-carrier protein] + H2O
oleic acid + acyl-carrier protein
show the reaction diagram
high efficiency of FatB
-
-
?
palmitoleoyl-[acyl-carrier protein] + H2O
palmitoleate + acyl-carrier protein
show the reaction diagram
high efficiency of FatB
-
-
?
palmitoyl-[acyl-carrier protein] + H2O
palmitate + acyl-carrier protein
show the reaction diagram
-
-
-
?
stearoyl-[acyl-carrier protein] + H2O
stearate + acyl-carrier protein
show the reaction diagram
-
-
-
?
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00042
oleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.00035
palmitoleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.00056
palmitoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.00054
stearoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.00067
oleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.00086
palmitoleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.00054
palmitoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.00088
stearoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.99
oleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
1.62
palmitoleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.46
palmitoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.56
stearoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.67
oleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.22
palmitoleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.41
palmitoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
0.38
stearoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19030
oleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
4630
palmitoleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
830
palmitoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
1030
stearoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
990
oleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
250
palmitoleoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
760
palmitoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
440
stearoyl-[acyl-carrier protein]
in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
calculated from sequence
7
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A9XK92_RICCO
371
0
42208
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37520
recombinant histidine-tagged FatA, gel filtration
42200
FatA open reading frames, calculated from sequence
36800
recombinant histidine-tagged FatB, gel filtration
46500
FatB open reading frames, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 42200, FatA open reading frames, calculated from sequence
?
x * 46500, FatA open reading frames, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity in a single step by gel filtration
to homogeneity in a single step by gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
PCR fragments cloned into the pMBL-T vector, subcloned into the BamHI-HindIII or SacI-KpnI sites of the pQE-80L vector. Resulting construct pQERcFatA overexpressed in Escherichia coli XL1-Blue
PCR fragments cloned into the pMBL-T vector, subcloned into the BamHI-HindIII or SacI-KpnI sites of the pQE-80L vector. Resulting construct pQERcFatB overexpressed in Escherichia coli XL1-Blue
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcript accumulation profile is temporally regulated during embryo development. Displays maximum level of transcription in the period of maximum oil accumulation
transcript accumulation profile is temporally regulated during embryo development. Displays maximum level of transcription in the period of maximum oil accumulation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
contribution of FatA to the synthesis of castor oil
industry
contribution of FatB to the synthesis of castor oil
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sanchez-Garcia, A.; Moreno-Perez, A.J.; Muro-Pastor, A.M.; Salas, J.J.; Garces, R.; Martinez-Force, E.
Acyl-ACP thioesterases from castor (Ricinus communis L.): An enzymatic system appropriate for high rates of oil synthesis and accumulation
Phytochemistry
71
860-869
2010
Ricinus communis (A9XK92), Ricinus communis (A9XUG5)
Manually annotated by BRENDA team