Information on EC 2.3.1.133 - shikimate O-hydroxycinnamoyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.133
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RECOMMENDED NAME
GeneOntology No.
shikimate O-hydroxycinnamoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-coumaroyl-CoA + shikimate = CoA + 4-coumaroylshikimate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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chlorogenic acid biosynthesis I
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chlorogenic acid biosynthesis II
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Flavonoid biosynthesis
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Metabolic pathways
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phaselate biosynthesis
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phenylpropanoid biosynthesis
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Phenylpropanoid biosynthesis
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Stilbenoid, diarylheptanoid and gingerol biosynthesis
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phenylpropanoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
4-coumaroyl-CoA:shikimate O-(hydroxycinnamoyl)transferase
Caffeoyl-CoA, feruloyl-CoA and sinapoyl-CoA can also act as donors, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
73904-44-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
D.F.L. von Schlechtendal
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
SW and EMX-1
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Manually annotated by BRENDA team
gene OsHCT4
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
young green dates
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
; genes PeHCT-1, PeHCT-2, PeHCT-3, PeHCT-4, PeHCT-5, PeHCT-6, and PeHCT-7
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
rye, var. Kustro
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Manually annotated by BRENDA team
gene cbhct2
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
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hydroxycinnamoyltransferases HCT1806 and HCT4918 physically interact with and suppress the hypersensitive response conferred by Leu-rich repeat protein Rp1-D21 when transiently coexpressed in Nicotiana benthamiana. Other maize hydroxycinnamoyltransferase homologs are unable to confer the same level of suppression on Rp1-D21-induced hypersensitive response. The metabolic activity of HCT1806 and HCT4918 is unlikely to be necessary for their role in suppressing hypersensitive response. HCT1806 and HCT4918 play roles in Rp1-mediated disease resistance
additional information
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PeHCT contains a conserved HXXXDG motif that is found in acyltransferase
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + 2,3-dihydroxybenzoate
CoA + 3-O-(4-coumaroyl)-2-hydroxybenzoate
show the reaction diagram
4-coumaroyl-CoA + 2,3-dihydroxybenzoate
CoA + ?
show the reaction diagram
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-
-
?
4-coumaroyl-CoA + 3,4-dihydroxybenzoate
CoA + 3-O-(4-coumaroyl)benzoate
show the reaction diagram
4-coumaroyl-CoA + 3-aminobenzoate
CoA + 3-N-(4-coumaroyl)-benzoate
show the reaction diagram
4-coumaroyl-CoA + 3-aminobenzoate
CoA + ?
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + 3-hydroxyanthranilate
CoA + 3-(4-coumaroyl)oxyanthranilate
show the reaction diagram
4-coumaroyl-CoA + 3-hydroxybenzoate
CoA + 3-(4-coumaroyl)oxybenzoate
show the reaction diagram
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-
-
?
4-coumaroyl-CoA + 3-hydroxybenzoate
CoA + 3-O-(4-coumaroyl)benzoate
show the reaction diagram
4-coumaroyl-CoA + 5-hydroxyanthranilate
CoA + 5-(4-coumaroyl)oxyanthranilate
show the reaction diagram
4-coumaroyl-CoA + catechol
CoA + 1-(4-coumaroyl)catechol
show the reaction diagram
low affinity substrate
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-
?
4-coumaroyl-CoA + catechol
CoA + 1-O-(4-coumaroyl)catechol
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + gentisate
CoA + 5-O-(4-coumaroyl)gentisate
show the reaction diagram
4-coumaroyl-CoA + glycerol
CoA + 2-O-(4-coumaroyl)glycerol + 1-O-(4-coumaroyl)glycerol
show the reaction diagram
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-
-
-
?
4-coumaroyl-CoA + hydroquinone
CoA + 1-(4-coumaroyl)hydroquinone
show the reaction diagram
low affinity substrate
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-
?
4-coumaroyl-CoA + hydroquinone
CoA + 1-O-(4-coumaroyl)hydroquinone
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + L-malate
CoA + 2-O-(4-coumaryl)-L-malate
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + quinate
CoA + 4-coumaroylquinate
show the reaction diagram
4-coumaroyl-CoA + quinate
CoA + 5-(4-coumaroyl)quinate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
show the reaction diagram
low activity towards quinate
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-
?
4-coumaroyl-CoA + shikimate
CoA + 4-coumaroylshikimate
show the reaction diagram
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
caffeoyl-CoA + 2,3-dihydroxybenzoate
CoA + ?
show the reaction diagram
-
-
-
?
caffeoyl-CoA + 3-aminobenzoate
CoA + ?
show the reaction diagram
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-
-
?
caffeoyl-CoA + 3-hydroxyanthranilate
CoA + 3-caffeoyloxyanthranilate
show the reaction diagram
-
-
-
?
caffeoyl-CoA + 3-hydroxybenzoate
CoA + 3-caffeoyloxybenzoate
show the reaction diagram
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-
-
?
caffeoyl-CoA + glycerol
CoA + ?
show the reaction diagram
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-
-
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?
caffeoyl-CoA + L-malate
CoA + 2-O-caffeoyl-L-malate
show the reaction diagram
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?
caffeoyl-CoA + quinate
CoA + 5-caffeoylquinate
show the reaction diagram
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-
r
caffeoyl-CoA + quinate
CoA + caffeoylquinate
show the reaction diagram
caffeoyl-CoA + shikimate
CoA + 5-caffeoylshikimate
show the reaction diagram
-
-
-
r
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
cinnamoyl-CoA + 2,3-dihydroxybenzoate
CoA + ?
show the reaction diagram
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-
-
?
cinnamoyl-CoA + 3-aminobenzoate
CoA + ?
show the reaction diagram
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?
cinnamoyl-CoA + 3-hydroxyanthranilate
CoA + 3-cinnamoyloxyanthranilate
show the reaction diagram
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?
cinnamoyl-CoA + 3-hydroxybenzoate
CoA + 3-cinnamoyloxybenzoate
show the reaction diagram
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?
cinnamoyl-CoA + shikimate
CoA + 5-O-cinnamoylshikimate
show the reaction diagram
feruloyl-CoA + 2,3-dihydroxybenzoate
CoA + ?
show the reaction diagram
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-
?
feruloyl-CoA + 3-aminobenzoate
CoA + ?
show the reaction diagram
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?
feruloyl-CoA + 3-hydroxyanthranilate
CoA + 3-feruloyloxyanthranilate
show the reaction diagram
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?
feruloyl-CoA + 3-hydroxybenzoate
CoA + 3-feruloyloxybenzoate
show the reaction diagram
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?
feruloyl-CoA + glycerol
CoA + ?
show the reaction diagram
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?
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
sinapoyl-CoA + 3-hydroxyanthranilate
CoA + 3-sinapoyloxyanthranilate
show the reaction diagram
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r
sinapoyl-CoA + shikimate
CoA + 5-O-sinapoylshikimate
show the reaction diagram
additional information
?
-
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
4-coumaroyl-CoA + quinate
CoA + 5-(4-coumaroyl)quinate
show the reaction diagram
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-
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?
4-coumaroyl-CoA + shikimate
CoA + 4-coumaroylshikimate
show the reaction diagram
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recombinant HCT shows substrate-specificity towards shikimic acid in contrast to hydroxycinnamoyl-CoA quinate transferase, HQT, EC 2.3.1.99
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?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
caffeoyl-CoA + quinate
CoA + 5-caffeoylquinate
show the reaction diagram
A4ZKE4
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r
caffeoyl-CoA + shikimate
CoA + 5-caffeoylshikimate
show the reaction diagram
A4ZKE4
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r
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Dihydroxybenzoate
0.8 mM, about 50% inhibition
3-aminobenzoate
0.8 mM, about 45% inhibition
3-Hydroxyanthranilate
0.8 mM, about 45% inhibition
4,4(-diisothiocyano-2,2)-stilbene disulfonic acid
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Diethylpyrocarbonate
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80% reversion after treatment with hydroxylamine
p-chloromercuribenzenesulfonic acid
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protocatechuate
0.8 mM, about 40% inhibition
RNAi
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HCT silencing is achieved by transformation of Pinus radiata callus cells with pHF5
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Sodium diphosphate
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tricine
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weak, not Tris/HCl
additional information
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no effect: 2,3-butanedione, phenylmethylsulfonylfluoride and N-methylmaleimide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Tris/HCl
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activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.188 - 0.699
2,3-Dihydroxybenzoate
1.48
3,4-dihydroxybenzoate
pH 7.5, 30°C
2.404
3-aminobenzoate
pH 7.0, 30°C, with 4-coumaroyl-CoA
0.449 - 0.83
3-Hydroxyanthranilate
0.733 - 1.677
3-hydroxybenzoate
1.1
3-phenylacryloyl-CoA
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0.0015 - 14.3
4-Coumaroyl-CoA
0.119
4-coumaroylshikimate
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0.0051 - 30.5
caffeoyl-CoA
0.0265
cinnamoyl-CoA
pH 7.0, 30°C, with shikimate
0.162
CoA
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0.0051 - 55.5
Feruloyl-CoA
0.0859
glycerol
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pH 7.5, 37°C, with feruloyl-CoA
0.00582 - 5.82
quinate
0.0009 - 83
shikimate
0.02
Sinapoyl-CoA
pH 7.0, 30°C, with shikimate
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0056
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additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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50 mM potassium phosphate buffer
7.1
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200 mM potassium phosphate buffer
additional information
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pI: 4.63
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
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about half-maximal activity at pH 5.5 and 7.5
6.1 - 6.7
optimal pH range with malate as the acceptor, highest reaction rates are observed for both hydroxycinnamoyl-CoA derivatives between pH 6.1 and 6.7 using sodium phosphate buffer
6.2 - 8.5
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about half-maximal activity at pH 6.2 in potassium phosphate buffer and 8.5 in Tris-HCl puffer
6.3 - 7.7
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about 80% of maximal activity at pH 6.3 and 7.7
7.5 - 7.9
optimal pH range with shikimic acid as the acceptor, highest reaction rates are observed for both hydroxycinnamoyl-CoA derivatives between pH 7.5 and 7.9 using sodium phosphate buffer; optimal pH range with shikimic acid as the acceptor, highest reaction rates are observed for both hydroxycinnamoyl-CoA derivatives between pH 7.5 and 7.9 using sodium phosphate buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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above 40°C rapid and irreversible loss of activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.78
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000 - 50000
recombinant HCT, gel filtration
47100
x * 47100, about, sequence calculation
48300
calculated from cDNA; calculated from cDNA; calculated from cDNA
48464
1 * 48000, recombinant enzyme, SDS-PAGE, 1 * 48464, mass spectrometry
49000
static light scattering
58000
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gel filtration
70000
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x * 70000, about, recombinant GST-tagged HCT, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant HCT, sitting drop technique, mixing of 100 nl of 20 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM 2-mercaptoethanol, with 100 nl of precipitant solution containing 1.6 M magnesium sulfate, 0.1 M MES pH 6.5, 20°C, 2 months, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement
in complex with CoA and 4-coumaroyl-shikimate. The 4-coumaroyl-shikimate contacts the enzyme via the phenolic group and carbonyl group of the 4-coumaroyl portion. The shikimate portion contacts the enzyme through both the carboxyl and hydroxyl groups. In the protocatechuate ternary complex, protocatechuate binds in a very similar manner to shikimate, with the carboxyl group making a tight salt bridge with Arg369, and the C3 hydroxyl group interacting with the nitrogen NE2 of His163
structures in its apo-form and ternary complex with shikimate and 4-coumaroyl-CoA, which is converted to its product during crystal soaking. Residues threonine36, serine38, tyrosine40, histidine162, arginine371, and threonine384 are involved in catalysis and specificity. Histidine162 and threonine36 play a role in the catalytic mechanism. Substrate binding should occur sequentially, with 4-coumaroyl-CoA binding prior to the acyl acceptor molecule. Comparison of the structure of sorghum HCT with the HCT involved in chlorogenic acid synthesis in Coffea canephora
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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denaturation after 5 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol stabilizes during storage
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.1 M phosphate buffer, pH 6.5, 65% of initial activity retained for at least 85 days
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-20°C, at least 6 months
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-20°C, for several months with 10-20% loss of apparent activities after thawing
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-20°C, for several months, no apparent loss of activity
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-20°C, with 10% glycerol at least 30 days
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-80°C, for several months with 10-20% loss of apparent activities after thawing
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incubation for days at room temperature, multiple freeze/thaw cycles, holding at -20°C for several months, with or without the addition of 10% glycerol, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crude extracts from stem material from various down-regulated and control lines are assayed for extractable HCT enzyme activity
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partial
recombinant enzyme
recombinant GST-tagged HCT from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography; recombinant GST-tagged PeHCT-1, PeHCT-2, PeHCT-3, PeHCT-4, PeHCT-5, PeHCT-6, and PeHCT-7 gene products from Escherichia coli strain BL21 (DE3) by glutathione affinity cromatography
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recombinant His-tagged HST from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis
recombinant N-terminally His6-tagged HCT from Escherichia coli strain BL21 Star(DE3)pLysS by nickel affinity chromatography, dialysis, and cleavage of the tag by TEV protease, followed by gel filtration
soluble recombinant GST-tagged OsHCT4 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
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tracheary elements are cultured
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an antisense construct is generated for down-regulation of HCT
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expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli
expression in Escherichia coli
expression of GST-tagged HCT in Escherichia coli strain BL21 (DE3); genes PeHCT-1, PeHCT-2, PeHCT-3, PeHCT-4, PeHCT-5, PeHCT-6, and PeHCT-7, expression as GST-tagged enzymes in Escherichia coli strain BL21 (DE3)
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gene cbhct2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged HST in Escherichia coli strain BL21(DE3)pLysS
gene OsHCT4, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression as soluble GST-tagged enzyme using vector pGEX 5X-1 in Escherichia coli strain BL21(DE3)
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overexpression of N-terminally His6-tagged HCT in Escherichia coli strain BL21 Star(DE3)pLysS using a commercially available synthetic gene encoding HCT with codons optimized for Escherichia coli expression
recombinantly expressed in Escherichia coli
the amplified PCR fragments of the putative HCT cDNA clone are sequenced and cloned into a derivative of pAHC25, the resulting plasmid containing the HCT RNAi construct is named pHF5
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H162A
complete loss of activity
R371A
complete loss of activity
S38A
40% of wild-type activity
T36A
6% of wild-type activity
T384A
9% of wild-type activity
Y40A
62% of wild-type activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
industry
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the global trend toward a biomaterials-based economy makes plant cell walls increasingly important as renewable resources, HCT is a metabolic entry point leading to the biosynthesis of G-lignin in coniferous gymnosperms
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