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Information on EC 2.3.1.167 - 10-deacetylbaccatin III 10-O-acetyltransferase
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EC Tree
2.3.1.167 10-deacetylbaccatin III 10-O-acetyltransferaseIUBMB Comments
The enzyme will not acylate the hydroxy group at 1beta, 7beta or 13alpha of 10-deacetyl baccatin III, or at 5alpha of taxa-4(20),11-dien-5alpha-ol. May be identical to EC 2.3.1.163, 10-hydroxytaxane O-acetyltransferase.
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Word Map
- 2.3.1.167
- taxus
-
taxoids
-
endophytic
-
needle
- baccata
- yunnanensis
- synthesis
-
taxol-producing
- chinensis
-
cephalomannine
- cuspidata
- taxadiene
-
diterpenoids
- 10-deacetyltaxol
- mairei
- wallichiana
-
oxetane
-
twigs
- pharmacology
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
10-dab, 10-deacetylbaccatin iii-10-o-acetyl transferase, tmdbat, 10-deacetylbaccatin iii-10-o-acetyltransferase, 10-dabt, 10-deacetylbaccatin iii-10beta-o-acetyltransferase, 10-dbat, 10-deacetylbaccatin iii:10beta-o-acetyltransferase, taxoid 10beta-o-acetyltransferase, 10-deacetylbaccatin iii 10beta-o-acetyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
10-DAB
10-DBAT
10-deacetylbaccatin III 10-O-acetyltransferase
10-deacetylbaccatin III 10beta-O-acetyltransferase
10-deacetylbaccatin III-10-beta-O-acetyltransferase
10-deacetylbaccatin III-10-O-acetyl transferase
10-deacetylbaccatin III-10-O-acetyltransferase
10-deacetylbaccatin III-10beta-O-acetyltransferase
10-hydroxytaxane 10-O-acetyltransferase
-
-
-
-
10-hydroxytaxane O-acetyltransferase
-
-
-
-
acetyl CoA:10-deacetylbaccatin-III 10-O-acetyltransferase
-
-
-
-
acetyl coenzyme A:10-hydroxytaxane O-acetyltransferase
-
-
-
-
DBAT
10-deacetylbaccatin III 10beta-O-acetyltransferase
-
10-deacetylbaccatin III-10beta-O-acetyltransferase
-
-
-
-
DBAT
gene encoding for 10-deacetylbaccatin-III-10beta-O-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + 10-deacetylbaccatin III = CoA + baccatin III
The enzyme will not acylate the hydroxy group at 1beta, 7beta or 13alpha of 10-deacetyl baccatin III, or at 5alpha of taxa-4(20),11-dien-5alpha-ol. May be identical to EC 2.3.1.163, 10-hydroxytaxane O-acetyltransferase
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
Acyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:taxan-10beta-ol O-acetyltransferase
The enzyme will not acylate the hydroxy group at 1beta, 7beta or 13alpha of 10-deacetyl baccatin III, or at 5alpha of taxa-4(20),11-dien-5alpha-ol. May be identical to EC 2.3.1.163, 10-hydroxytaxane O-acetyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
220946-63-4
-
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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 + 7,13-diacetyl-4-deacetylbaccatin III
CoA + 13-acetylbaccatin III
-
-
-
-
?
butyryl-CoA + 10-deacetylbaccatin III
CoA + 10-deacetyl-10-butyrylbaccatin III
Taxus sp.
-
-
-
-
?
N-acetyl-D-glucosamine + 10-deacetylbaccatin III
D-glucosamine + baccatin III
the yield when using N-acetyl-D-glucosamine as acetyl donor in open-whole-cell catalytic system is 2.13fold of that when using acetyl-CoA. In the in vivo system, the yield increased 24.17%, which may indicate its cooperation with acetyl-CoA
-
-
?
n-butyryl-CoA + 10-deacetylbaccatin III
CoA + 10-deacetyl-10-butyrylbaccatin III
Taxus sp.
-
-
-
-
?
n-butyryl-CoA + 10-deacetylbaccatin III
CoA + 10-n-butyryl-10-deacetylbaccatin III
Taxus sp.
-
-
-
-
?
propionyl-CoA + 10-deacetylbaccatin III
CoA + 10-deacetyl-10-propionylbaccatin III
Taxus sp.
-
-
-
-
?
propionyl-CoA + 10-deacetylbaccatin III
CoA + 10-propionyl-10-deacetylbaccatin III
Taxus sp.
-
-
-
-
?
additional information
?
-
Taxus sp.
-
DBAT catalyzes the transfer of acetyl, propionyl or n-butyryl from CoA to the C10-hydroxyl of 10-deacetylbaccatin III
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
catalyzes the acetylation of the C10 hydroxyl group of the advanced metabolite 10-deacetylbaccatin III to yield baccatin III, which is the immediate diterpenoid precursor of taxol
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
catalyzes the acetylation of the C10 hydroxyl group of the advanced metabolite 10-deacetylbaccatin III to yield baccatin III, which is the immediate diterpenoid precursor of taxol
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
the enzyme is involved in taxol biosynthesis
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
-
?
vinyl acetate + 10-deacetylbaccatin III
vinyl alcohol + baccatin III
-
-
-
?
vinyl acetate + 10-deacetylbaccatin III
vinyl alcohol + baccatin III
42% of the activity as compared to N-acetyl-D-glucosamine
-
-
?
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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
butyryl-CoA + 10-deacetylbaccatin III
CoA + 10-deacetyl-10-butyrylbaccatin III
Taxus sp.
-
-
-
-
?
propionyl-CoA + 10-deacetylbaccatin III
CoA + 10-deacetyl-10-propionylbaccatin III
Taxus sp.
-
-
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
the enzyme is involved in taxol biosynthesis
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Bioprospecting endophytic fungi from Fusarium genus as sources of bioactive metabolites.
Breast Neoplasms
Bioprospecting endophytic fungi from Fusarium genus as sources of bioactive metabolites.
Hepatitis C
Bioprospecting endophytic fungi from Fusarium genus as sources of bioactive metabolites.
Neoplasms
Bioprospecting endophytic fungi from Fusarium genus as sources of bioactive metabolites.
Tuberculosis
Bioprospecting endophytic fungi from Fusarium genus as sources of bioactive metabolites.
Uterine Cervical Neoplasms
Bioprospecting endophytic fungi from Fusarium genus as sources of bioactive metabolites.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
10-deacetylbaccatin III
-
recombinant enzyme with a hexahistidine fusion tag
0.049
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
0.075
10-deacetylbaccatin III
wild-type enzyme, 30°C, pH not specified in the publication
0.134
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
0.231
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
1.67
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
2.28
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
3.21
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
0.073
acetyl-CoA
wild-type enzyme, 30°C, pH not specified in the publication
0.148
acetyl-CoA
mutant enzyme, 30°C, pH not specified in the publication
0.762
acetyl-CoA
mutant enzyme, 30°C, pH not specified in the publication
0.925
acetyl-CoA
mutant enzyme, 30°C, pH not specified in the publication
1.094
acetyl-CoA
mutant enzyme, 30°C, pH not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.59
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
14.69
10-deacetylbaccatin III
wild-type enzyme, 30°C, pH not specified in the publication
21.74
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
27.03
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
27.61
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
33.12
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
12.73
acetyl-CoA
mutant enzyme, 30°C, pH not specified in the publication
16.12
acetyl-CoA
wild-type enzyme, 30°C, pH not specified in the publication
18.79
acetyl-CoA
mutant enzyme, 30°C, pH not specified in the publication
20.54
acetyl-CoA
mutant enzyme, 30°C, pH not specified in the publication
26.65
acetyl-CoA
mutant enzyme, 30°C, pH not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
20
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
30
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
70
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
120
10-deacetylbaccatin III
mutant enzyme, 30°C, pH not specified in the publication
200
10-deacetylbaccatin III
wild-type enzyme, 30°C, pH not specified in the publication
220
acetyl-CoA
wild-type enzyme, 30°C, pH not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
endophytic taxol-producing fungus strain MD3 isolated from the inner bark of Taxus x media
TREMBL
brenda
endophytic taxol-producing fungus strain MD2 isolated from the inner bark of Taxus media
TREMBL
brenda
Taxus sp.
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
higher content of 10-deacetylbaccatin III in the aerial part of the plantlets than in the roots
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
10-deacetylbaccatin III-10-O-acetyl transferase functions in the last step of Taxol core synthesis is the most important enzyme of the pathway
metabolism
-
the relationship between taxane patterns and the expression of genes encoding the enzymes taxadiene synthase, 10-deacetylbaccatin III-10beta-O-acetyltransferase, baccatin III 13-O-(3-amino-3-phenylpropanoyl) transferase and 3'-N-debenzoyl-2'-deoxytaxol-N-benzoyltransferase, involved in early and late steps of the taxane pathway, overview. The most abundant taxane in the aerial parts is 10-deacetylbaccatin III, which increases as the plantlets grow, indicating a low conversion to baccatin III and taxol. In contrast, the levels of 10-deacetylbaccatin III in the roots remain lower than those of taxol. But in the aerial parts the expression of DBAT, which codes for the enzyme that converts 10-deacetylbaccatin III into baccatin III, does not increase with the age of plantlets, unlike that of the other three enzymes, suggesting that this gene controls a rate-limiting step in the taxane biosynthetic pathway
metabolism
key enzyme to produce baccatin III, a key precursor in paclitaxel synthesis
metabolism
-
10-deacetylbaccatin III-10-O-acetyl transferase functions in the last step of Taxol core synthesis is the most important enzyme of the pathway
-
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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). DBAT_TAXCU
440
0
49053
Swiss-Prot
Chloroplast (Reliability: 5)
B9RN49_RICCO
421
0
46679
TrEMBL
Chloroplast (Reliability: 5)
D5K1Q6_FUSSL
207
0
23461
TrEMBL
other Location (Reliability: 1)
B9S966_RICCO
446
0
50013
TrEMBL
other Location (Reliability: 3)
A0A396IQ50_MEDTR
126
0
14323
TrEMBL
other Location (Reliability: 4)
B9SDF1_RICCO
244
0
27722
TrEMBL
other Location (Reliability: 4)
B9SDF2_RICCO
265
0
29481
TrEMBL
other Location (Reliability: 3)
A0A396IUY9_MEDTR
240
0
26648
TrEMBL
other Location (Reliability: 1)
A0A396H8N0_MEDTR
271
0
30264
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
65000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F301A
activity against 10-deacetyltaxol is 1.6times more active than wild-type activity, activitys against 10-deacetylbaccatin III is degraded
F301V
mutant enzyme is 2.85times more active against 10-deacetyltaxol than the wild-type enzyme
G38A
activity against 10-deacetyltaxol is 1.45times more active than wild-type activity, activitys against 10-deacetylbaccatin III is slightly decreased
G38R
mutant enzyme is 2.19times more active against 10-deacetyltaxol than the wild-type enzyme
G38R/F301V
mutant enzyme is 3.7times more active against 10-deacetyltaxol than the wild-type enzyme, activity against 10-deacetylbaccatin III is 69% as compared to wild-type enzyme
D390H
catalytic efficiency towards 10-deacetylbaccatin III and vinyl acetate is 96% of the wild-type value
D390R
catalytic efficiency towards 10-deacetylbaccatin III and vinyl acetate is improved by 2.3fold
H162A
mutation results in complete loss of enzymatic activity, suggesting that the residue histidine at 162 is essential to DBAT activity
I43S
catalytic efficiency towards 10-deacetylbaccatin III and vinyl acetate is improved by 2.1fold
I43S/D390R
catalytic efficiency towards 10-deacetylbaccatin III and vinyl acetate is improved by 3.3fold, compared to that of wild-type enzyme. Catalytic efficiency is 2.99fold higher than the catalytic efficiency of wild-type enzyme towards 10-deacetylbaccatin III and acetyl-CoA
I43T
catalytic efficiency towards 10-deacetylbaccatin III and vinyl acetate is improved by 2.1fold
additional information
-
functional expression in Saccharomyces cerevisiae for reconstruction of taxoid biosynthesis
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the recombinant DBAT is immobilized by cross-linked enzyme aggregates. To further optimize the enzyme recovery, single-factor experiment and response surface methodology is applied. 60% ammonium sulfate as precipitant, 0.05% glutaraldehyde as fixing agent, pH 7.0, 2 h as cross-linking time, 30°C as cross-linking temperature are confirmed to be the optimum conditions. 62% for ammonium sulfate saturation, 0.15% for glutaraldehyde, and pH 6.75 are the optimum conditions with averagely 73.9% activity recovery in 3 replications
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography in Ni-nitrilotriacetic acid columns, the tag is removed by digestion with enterokinase
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene dbat, functional expression in Escherichia coli strain JM109, co-expression with acetyl-CoA synthase, gene acs, EC 6.2.1.1, or with acetoacetate:acetyl-CoA CoA-transferase, genes atoAD of the ato operon, EC 2.8.3.8, expressed from and regulated by genes encoded on the bacterial chromosome, overview
Taxus sp.
-
into the TA cloning vector pMD19-T for sequencing
into the vector pCWori+ for expression in Escherichia coli JM109 and BL21DE3 cells
Taxus sp.
-
overexpression in Escherichia coli. Three kinds of fusion systems with isopropyl-beta-D-1-thiogalactopyranoside inducible promoters are used. The fusion partners are glutathione S-transferase tag, hexahistidine fusion tag, and a biotinylated peptide tag
-
the amplified PCR fragment is subcloned into the pGEM-T Easy vector and subsequently into the pET32a+ vector for expression in Escherichia coli BL21DE3 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
10-DBAT is induced by F3, and elicitor isolated from the inner bark of Taxus cuspidata, it is also induced by methyljasmonate, salicylate, and hydrogen peroxide to maximal activities of 6.82, 5.47, 0.97, and 3.30 U, respectively. The metabolite pattern in the suspension cell culture changed due to elicitation, accumulation of baccatin III and 10-DAB III increases slowly, taxol accumulated rapidly, time course of enzyme activity of 10-DBAT, verview
highest level of dbat expression was detected 24 h after inoculation followed by a decrease
10-DBAT is induced by F3, and elicitor isolated from the inner bark of Taxus cuspidata, it is also induced by methyljasmonate, salicylate, and hydrogen peroxide to maximal activities of 6.82, 5.47, 0.97, and 3.30 U, respectively. The metabolite pattern in the suspension cell culture changed due to elicitation, accumulation of baccatin III and 10-DAB III increases slowly, taxol accumulated rapidly, time course of enzyme activity of 10-DBAT, verview
-
10-DBAT is induced by F3, and elicitor isolated from the inner bark of Taxus cuspidata, it is also induced by methyljasmonate, salicylate, and hydrogen peroxide to maximal activities of 6.82, 5.47, 0.97, and 3.30 U, respectively. The metabolite pattern in the suspension cell culture changed due to elicitation, accumulation of baccatin III and 10-DAB III increases slowly, taxol accumulated rapidly, time course of enzyme activity of 10-DBAT, verview
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
Taxus sp.
-
optimizing the semi-biosynthetic method in bacteria potentially provides a practical means of developing commercial-scale production of baccatin III analogs, which serve as key intermediates in the semi-synthesis of second-generation taxols
pharmacology
synthesis
pharmacology
key enzyme in the biosynthesis of the anticancer drug paclitaxel, which catalyses the formation of baccatin III from 10-deacetylbaccatin III
pharmacology
paclitaxel is a type of broad-spectrum anticancer drug in short supply. The price of acetyl-CoA, which is the acetyl group donor for the enzymatic synthesis of the intermediate, baccatin III, is the bottleneck of the mass production of paclitaxel. The study reports that N-acetyl-D-glucosamineas an acetyl group donor can substantially reduce the cost of production
synthesis
Taxus sp.
-
bioengineered Escherichia coli cells synthesize nonnatural 10-deacetyl-10-acylbaccatin III derivatives as potential precursors of second-generation Taxol derivatives using the enzyme in concert with acyl-CoA transferases, determination of optimal alkanoic acid concentration for in vivo production of baccatin III analogues, overview
synthesis
Taxus sp.
-
synthesis of baccatin III in Escherichia coli producing endogenous acetyl-CoA and overexpressing recombinant 10-deacetylbaccatin III 10-O-acetyltransferase. Use of enzyme to couple unnatural acyl-CoA analogues various amino and/or hydroxyl acceptors
synthesis
-
transgenic Flammulina velutipes expressing the DBAT gene is able to produce baccatin III, an advanced precursor of paclitaxel
synthesis
key enzyme in the biosynthesis of the anticancer drug paclitaxel, which catalyses the formation of baccatin III from 10-deacetylbaccatin III
synthesis
mutant enzyme G38R/F301V with a catalytic efficiency approximately six times higher than that of the wild-type is combined with a beta-xylosidase to obtain an in vitro one-pot conversion of 7-beta-xylosyl-10-deacetyltaxol to Taxol yielding 0.64 mg/mlx02taxol in 50 ml at 15 h. This approach represents a promising environmentally friendly alternative for Taxol production from an abundant analogue
synthesis
paclitaxel is a type of broad-spectrum anticancer drug in short supply. The price of acetyl-CoA, which is the acetyl group donor for the enzymatic synthesis of the intermediate, baccatin III, is the bottleneck of the mass production of paclitaxel. The study reports that N-acetyl-D-glucosamineas an acetyl group donor can substantially reduce the cost of production
synthesis
-
transgenic Flammulina velutipes expressing the DBAT gene is able to produce baccatin III, an advanced precursor of paclitaxel
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walker, K.; Croteau, R.
Taxol biosynthetic genes
Phytochemistry
58
1-7
2001
Taxus cuspidata (Q9M6E2)
brenda
Walker.K.; Croteau, R.
Molecular cloning of a 10-deacetylbaccatin III-10-O-acetyl transferase cDNA from Taxus and functional expression in Escherichia coli
Proc. Natl. Acad. Sci. USA
97
583-587
2000
Taxus cuspidata (Q9M6E2), Taxus cuspidata
brenda
Pennington, J.J.; Fett-Neto, A.G.; Nicholson, S.A.; Kingston, D.G.I.; Dicosmo, F.
Acetyl CoA: 10-deacetylbaccatin-III-10-O-acetyltransferase activity in leaves and cell suspension cultures of Taxus cuspidata
Phytochemistry
49
2261-2266
1998
Taxus cuspidata (Q9M6E2)
-
brenda
Fang, J.; Ewald, D.
Expression cloned cDNA for 10-deacetylbaccatin III-10-O-acetyltransferase in Escherichia coli: a comparative study of three fusion systems
Protein Expr. Purif.
35
17-24
2004
Taxus baccata
brenda
DeJong, J.H.; Liu, Y.; Bollon, A.P.; Long, R.M.; Jennewein, S.; Williams, D.; Croteau, R.B.
Genetic engineering of taxol biosynthetic genes in Saccharomyces cerevisiae
Biotechnol. Bioeng.
93
212-224
2006
Taxus brevifolia
brenda
Loncaric, C.; Ward, A.F.; Walker, K.D.
Expression of an acetyl-CoA synthase and a CoA-transferase in Escherichia coli to produce modified taxanes in vivo
Biotechnol. J.
2
266-274
2007
Taxus sp.
brenda
Loncaric, C.; Merriweather, E.; Walker, K.D.
Profiling a taxol pathway 10beta-acetyltransferase: Assessment of the specificity and the production of baccatin III by in vivo acetylation in E. coli
Chem. Biol.
13
309-317
2006
Taxus sp.
brenda
Hao, d.a..C.; Huang, B.; Yang, L.
Phylogenetic relationships of the genus Taxus inferred from chloroplast intergenic spacer and nuclear coding DNA
Biol. Pharm. Bull.
31
260-265
2008
Taxus baccata, Taxus brevifolia, Taxus canadensis, Taxus wallichiana var. wallichiana, Taxus chinensis, Taxus mairei, Taxus fuana, Taxus sumatrana, Taxus globosa, Taxus wallichiana, Taxus floridana
brenda
Hao, D.C.; Huang, B.; Yang, L.
Molecular evolution of paclitaxel biosynthetic genes TS and DBAT of Taxus species
Genetica
135
123-135
2008
Taxus x media (A0MPB1), Taxus x hunnewelliana (B5KRF3), Taxus canadensis (B5KRF5), Taxus chinensis (B5KRF6), Taxus chinensis (B5KRG3), Taxus wallichiana var. wallichiana (B5KRF7), Taxus fuana (B5KRF8), Taxus mairei (B5KRG1), Taxus mairei (Q67DV6), Taxus baccata (B5KRG2), Taxus baccata (Q8W169), Taxus brevifolia (B5KRG4), Taxus sumatrana (B5KRG5), Taxus globosa (B5KRG6), Taxus cuspidata (Q9M6E2)
brenda
Guo, B.; Kai, G.; Gong, Y.; Jin, H.; Wang, Y.; Miao, Z.; Sun, X.; Tang, K.
Molecular cloning and heterologous expression of a 10-deacetylbaccatin III-10-O-acetyl transferase cDNA from Taxus x media
Mol. Biol. Rep.
34
89-95
2007
Taxus x media (Q6SQJ5), Taxus x media
brenda
Zhang, P.; Zhou, P.P.; Yu, L.J.
An endophytic taxol-producing fungus from Taxus media, Cladosporium cladosporioides MD2
Curr. Microbiol.
59
227-232
2009
Cladosporium cladosporioides (B1PBV3), Cladosporium cladosporioides
brenda
Zhang, P.; Zhou, P.P.; Yu, L.J.
An endophytic taxol-producing fungus from Taxus x media, Aspergillus candidus MD3
FEMS Microbiol. Lett.
293
155-159
2009
Aspergillus candidus (B6D960), Aspergillus candidus
brenda
Ondari, M.E.; Walker, K.D.
The taxol pathway 10-O-acetyltransferase shows regioselective promiscuity with the oxetane hydroxyl of 4-deacetyltaxanes
J. Am. Chem. Soc.
130
17187-17194
2008
Taxus cuspidata
brenda
Katkovcinova, Z.; Lazarova, M.; Brunakova, K.; Kosuth, J.; Cellarova, E.
Expression of dbat and dbtnbt genes involved in paclitaxel biosynthesis during the growth cycle of Taxus baccata L. callus cultures
Z. Naturforsch. C
63
721-730
2008
Taxus baccata (Q8W169)
brenda
Zhang, J.; Gong, S.; Guo, Z.
Effects of different elicitors on 10-deacetylbaccatin III-10-O-acetyl transferase activity and cytochrome P450 monooxygenase content in suspension cultures of Taxus cuspidata cells
Cell Biol. Int.
18
e00009
2010
Taxus cuspidata, Taxus cuspidata T5
brenda
Onrubia, M.; Moyano, E.; Bonfill, M.; Palazon, J.; Goossens, A.; Cusido, R.M.
The relationship between TXS, DBAT, BAPT and DBTNBT gene expression and taxane production during the development of Taxus baccata plantlets
Plant Sci.
181
282-287
2011
Taxus baccata
brenda
Han, F.; Kang, L.Z.; Zeng, X.L.; Ye, Z.W.; Guo, L.Q.; Lin, J.F.
Bioproduction of baccatin III, an advanced precursor of paclitaxol, with transgenic Flammulina velutipes expressing the 10-deacetylbaccatin III-10-O-acetyl transferase gene
J. Sci. Food Agric.
94
2376-2383
2014
Taxus chinensis, Taxus chinensis var. mairei
brenda
You, L.; Wei, T.; Zheng, Q.; Lin, J.; Guo, L.; Jiang, B.; Huang, J.
Activity essential residue analysis of taxoid 10beta-O-acetyl transferase for enzymatic synthesis of baccatin
Appl. Biochem. Biotechnol.
186
949-959
2018
Taxus mairei (H9BIH8)
brenda
Sah, B.; Subban, K.; Chelliah, J.
Cloning and sequence analysis of 10-deacetylbaccatin III-10-O-acetyl transferase gene and WRKY1 transcription factor from taxol-producing endophytic fungus Lasiodiplodia theobromea
FEMS Microbiol. Lett.
364
fnx253
2017
Lasiodiplodia theobromae (A0A0D4BT92), Lasiodiplodia theobromae
brenda
Lin, S.L.; Wei, T.; Lin, J.F.; Guo, L.Q.; Wu, G.P.; Wei, J.B.; Huang, J.J.; Ouyang, P.L.
Bio-production of baccatin III, an important precursor of paclitaxel by a cost-effective approach
Mol. Biotechnol.
60
492-505
2018
Taxus mairei (H9BIH8)
brenda
You, L.F.; Wei, T.; Zheng, Q.W.; Jiang, B.H.; Lin, J.F.; Guo, L.Q.
Optimization of baccatin III production by cross-linked enzyme aggregate of taxoid 10beta-O-acetyltransferase
Mol. Biotechnol.
61
p498-505
2019
Taxus mairei (H9BIH8)
brenda
Li, B.J.; Wang, H.; Gong, T.; Chen, J.J.; Chen, T.J.; Yang, J.L.; Zhu, P.
Improving 10-deacetylbaccatin III-10-beta-O-acetyltransferase catalytic fitness for Taxol production
Nat. Commun.
8
15544
2017
Taxus canadensis (B5KRF5), Taxus wallichiana (B5KRG1), Taxus brevifolia (B5KRG4), Taxus x media (Q6SQJ5), Taxus cuspidata (Q9M6E2)
brenda
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