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Information on EC 2.3.1.167 - 10-deacetylbaccatin III 10-O-acetyltransferase and Organism(s) Taxus cuspidata and UniProt Accession Q9M6E2
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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
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cephalomannine
- cuspidata
- taxadiene
-
diterpenoids
- 10-deacetyltaxol
- mairei
- wallichiana
-
oxetane
-
twigs
- pharmacology
- biotechnology
The taxonomic range for the selected organisms is: Taxus cuspidata
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
10-dab, 10-deacetylbaccatin iii-10-o-acetyl transferase, tmdbat, 10-deacetylbaccatin iii-10-o-acetyltransferase, 10-dabt, 10-dbat, 10-deacetylbaccatin iii-10beta-o-acetyltransferase, 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-deacetylbaccatin III-10beta-O-acetyltransferase
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-
-
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10-hydroxytaxane 10-O-acetyltransferase
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-
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10-hydroxytaxane O-acetyltransferase
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-
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acetyl CoA:10-deacetylbaccatin-III 10-O-acetyltransferase
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acetyl coenzyme A:10-hydroxytaxane O-acetyltransferase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
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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.
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
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-
-
-
?
acetyl-CoA + 10-deacetylbaccatin III
CoA + baccatin III
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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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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10-deacetylbaccatin III-10-O-acetyl transferase functions in the last step of Taxol core synthesis is the most important enzyme of the pathway
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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)
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
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)
-
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 baccata (B5KRG2), Taxus baccata (Q8W169), Taxus brevifolia (B5KRG4), Taxus canadensis (B5KRF5), Taxus chinensis (B5KRF6), Taxus chinensis (B5KRG3), Taxus cuspidata (Q9M6E2), Taxus fuana (B5KRF8), Taxus globosa (B5KRG6), Taxus mairei (B5KRG1), Taxus mairei (Q67DV6), Taxus sumatrana (B5KRG5), Taxus wallichiana var. wallichiana (B5KRF7), Taxus x hunnewelliana (B5KRF3), Taxus x media (A0MPB1)
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
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
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 brevifolia (B5KRG4), Taxus canadensis (B5KRF5), Taxus cuspidata (Q9M6E2), Taxus wallichiana (B5KRG1), Taxus x media (Q6SQJ5)
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