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Literature summary for 2.3.1.167 extracted from

  • 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 (2017), Nat. Commun., 8, 15544 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.167

Application

Application Comment Organism
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 Taxus cuspidata

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Taxus cuspidata
expression in Escherichia coli Taxus canadensis
expression in Escherichia coli Taxus x media
expression in Escherichia coli Taxus brevifolia
expression in Escherichia coli Taxus wallichiana

Protein Variants

Protein Variants Comment Organism
F160A mutation negatively affects activity Taxus cuspidata
F301A activity against 10-deacetyltaxol is 1.6times more active than wild-type activity, activitys against 10-deacetylbaccatin III is degraded Taxus cuspidata
F301V mutant enzyme is 2.85times more active against 10-deacetyltaxol than the wild-type enzyme Taxus cuspidata
F400A mutation negatively affects activity Taxus cuspidata
F44A activity against 10-deacetyltaxol is nearly undetectable Taxus cuspidata
G359A mutation negatively affects activity Taxus cuspidata
G361A no activity against 10-deacetylbaccatin III or 10-deacetyltaxol Taxus cuspidata
G38A activity against 10-deacetyltaxol is 1.45times more active than wild-type activity, activitys against 10-deacetylbaccatin III is slightly decreased Taxus cuspidata
G38R mutant enzyme is 2.19times more active against 10-deacetyltaxol than the wild-type enzyme Taxus cuspidata
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 Taxus cuspidata
H162A no activity against 10-deacetylbaccatin III or 10-deacetyltaxol Taxus cuspidata
I164A no activity against 10-deacetylbaccatin III or 10-deacetyltaxol Taxus cuspidata
P37A mutation negatively affects activity Taxus cuspidata
R363A no activity against 10-deacetylbaccatin III or 10-deacetyltaxol Taxus cuspidata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.178
-
 10-deacetyltaxol mutant enzyme F301V, pH 5.5, 37.5°C Taxus cuspidata
0.368
-
 10-deacetyltaxol mutant enzyme G38R, pH 5.5, 37.5°C Taxus cuspidata
0.424
-
 10-deacetyltaxol mutant enzyme G38R/F301V, pH 5.5, 37.5°C Taxus cuspidata
0.546
-
 10-deacetyltaxol wild-type enzyme, pH 5.5, 37.5° Taxus cuspidata

Organism

Organism UniProt Comment Textmining
Taxus brevifolia B5KRG4
-
-
Taxus canadensis B5KRF5
-
-
Taxus cuspidata Q9M6E2
-
-
Taxus wallichiana B5KRG1
-
-
Taxus x media Q6SQJ5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Taxus cuspidata
-
 Taxus canadensis
-
 Taxus x media
-
 Taxus brevifolia
-
 Taxus wallichiana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + 10-deacetylbaccatin III
-
 Taxus cuspidata CoA + baccatin III
-
 ?
acetyl-CoA + 10-deacetylbaccatin III
-
 Taxus canadensis CoA + baccatin III
-
 ?
acetyl-CoA + 10-deacetylbaccatin III
-
 Taxus x media CoA + baccatin III
-
 ?
acetyl-CoA + 10-deacetylbaccatin III
-
 Taxus brevifolia CoA + baccatin III
-
 ?
acetyl-CoA + 10-deacetylbaccatin III
-
 Taxus wallichiana CoA + baccatin III
-
 ?
acetyl-CoA + 10-deacetyltaxol
-
 Taxus cuspidata CoA + paclitaxel
-
 ?
acetyl-CoA + 10-deacetyltaxol
-
 Taxus canadensis CoA + taxol
-
 ?
acetyl-CoA + 10-deacetyltaxol
-
 Taxus x media CoA + taxol
-
 ?
acetyl-CoA + 10-deacetyltaxol
-
 Taxus brevifolia CoA + taxol
-
 ?
acetyl-CoA + 10-deacetyltaxol
-
 Taxus wallichiana CoA + taxol
-
 ?

Synonyms

Synonyms Comment Organism
10-deacetylbaccatin III-10-beta-O-acetyltransferase
-
 Taxus cuspidata
10-deacetylbaccatin III-10-beta-O-acetyltransferase
-
 Taxus canadensis
10-deacetylbaccatin III-10-beta-O-acetyltransferase
-
 Taxus x media
10-deacetylbaccatin III-10-beta-O-acetyltransferase
-
 Taxus brevifolia
10-deacetylbaccatin III-10-beta-O-acetyltransferase
-
 Taxus wallichiana
DBAT
-
 Taxus cuspidata
DBAT
-
 Taxus canadensis
DBAT
-
 Taxus x media
DBAT
-
 Taxus brevifolia
DBAT
-
 Taxus wallichiana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
38
-
 substrate: 10-deacetyltaxol Taxus cuspidata
40
-
 substrate: 10-deacetylbaccatin III Taxus cuspidata

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.000334
-
 10-deacetyltaxol wild-type enzyme, pH 5.5, 37.5° Taxus cuspidata
0.000396
-
 10-deacetyltaxol mutant enzyme F301V, pH 5.5, 37.5°C Taxus cuspidata
0.000815
-
 10-deacetyltaxol mutant enzyme G38R, pH 5.5, 37.5°C Taxus cuspidata
0.001499
-
 10-deacetyltaxol mutant enzyme G38R/F301V, pH 5.5, 37.5°C Taxus cuspidata

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 substrates: 10-deacetylbaccatin III, 10-deacetyltaxol Taxus cuspidata

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.000611
-
 10-deacetyltaxol wild-type enzyme, pH 5.5, 37.5°C Taxus cuspidata
0.002218
-
 10-deacetyltaxol mutant enzyme G38R, pH 5.5, 37.5°C Taxus cuspidata
0.00222
-
 10-deacetyltaxol mutant enzyme F301V, pH 5.5, 37.5°C Taxus cuspidata
0.003539
-
 10-deacetyltaxol mutant enzyme G38R/F301V, pH 5.5, 37.5°C Taxus cuspidata