Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.3.1.167: 10-deacetylbaccatin III 10-O-acetyltransferase

This is an abbreviated version!
For detailed information about 10-deacetylbaccatin III 10-O-acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.167

Reaction

acetyl-CoA
+
10-deacetylbaccatin III
=
CoA
 +
baccatin III

Synonyms

10-DAB, 10-DABT, 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-deacetylbaccatin III:10beta-O-acetyltransferase, 10-deacetylbaccatin-III-10beta-O-acetyltransferase, 10-hydroxytaxane 10-O-acetyltransferase, 10-hydroxytaxane O-acetyltransferase, 10beta-O-acetyltransferase, acetyl CoA:10-deacetylbaccatin-III 10-O-acetyltransferase, acetyl coenzyme A:10-hydroxytaxane O-acetyltransferase, DBAT, taxoid 10beta-O-acetyl transferase, taxoid 10beta-O-acetyltransferase, TmDBAT

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.167 10-deacetylbaccatin III 10-O-acetyltransferase

Engineering

Engineering on EC 2.3.1.167 - 10-deacetylbaccatin III 10-O-acetyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F160A
mutation negatively affects activity
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
F400A
mutation negatively affects activity
F44A
activity against 10-deacetyltaxol is nearly undetectable
G359A
mutation negatively affects activity
G361A
no activity against 10-deacetylbaccatin III or 10-deacetyltaxol
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
H162A
no activity against 10-deacetylbaccatin III or 10-deacetyltaxol
I164A
no activity against 10-deacetylbaccatin III or 10-deacetyltaxol
P37A
mutation negatively affects activity
R363A
no activity against 10-deacetylbaccatin III or 10-deacetyltaxol
D166A
decrease of kcat/KM of 10-deacetylbaccatin III and acetyl CoA
D34E
decrease of kcat/KM of 10-deacetylbaccatin III and acetyl CoA
D372E
decrease of kcat/KM of 10-deacetylbaccatin III and acetyl CoA
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
G376A
decrease of kcat/KM of 10-deacetylbaccatin III and acetyl CoA
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
R363A
decrease of kcat/KM of 10-deacetylbaccatin III and acetyl CoA
S31A
decrease of kcat/KM of 10-deacetylbaccatin III and acetyl CoA
additional information
-
functional expression in Saccharomyces cerevisiae for reconstruction of taxoid biosynthesis