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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

General Stability

General Stability on EC 2.3.1.167 - 10-deacetylbaccatin III 10-O-acetyltransferase

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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