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2.3.1.9: acetyl-CoA C-acetyltransferase

This is an abbreviated version!
For detailed information about acetyl-CoA C-acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.9

Reaction

2 acetyl-CoA =

CoA
+
acetoacetyl-CoA

Synonyms

2-methylacetoacetyl-CoA thiolase, 3-ketoacyl-CoA (T1)-like thiolase, 3-ketoacyl-CoA thiolase, 3-ketoacyl-coenzyme A thiolase, 3-oxothiolase, A1887, AACT, AACT1, AACT2, ACAT, ACAT1, ACAT2, ACCT, acetoacetyl CoA thiolase, acetoacetyl-CoA acetyltransferase, acetoacetyl-CoA C-acetyltransferase, acetoacetyl-CoA thiolase, acetoacetyl-CoA thiolase T2, acetyl coenzyme A thiolase, acetyl-CoA acetyltransferase, acetyl-CoA C-acetyltransferase, acetyl-CoA:N-acetyltransferase, acetyltransferase, acetyl coenzyme A, ACOAT, ACTRANS, AFUB_000550, AtoB, beta-acetoacetyl coenzyme A thiolase, beta-ketoacyl-CoA thiolase, beta-ketothiolase, CT, cytosolic acetoacetyl-CoA thiolase, cytosolic acetoacetyl-CoA thiolase 1, cytosolic acetoacetyl-CoA thiolase 2, ERG10, Erg10A, HFX_1022, HFX_1023, HFX_6003, HFX_6004, KACT, MmgA, Msed_0656, MSM-13 thiolase, OsAT1, phaA, ReH16_B0759, thiolase II, ThL, Tneu_0249, type II thiolase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.9 acetyl-CoA C-acetyltransferase

Engineering

Engineering on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V77Q/N153Y/A286K
the mutant, which is not able to form disulfide bonds, exhibits higher activity than the wild type enzyme
C377A
site-directed mutagenesis, almost inactive mutant
C378A
site-directed mutagenesis, almost inactive mutant
C89A
site-directed mutagenesis, almost inactive mutant
C91A
site-directed mutagenesis, almost inactive mutant
F156A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H347A
site-directed mutagenesis, almost inactive mutant
H348A
site-directed mutagenesis, almost inactive mutant
K17A
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
K18A
site-directed mutagenesis, the mutant shows over 80% reduced activity compared to the wild-type enzyme
K217A
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
M124A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q151A
site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type enzyme
R210A
site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme
R220A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V231A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C377A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis, almost inactive mutant
-
C89A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis, almost inactive mutant
-
C91A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis, almost inactive mutant
-
F156A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
K17A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
-
K18A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis, the mutant shows over 80% reduced activity compared to the wild-type enzyme
-
K217A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
-
Q151A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type enzyme
-
R210A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme
-
R220A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
E252del
M193T
-
naturally occuring mutation leading to enzyme deficiency and to the ketoacidotic episode phenotype, but with differing clinical severity, overview
N158D
N158S
N282H
N353K
Q272X
-
no residual activity under any condition
R208Q
Y219H
C92S
-
kcat decreases to 0.2% of that for the recombinant thiolase
C378G
-
mutation eliminates the ability of thiolase to catalyze proton abstraction from C2 of acetyl-CoA
C89A
no thiolytic activity towards acetoacetyl-CoA
Q64A
30% lower kcat than that of the wild-type
additional information