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

BRENDA support

2.3.1.41: beta-ketoacyl-[acyl-carrier-protein] synthase I

This is an abbreviated version!
For detailed information about beta-ketoacyl-[acyl-carrier-protein] synthase I, go to the full flat file.

Word Map on EC 2.3.1.41

Reaction

an acyl-[acyl-carrier protein]
+
a malonyl-[acyl-carrier protein]
=
a 3-oxoacyl-[acyl-carrier protein]
+
CO2
+
an [acyl-carrier protein]

Synonyms

3-ketoacyl-ACP synthase, 3-ketoacyl-acyl carrier protein synthase, 3-ketoacyl-acyl-carrier protein synthase I, 3-oxoacyl synthase, 3-oxoacyl-[acyl-carrier-protein] synthase, acyl-malonyl(acyl-carrier-protein)-condensing enzyme, B-ketoacyl-ACP synthase I, beta-ketoacyl ACP synthase I, beta-ketoacyl acyl carrier protein synthase, beta-ketoacyl acyl carrier protein synthase I, beta-ketoacyl synthase, beta-ketoacyl synthetase, beta-ketoacyl [ACP] synthase, beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP synthase I, beta-ketoacyl-ACP synthetase, beta-ketoacyl-ACP-synthase, beta-ketoacyl-ACP-synthase I, beta-ketoacyl-acyl carrier protein synthase I, beta-ketoacyl-acyl carrier protein synthetase, beta-ketoacyl-acyl-ACP synthase I, beta-ketoacyl-CoA synthase-I, beta-ketoacyl-[acyl carrier protein (ACP)] synthase III, beta-ketoacyl-[acyl carrier protein] synthase, beta-ketoacyl-[acyl carrier protein] synthase I, beta-ketoacyl-[acyl-carrier-protein] synthase I, beta-ketoacylsynthase, condensing enzyme, Cys-His-His-type beta-ketoacyl-acyl carrier protein synthase, DpsC, elongase, elongating beta-ketoacyl-acyl carrier protein synthase, FabB, FabBF, FabH, fatty acid condensing enzyme, KAS, Kas A, KAS I, KasA, KasI, KASI-1, KASI-2, KCSI, More, OsKASI, synthase, 3-oxoacyl-[acyl-carrier-protein]

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.41 beta-ketoacyl-[acyl-carrier-protein] synthase I

Engineering

Engineering on EC 2.3.1.41 - beta-ketoacyl-[acyl-carrier-protein] synthase I

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
C163A
-
synthase I, site-directed mutagenesis, active site mutant, no activity, but decarboxylates malonyl-[acyl-carrier-protein]
C163S
-
synthase I, site-directed mutagenesis, active site mutant, increased activity, decarboxylates malonyl-[acyl-carrier-protein]
D306A
-
synthase I, site-directed mutagenesis, active site mutant, increased activity
E309A
-
synthase I, site-directed mutagenesis, active site mutant, reduced activity
H298A
-
synthase I, site-directed mutagenesis, active site mutant, reduced activity
H298E
-
site-directed mutagenesis, the mutant is decarboxylation deficient, residual decarboxylase activity in the range of pH 6.0–8.0, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure
H298Q
-
site-directed mutagenesis, the mutant is completely decarboxylation deficient, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure
H333A
-
synthase I, site-directed mutagenesis, active site mutant, increased activity
K151Q
-
conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
K328A
K328E
-
site-directed mutagenesis, the mutant is almost completely decarboxylation deficient
K328F
-
site-directed mutagenesis, the mutant is completely decarboxylation deficient
K328H
-
site-directed mutagenesis, the mutant is completely decarboxylation deficient
K328I
-
site-directed mutagenesis, the mutant is almost completely decarboxylation deficient
K328R
-
site-directed mutagenesis, the mutant is almost completely decarboxylation deficient, crystal structure determination with the free mutant enzyme, comparison to the wild-type enzyme structure
K63Q
-
conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
R62Q
-
conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
R66Q
-
conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
C171Q
-
mimics the acyl enzyme intermediate
D66N
the non-active site mutation alters the structural stability of the mutant protein structures
F413L
the non-active site mutation alters the structural stability of the mutant protein structures
G269S
the non-active site mutation alters the structural stability of the mutant protein structures
G312S
the non-active site mutation alters the structural stability of the mutant protein structures
R161A
-
69.6% of wild-type activity
R46A
-
7.3% of wild-type activity
R46A/R161A
-
0.3% of wild-type activity
T97F
-
no enzymic activity
W42A
-
21.5% of wild-type activity
W42A/R161A
-
0.2% of wild-type activity
D66N
-
the non-active site mutation alters the structural stability of the mutant protein structures
-
F413L
-
the non-active site mutation alters the structural stability of the mutant protein structures
-
G269S
-
the non-active site mutation alters the structural stability of the mutant protein structures
-
G312S
-
the non-active site mutation alters the structural stability of the mutant protein structures
-
C161Q
-
site-directed mutagenesis, active site Cys mutant, no condensation activity, but 377fold increased decarboxylation activity
C122A
-
site-directed mutagenesis, 75% enhanced production of straight-chain fatty acids relative to branched-chain fatty acids compared to wild-type
C122Q
-
site-directed mutagenesis, 500% enhanced production of straight-chain fatty acids relative to branched-chain fatty acids compared to wild-type
C122S
-
site-directed mutagenesis, enhanced production of straight-chain fatty acids relative to branched-chain fatty acids compared to wild-type
A193M
-
site-directed mutagenesis, hydrophobic acyl-binding pocket is decreased in size by 2.55fold, 12fold reduced catalytic activity
I108F
-
site-directed mutagenesis, hydrophobic acyl-binding pocket is decreased in size by 1.75fold, 38fold reduced catalytic activity towards octanoyl-[acyl-carrier-protein] compared to the activity towards hexanoy-[acyl-carrier-protein]
additional information