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2.3.1.179: beta-ketoacyl-[acyl-carrier-protein] synthase II

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

Word Map on EC 2.3.1.179

Reaction

a (Z)-hexadec-9-enoyl-[acyl-carrier protein]
+
a malonyl-[acyl-carrier protein]
=
a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein]
+
CO2
+
an [acyl-carrier protein]

Synonyms

3-ketoacyl acyl synthase II, 3-ketoacyl-ACP synthase, 3-ketoacyl-ACP synthase 2, 3-ketoacyl-ACP synthase II, 3-oxoacyl-(acylcarrier protein) synthase II, 3-oxoacyl-ACP synthase II, B-ketoacyl-ACP synthase II, beta-ketoacyl ACP-synthase II, beta-ketoacyl acyl carrier protein synthase II, beta-ketoacyl acyl-carrier protein synthase II, beta-ketoacyl synthase II, beta-ketoacyl-(acyl-carrier-protein) synthase II, beta-ketoacyl-ACP synthase FabF3, beta-ketoacyl-ACP synthase II, beta-ketoacyl-acyl carrier protein synthase I/II, beta-ketoacyl-acyl carrier protein synthase II, beta-ketoacyl-acyl carrier protein synthases II, beta-ketoacyl-acyl carrier protein synthetase II, beta-ketoacyl-acyl-carrier protein synthase II, beta-ketoacyl-acyl-carrier-protein synthase II, beta-ketoacyl-[ACP] synthase II, beta-ketoacyl-[ACP] synthase-II, beta-ketoacyl-[acyl carrier protein (ACP)] synthase II, beta-ketoacyl-[acyl-carrier protein (ACP)] synthase II, beta-ketoacyl-[acyl-carrier-protein] synthase II, FabB, FabB/F, FabF, FabF elongation condensing enzyme, FabF of type II fatty acid biosynthesis, FabF1, FASII, fatty acid synthesis type II, KAS II, KAS-II, KAS2, KASII

ECTree

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

Engineering

Engineering on EC 2.3.1.179 - beta-ketoacyl-[acyl-carrier-protein] synthase II

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L337F
the point mutation, mutant fab1-1, causes a partially deficient KAS2 activity
E122K
the mutant is less inhibited by cerulenin and platensimycin compared to the wild type enzyme and is resistant towards inhibition by acylated sulfonamides
G200S
the mutant is resistant towards inhibition by acylated sulfonamides
E122K
-
the mutant is less inhibited by cerulenin and platensimycin compared to the wild type enzyme and is resistant towards inhibition by acylated sulfonamides
-
G200S
-
the mutant is resistant towards inhibition by acylated sulfonamides
-
C163Q
site-directed mutagenesis, interaction with platensimycin compared to the interaction with the wild-type enzyme
R206G
-
R206 impairs the binding of CoA
C164Q
site-directed mutagenesis, a mutant in which the binding site is altered to resemble the substrate-bound state
C164A
-
site-directed mutagenesis, inactive mutant
C164A/H337A
-
site-directed mutagenesis, inactive mutant
C164A/K332A
-
site-directed mutagenesis, inactive mutant
E346A
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
E383A
crystal structure determination and comparison to the wild-type enzyme, the mutation E383A appears to play a key role in disfavouring the less desirable triclinic crystal form and in generating a new surface for a packing interaction that stabilizes the new crystal form
E396A
-
site-directed mutagenesis, the mutant shows no condensation activity but retains about 50% of wild-type transacylation activity with acyl-ACP and ACP, and 40% of wild-type decarboxylation activity
H303A
-
site-directed mutagenesis, the mutant shows 74% reduced condensation activity, 40% reduced transacylation activity, and 5fold increased decarboxylation activity, compared to the wild-type enzyme
H337A
-
site-directed mutagenesis, inactive mutant
K332A
-
site-directed mutagenesis, the mutant shows no condensation activity but retains about 30% of wild-type transacylation activity with acyl-ACP and ACP, and 10% of wild-type decarboxylation activity
F107I
-
less efficient than wild type protein
F107L
-
less efficient than wild type protein
F107S
-
suggested that the Ser residue has less significant effects than the Ile and Leu mutations
additional information