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1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase

This is an abbreviated version!
For detailed information about 3-oxoacyl-[acyl-carrier-protein] reductase, go to the full flat file.

Word Map on EC 1.1.1.100

Reaction

a (3R)-3-hydroxyacyl-[acyl-carrier protein]
+
NADP+
=
a 3-oxoacyl-[acyl-carrier protein]
+
NADPH
+
H+

Synonyms

3-ketoacyl acyl carrier protein reductase, 3-ketoacyl-(acyl-carrier-protein) reductase, 3-ketoacyl-ACP reductase, 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenase, 3-ketoacyl-ACP(CoA) reductase, 3-ketoacyl-acyl carrier protein reductase, 3-ketoacyl-thioester reductase, 3-ketoacyl-[acyl-carrier-protein] reductase, 3-oxo-acyl-ACP reductase, 3-oxoacyl-(acyl carrier protein) reductase, 3-oxoacyl-(acyl-carrier-protein) reductase, 3-oxoacyl-ACP reductase, 3-oxoacyl-AcpM reductase, 3-oxoacyl-thioester reductase, 3-oxoacyl-[ACP]reductase, ACP reductase, beta-ketoacyl acyl carrier protein (ACP) reductase, beta-ketoacyl acyl carrier protein reductase, beta-ketoacyl reductase, beta-ketoacyl thioester reductase, beta-ketoacyl-(acyl carrier protein) reductase, beta-ketoacyl-ACP reductase, beta-ketoacyl-acyl carrier protein reductase, beta-ketoacyl-[acyl carrier protein] reductase, beta-ketoacyl-[acyl-carrier protein] (ACP) reductase, BKR, FabG, FabG1, FabG2, fabG3, fabG4, KACPR, KAR, KCR1, KCR2, ketoacyl-acyl carrier protein reductase, MabA, MSMEG_3150, MSMEG_6753, NADPH-dependent acetoacetyl coenzyme A reductase, NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase, OAR, OAR1, Oar1p, PA4389, PA4786, PHA-specific acetoacetyl-CoA reductase, PhaB, pks3, polyhydroxyalkanoate-specific acetoacetyl coenzyme A reductase, reductase, 3-oxoacyl-[acyl carrier protein], RhlG, XCC0416

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase

Engineering

Engineering on EC 1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q47L
the mutant with increased specific activity exhibits a kcat value that is 2.4fold higher than that of the wild type enzyme
T173S
the mutant with increased specific activity exhibits a kcat value that is 3.5fold higher than that of the wild type enzyme
Q47L
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
the mutant with increased specific activity exhibits a kcat value that is 2.4fold higher than that of the wild type enzyme
-
T173S
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
the mutant with increased specific activity exhibits a kcat value that is 3.5fold higher than that of the wild type enzyme
-
A154T
-
similar thermal stability as wild-type enzyme
A154T/E233K
-
temperature-sensitive phenoptype, reductase activity is much more thermolabile than the activity of the wild-type strain
E233K
-
temperature-sensitive phenoptype, reductase activity is much more thermolabile than the activity of the wild-type strain
F87T
-
coexpression with fabH mutant F87T and polyhydroxyalkanoate synthase genes enhances the production of short chain length-medium chain length polyhydroxyalkanoate copolymer from both related and unrelated carbon sources
D42A
the mutant shows 36% activity with acetoacetyl-CoA and NADH, 20% activity with acetoacetyl-CoA and NADPH, 4% activity with 9,10-phenanthrene and NAD+, and 26% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
K152A
the mutant shows 109% activity with acetoacetyl-CoA and NADH, no activity with acetoacetyl-CoA and NADPH, 123% activity with 9,10-phenanthrene and NAD+, and 2.2% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
K169E
the mutant shows 95% activity with acetoacetyl-CoA and NADH, 5.5% activity with acetoacetyl-CoA and NADPH, 76% activity with 9,10-phenanthrene and NAD+, and 6% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
K173A
the mutant shows 0.3% activity with acetoacetyl-CoA and NADH, 2.4% activity with acetoacetyl-CoA and NADPH, 6% activity with 9,10-phenanthrene and NAD+, and 22% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
Q126E/K169E
the mutant shows 156% activity with acetoacetyl-CoA and NADH, 4.3% activity with acetoacetyl-CoA and NADPH, 84% activity with 9,10-phenanthrene and NAD+, and 8% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
Q126E/R168E/K169E
the mutant shows 72% activity with acetoacetyl-CoA and NADH, 0.5% activity with acetoacetyl-CoA and NADPH, 40% activity with 9,10-phenanthrene and NAD+, and no activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
R168E
the mutant shows 106% activity with acetoacetyl-CoA and NADH, 6.3% activity with acetoacetyl-CoA and NADPH, 38% activity with 9,10-phenanthrene and NAD+, and 8% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
R34A
the mutant shows 102% activity with acetoacetyl-CoA and NADH, 100% activity with acetoacetyl-CoA and NADPH, 40.44% activity with 9,10-phenanthrene and NAD+, and 2.1% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
Y169A
the mutant shows 3% activity with acetoacetyl-CoA and NADH, 2% activity with acetoacetyl-CoA and NADPH, 4% activity with 9,10-phenanthrene and NAD+, and 15% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
S140A
-
mutant shows no enzymatic activity. S140A mutant does not bind to NADPH
S140T
-
mutant shows no enzymatic activity. Mutant S140T shows impaired NADPH binding
R187A
-
kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 3fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187A/R230A
-
kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. 5fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187E
-
kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 4fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187E/R230E
-
kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. 80fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187K
-
no decreased affinity binding to acyl-carrier protein with respect to wild-type
R230A
-
kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 5fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R230E
-
kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 41fold decreased affinity binding to acyl-carrier protein with respect to wild-type
S36A
the mutant shows reduced activity compared to the wild type enzyme
S40A
the mutant shows reduced activity compared to the wild type enzyme
E233K
-
temperature-sensitive mutant enzyme does not allow growth of Escherichia coli at 42°C in complementation assay
M125I/S233T
-
temperature-sensitive mutant enzyme does not allow growth of Escherichia coli at 42°C in complementation assay
G141A
-
the mutant shows less than 5% of wild type activity
G92A
-
the mutant shows less than 60% of wild type activity
G92D
-
the mutant shows less than 5% of wild type activity
Q152A
-
the mutant shows less than 10% of wild type activity
Y155F
-
the mutant shows less than 3% of wild type activity
additional information