1.1.1.30: 3-hydroxybutyrate dehydrogenase

This is an abbreviated version, for detailed information about 3-hydroxybutyrate dehydrogenase, go to the full flat file.

Reaction

(R)-3-hydroxybutanoate
+
NAD+
=
acetoacetate
+
NADH
+
H+

Synonyms

3-D-hydroxybutyrate dehydrogenase, 3-HBDH, 3-hydroxybutyrate dehydrogenase, 3-hydroxybutyrate dehydrogenase 2, 3-hydroxybutyrate dehydrogenase-2, 3HBDH, acetoacetyl-CoA reductase, BDH, BDH1, BDH2, BDH3, BdhA, beta-hydroxybutyrate dehydrogenase, beta-hydroxybutyric acid dehydrogenase, beta-hydroxybutyric dehydrogenase, D(-)-3-hydroxybutyrate dehydrogenase, D-(-)-3-hydroxybutyrate dehydrogenase, D-3-hydroxybutyrate dehydrogenase, D-beta-hydroxybutyrate dehydrogenase, DHRS6, HBD, HBDH, hydroxybutyrate oxidoreductase, More, NAD-beta-hydroxybutyrate dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.30 3-hydroxybutyrate dehydrogenase

Engineering

Engineering on EC 1.1.1.30 - 3-hydroxybutyrate dehydrogenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H144A
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144F
-
the mutant shows increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H144I
-
the mutant shows increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L/W187A
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L/W187F
H144L/W187I
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L/W187L
-
the mutant shows strongly increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L/W187V
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144V
-
the mutant shows wild type catalytic efficiency with levulinic acid
W187A
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
W187I
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
W187L
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
W187V
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
C242S
-
PCR derived cDNA clone
M92V
-
PCR derived cDNA clone
S24T
-
PCR derived cDNA clone
H144A
-
catalytic efficiency (kcat/Km) is 0.2% of the activity of wild-type HBDH
K152A
-
no activity
K152E
-
very low activity
K152Q
-
very low activity
K152R
-
retains a significant level of activity
L215A
-
both Km and kcat values are largely affected and the catalytic efficiency (kcat/Km) is less than 3% that of the wild-type enzyme
L215V
-
Km values increase 3.5- and 4.3fold and the kcat values are 73-118% those of the wild-type toward D-3-hydroxybutyrate and acetoacetate, respectively. Mutation does not significantly change Km and kcat toward NAD+ and NADH
Q196A
-
kcat/Km value is 0.6% that of the wild-type
Q196E
-
substantially reduced activity
Q196N
-
substantially reduced activity
Q94A
-
catalytic efficiency (kcat/Km) is 1.4% of the activity of wild-type HBDH
T190A
-
activity decreases to 0.1% that of the wild-type enzyme
T190C
-
decreased activity
T190S
-
retains 37% of the activity
W187A
-
very low activity
W187F
-
shows significant activity levels, 65% that of the wild-type enzyme
W187T
-
shows faint activity
W187Y
-
shows significant activity levels, 41% that of the wild-type enzyme
W257A
-
no activity
W257F
-
shows low activity levels, 2% that of the wild-type enzyme
W257Y
-
shows low activity levels, 1% that of the wild-type enzyme
Y155F
-
no activity
K149A
-
inactive mutant enzyme
K149R
-
kcat/KM for (R)-3-hydroxybutanoate is 184.2fold lower than wild-type value, kcat/Km for NAD+ is 7.2fold lower than wild-type enzyme
L149A
-
inactive
Q133A
-
decreased activity
Q193A
-
kcat/KM for (R)-3-hydroxybutanoate is 307fold lower than wild-type value, kcat/Km for NAD+ is 6.2fold lower than wild-type enzyme
additional information