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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.

Word Map on EC 1.1.1.30

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, Psyc_1428

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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PROTEIN VARIANTS
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
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
W187F
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
H141A
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
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