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1.1.1.6: glycerol dehydrogenase

This is an abbreviated version!
For detailed information about glycerol dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.6

Reaction

glycerol
+
NAD+
=
Glycerone
+
NADH
+
H+

Synonyms

B4100_2156, CglD, dehydrogenase, glycerol, GDH, GDH2, GLD, Gld3, GldA, GLDH , GlhA, glycerin dehydrogenase, glycerol dehydrogenase, glycerol NAD 2-oxidoreductase, glycerol:NAD+ 2-oxidoreductase, GlyDH, Gro dehydrogenase, GroDHase, GSH, gycerol dehydrogenase, NAD+-dependent glycerol dehydrogenase, NAD-linked glycerol dehydrogenase, NAD-specific glycerol dehydrogenase, TmGlyDH, TTHADH

ECTree

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

Engineering

Engineering on EC 1.1.1.6 - glycerol dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A15T/D16G/V17A/N19K/E23D/Q45E/S46E/T47M/V48L/E49R/F52L/K53A/V58A/V59A/Q70H/D74N/G78D/E81G/T82N/Q83K/G86T/I88V/G108N/R139S/L142M/N145R/K155Q/V256I/L260M
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
D121A
-
D121 can potentially hinder the proper binding of substrate 1,3-butanediol due to steric hindrance
D16N/N19A/E23D/L28M/E30N/R31N/Q45E/S46E/V48L/E49R/F52L/K53T/D54G/V58S/G78V/I79V/T82K/A83S/I88V/G108N/R139S/L142M/N145R/K155Q/L211I/G248S/V256I/H268Y/D317E/P319L
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
Q70H/D121A/G193C/E291Q/A310T
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae) and site-directed mutation D121A
Q70H/D74N/G78D/E81G/T82N/Q83K/C84Y/G86T/I88V/G108N/E134A/E204K/L211I/E215K/I234V/V256I/L260M/E291D/S300C/A302S/E316G/V318I/A320T/I324L/T344D/P345S
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
Q70H/G193C/E291Q/A310T
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
D123N
mutation abolishes the oxidative activity. The carboxylate of D123 is the base needed for abstracting the proton to form the alkoxy intermediate that precedes the hydride transfer to the nicotinamide cofactor
L252A
S305C
-
S305C mutant used for crystallisation
V131A
about 70% of wild-type activity with glycerol
Y142A
mutation reduces the enzyme activity to less than 10% of wild-type activity
I154A
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
I154A/K157G
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
I154A/K157N
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
K157G
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
K157N
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
V44A
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
V44A/I154A
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
V44A/K157G
V44A/K157N
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
I154A
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
-
K157N
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
-
V44A
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
-
V44A/K157G
D121N
mutation lowers the activity of the enzyme with most all the tested substrates relative to the native enzyme
D121N/F245S
mutant acquires D-lactate dehydrogenase activiy, the alteration increases the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 gamma-O and the C1 carboxylate of pyruvate
F245S
mutant acquires D-lactate dehydrogenase activiy, the alteration increases the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 gamma-O and the C1 carboxylate of pyruvate
additional information