1.1.1.119: glucose 1-dehydrogenase (NADP+)

This is an abbreviated version, for detailed information about glucose 1-dehydrogenase (NADP+), go to the full flat file.

Reaction

D-glucose
+
NADP+
=
D-glucono-1,5-lactone
+
NADPH
+
H+

Synonyms

beta-D-glucose: NAD(P) 1-oxidoreductase, dehydrogenase, glucose (nicotinamide adenine dinucleotide phosphate), GDH, GlcDH, GlcDH 2, glucose dehydrogenase, halophilic glucose dehydrogenase, Hm GDH, NAD(P)+ glucose dehydrogenase, NADP-dependent glucose dehydrogenase, NADP-linked aldohexose dehydrogenase, nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase, STK_17040

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.119 glucose 1-dehydrogenase (NADP+)

Engineering

Engineering on EC 1.1.1.119 - glucose 1-dehydrogenase (NADP+)

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D172K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D172K/D216K/D344K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D216K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D344K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D38C
-
crystallization of a range of binary and ternary complexes of the wild-type and a D38C mutant protein
G206D
-
less efficient with NADP+ than the wild type, 1.6fold increase in ratio kcat/Km for NAD+; prefers NAD+ over NADP+; the mutant is less efficient with NADP+ than the wild type enzyme, the relation kcat/KNAD+ is 1.6times higher than in the wild type, resulting in an enzyme that prefers NAD+ over NADP+
G206D/R207I
-
active only with NAD+; no activity with NADP+, highest reaction rate with cofactor NAD+ of all mutants tested; the mutant shows no activity with NADP+, when the coenzyme NAD+ is incubated with this double mutant, it reaches the highest kcat value, between 1.5 and 2times higher than the kcat of the wild type enzyme with NADP+, and between 3 and 4times higher than the kcat of the wild type with NAD+
G206D/R207I/R208N
-
active only with NAD+; no activity with NADP+; the mutant shows no activity with NADP+
R207I
-
less efficient with NAD+ or NADP+ than the wild-type enzyme; less efficient with NADP+ than the wild type; the mutant is less efficient with NADP+ than the wild type enzyme, shows an increase of 48times in Km value with NADP+ when compared with the wild type accompanied by a decrease in kcat, which clearly makes the R207I mutant less efficient in catalysis with NADP+, the R207I substitution also makes the enzyme less efficient with NAD+, with a decrease of 4 times in kcat/Km, this substitution also increases the Km for glucose
D38C
-
crystallization of a range of binary and ternary complexes of the wild-type and a D38C mutant protein
-
additional information
-
Escherichia coli strain expressing both recombinant glucose 1-dehydrogenase and a glucose facilitator for uptake of unphosphorylated glucose shows a nine times higher initial alpha-pinene oxide formation rate corresponding to a sixfold higher yield of 20 mg per g cell dry weight after 1.5 h and to a sevenfold increased alpha-pinene oxide yield in the presence of glucose compared to glucose-free conditions; introduction of both, GLF and GlcDH, in P450-overexpressing Escherichia coli should enable the cell to carry out a straightforward intracellular cofactor regeneration driven by externally added glucose. For the generation of recombinant Escherichia coli strains carrying two plasmids, these are transformed successively. Firstly, pZY507glf is transformed into Escherichia coli BL21 (DE3). Subsequently, competent cells are prepared from a positive transformant, and then pETDUETbm-3qm glcdh is transformed.