Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.1.119 - glucose 1-dehydrogenase (NADP+) and Organism(s) Haloferax mediterranei and UniProt Accession Q977U7

for references in articles please use BRENDA:EC1.1.1.119
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Haloferax mediterranei
UNIPROT: Q977U7
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Haloferax mediterranei
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glcdh, glucose-1-dehydrogenase, nadp-dependent glucose dehydrogenase, nad(p)-dependent gdh, halophilic glucose dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-D-glucose: NAD(P) 1-oxidoreductase
-
glucose dehydrogenase
-
halophilic glucose dehydrogenase
-
NAD(P)+ glucose dehydrogenase
-
dehydrogenase, glucose (nicotinamide adenine dinucleotide phosphate)
-
-
-
-
glucose dehydrogenase
-
-
NADP-dependent glucose dehydrogenase
-
-
-
-
NADP-linked aldohexose dehydrogenase
-
-
-
-
nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
D-glucose:NADP+ 1-oxidoreductase
Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-50-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-D-glucose + NAD+
?
show the reaction diagram
activity with NAD+ is 26% of the activity with NADP+
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
the enzyme has a strong preference for NADP+ over NAD+
-
-
?
beta-D-glucose + NADP+
?
show the reaction diagram
activity with NAD+ is 26% of the activity with NADP+. The enzyme shows also activity with D-fucose and NADP+ (at 18% compared to the activity with beta-D-glucose and NADP+), with D-galactose and NADP+ (at 13% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NAD+ (at 79% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NADP+ (at 88% compared to the activity with beta-D-glucose and NADP+)
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
show the reaction diagram
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
-
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
show the reaction diagram
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH
show the reaction diagram
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH
show the reaction diagram
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
Km-value for NAD+ is 50fold higher than Km-value for NADP+
NADP+
NAD+
poor substrate for wild-type
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M
Mg2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Mg2+ is more effective than Mg2+ or Ni2+
Mn2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Mn2+ is less effective than Mg2+ and more effective than Ni2+
NaCl
the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M
Ni2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Ni2+ is more effective than Mg2+ or Mn2+
Zinc
a member of the zinc-containing medium chain polyol dehydrogenase family
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCl
-
at 40°C, half-life in 0.5 M KCl is 86 h for wild-type, and 114 h for mutant D172K/D216K/D344K, 95 h for mutant D172K, 117 h for mutant D216K, 114 h for mutant D344K. At 25°C, half-life in 0.5 M KCl is 506 h for wild-type, and 613 h for mutant D172K/D216K/D344K, 630 h for mutant D172K, 660 h for mutant D216K, 537 h for mutant D344K
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
-
triple mutant D172K/D216K/D344K shows its maximum activity in a buffer with 0.50-0.75 M NaCl while the wild type protein has its maximum activity with 1.5 M NaCl
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.9 - 80
beta-D-glucose
2.8 - 12.9
D-glucose
0.035 - 0.4
NAD(P)+
0.4 - 2.7
NAD+
0.024 - 2.6
NADP+
1.8 - 80
D-glucose
0.4 - 2.7
NAD+
0.035 - 2.6
NADP+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00041 - 0.9
D-glucose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000008 - 0.00019
D-glucose
0.000035 - 0.00112
NAD+
0.0001 - 0.015
NADP+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 2
NAD(P)+
1 - 2.1
NAD+
0.09 - 1.3
NADP+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
2 * 53000, SDS-PAGE
89000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 53000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.6 A structure determination of the enzyme using crystals grown under conditions that closely mimic those experienced within the cell of the halophile. The structure is compared with nonhalophilic homologues. Location of bound counterions in the structure. Analysis of protein-solvent interactions to further the understanding of the molecular basis of halophilic adaptation
hanging-drop vapour-diffusion method at 17°C, crystallization of a range of binary and ternary complexes of the wild-type and a D38C mutant protein. For most of the complexes, crystals belonging to space group I222 are obtained using sodium/potassium citrate as a precipitant. For the binary and non-productive ternary complexes with NADPH/Zn, it is necessary to replace the citrate with 2-methyl-2,4-pentanediol. Despite the radical change in conditions, the crystals thus formed are isomorphous
hanging-drop vapour-diffusion method using sodium citrate as the precipitant. Two crystal forms representing the free enzyme and the binary complex with NADP+ grow under these conditions. Crystals of form I diffract to beyond 3.5 A resolution and belong to the hexagonal space group P622, with unit-cell parameters a = b = 89.1, c = 214.6 A, alpha = beta = 90°, gamma = 120°. Crystals of form II diffract to greater than 2.0 A and belong to the orthorhombic space group I222 or I212121, with unit-cell parameters a = 61.8, b = 110.9, c = 151.7 A, alpha = beta = gamma = 90°
the structures of GlcDH in binary complexes with either NADP+/Zn2+ or NADPH/Zn2+, a ternary complex with NADP+/Zn2+/glucose, and a nonproductive ternary complex with NADP+/Zn2+ /gluconolactone are determined from isomorphous crystals, in the presence of zinc (1 mM) and either 5 mM NADP+, by using 1.4-1.6 M sodium citrate as the precipitant (in 100 mM HEPES, pH 7.0, and 2 M NaCl) or 5 mM NADPH, using 67-72% (w/v) 2-methyl-2,4-pentanediol as precipitant (in 100 mM HEPES, pH 7.5, and 2 M NaCl)
hanging-drop vapour diffusion
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D38C
crystallization of a range of binary and ternary complexes of the wild-type and a D38C mutant protein
G206D
G206D/R207I
G206D/R207I/R208N
R207I
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
G206D
less efficient with NADP+ than the wild type, 1.6fold increase in ratio kcat/Km for NAD+
G206D/R207I
no activity with NADP+, highest reaction rate with cofactor NAD+ of all mutants tested
G206D/R207I/R208N
no activity with NADP+
R207I
less efficient with NADP+ than the wild type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
half-life: 56.8 h, in the presence of 3 M NaCl, stability decreases significantly with lower salt concentrations
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for several months
4°C, stable for weeks
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as recombinant protein in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli BL21 (DE3) cells
overexpressed in Escherichia coli
expression as inclusion bodies in Escherichia coli
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bonete, M.J.; Pire, C.; Llorca, F.I.; Camacho, M.L.
Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: Enzyme purification, characterization and N-terminal sequence
FEBS Lett.
383
227-229
1996
Haloferax mediterranei (Q977U7), Haloferax mediterranei, Haloferax mediterranei DSM 1411 (Q977U7)
Manually annotated by BRENDA team
Esclapez, J.; Britton, K.L.; Baker, P.J.; Fisher, M.; Pire, C.; Ferrer, J.; Bonete, M.J.; Rice, D.W.
Crystallization and preliminary X-ray analysis of binary and ternary complexes of Haloferax mediterranei glucose dehydrogenase
Acta Crystallogr. Sect. F
61
743-746
2005
Haloferax mediterranei, Haloferax mediterranei (Q977U7), Haloferax mediterranei DSM 1411 (Q977U7)
Manually annotated by BRENDA team
Esclapez, J.; Pire, C.; Bautista, V.; Martinez-Espinosa, R.M.; Ferrer, J.; Bonete, M.J.
Analysis of acidic surface of Haloferax mediterranei glucose dehydrogenase by site-directed mutagenesis
FEBS Lett.
581
837-842
2007
Haloferax mediterranei
Manually annotated by BRENDA team
Pire, C.; Esclapez, J.; Diaz, S.; Perez-Pomares, F.; Ferrer, J.; Bonete, M.
Alteration of coenzyme specificity in halophilic NAD(P)+ glucose dehydrogenase by site-directed mutagenesis
J. Mol. Catal. B
59
261-265
2009
Haloferax mediterranei, Haloferax mediterranei (Q977U7)
-
Manually annotated by BRENDA team
Baker, P.J.; Britton, K.L.; Fisher, M.; Esclapez, J.; Pire, C.; Bonete, M.J.; Ferrer, J.; Rice, D.W.
Active site dynamics in the zinc-dependent medium chain alcohol dehydrogenase superfamily
Proc. Natl. Acad. Sci. USA
106
779-784
2009
Haloferax mediterranei (Q977U7)
Manually annotated by BRENDA team
Ferrer, J.; Fisher, M.; Burke, J.; Sedelnikova, S.E.; Baker, P.J.; Gilmour, D.J.; Bonete, M.J.; Pire, C.; Esclapez, J.; Rice, D.W.
Crystallization and preliminary X-ray analysis of glucose dehydrogenase from Haloferax mediterranei
Acta Crystallogr. Sect. D
57
1887-1889
2001
Haloferax mediterranei (Q977U7), Haloferax mediterranei DSM 1411 (Q977U7)
Manually annotated by BRENDA team
Britton, K.L.; Baker, P.J.; Fisher, M.; Ruzheinikov, S.; Gilmour, D.J.; Bonete, M.J.; Ferrer, J.; Pire, C.; Esclapez, J.; Rice, D.W.
Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei
Proc. Natl. Acad. Sci. USA
103
4846-4851
2006
Haloferax mediterranei (Q977U7), Haloferax mediterranei DSM 1411 (Q977U7)
Manually annotated by BRENDA team