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D-glucose + acceptor
D-glucono-1,5-lactone + reduced acceptor
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
maltose + acceptor
maltono-1,5-lactone + reduced acceptor
-
-
-
?
2-deoxy-D-glucose + oxidized 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
3-O-methyl-D-glucose + oxidized 2,6-dichlorophenolindophenol
3-O-methyl-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
cellobiose + N-methylphenazonium methylsulfate
cellobiono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
-
-
-
?
cellobiose + oxidized 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-allose + N-methylphenazonium methylsulfate
D-allono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
-
-
-
?
D-allose + oxidized 2,6-dichlorophenolindophenol
D-allono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-fucose + oxidized 2,6-dichlorophenolindophenol
D-fucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-galactose + N-methylphenazonium methylsulfate
D-galactono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
30% activity compared to D-glucose
-
-
?
D-galactose + oxidized 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-galactose + oxidized N-methylphenazonium methyl sulfate
D-galactono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-glucose + acceptor
D-glucono-1,5-lactone + reduced acceptor
-
-
-
-
?
D-glucose + dimethyl((6-methyl-7-((4-nitrosophenyl)amino)-1H-imidazo[1,2-b]pyrazol-1-yl)methyl)phosphine oxide
D-glucono-1,5-lactone + reduced dimethyl((6-methyl-7-((4-nitrosophenyl)amino)-1H-imidazo[1,2-b]pyrazol-1-yl)methyl)phosphine oxide
-
-
-
?
D-glucose + N-methylphenazonium methylsulfate
D-glucono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
100% activity
-
-
?
D-glucose + osmium polymer
D-glucono-1,5-lactone + reduced osmium polymer
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol-indophenol
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-glucose + oxidized N-methylphenazonium methyl sulfate
D-glucono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-lyxose + N-methylphenazonium methylsulfate
D-lyxono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
-
-
-
?
D-lyxose + oxidized 2,6-dichlorophenolindophenol
D-lyxono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-mannose + N-methylphenazonium methylsulfate
D-mannono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
-
-
-
?
D-mannose + oxidized 2,6-dichlorophenolindophenol
D-mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-ribose + N-methylphenazonium methylsulfate
D-ribono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
5% activity compared to D-glucose
-
-
?
D-ribose + oxidized 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-xylose + N-methylphenazonium methylsulfate
D-xylono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
14% activity compared to D-glucose
-
-
?
D-xylose + oxidized 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-xylose + oxidized N-methylphenazonium methyl sulfate
D-xylono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
L-arabinose + N-methylphenazonium methylsulfate
L-arabinono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
-
-
-
?
L-arabinose + oxidized 2,6-dichlorophenolindophenol
L-arabinono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
lactose + 1-(N,N-dimethylamine)-4-(4-morpholine)benzene
lactono-1,5-lactone + reduced 1-(N,N-dimethylamine)-4-(4-morpholine)benzene
-
-
-
?
lactose + N,N'-dimethyl-4,4'-azopyridinium methyl sulfate
lactono-1,5-lactone + reduced N,N'-dimethyl-4,4'-azopyridinium methyl sulfate
-
-
-
?
lactose + N-methylphenazonium methylsulfate
lactono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
4% activity compared to D-glucose
-
-
?
lactose + oxidized 2,6-dichlorophenol-indophenol
? + reduced 2,6-dichlorophenol-indophenol
-
-
-
-
?
lactose + oxidized 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
lactose + oxidized 2,6-dichlorophenolindophenol
lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
lactose + oxidized N-methylphenazonium methyl sulfate
4-O-beta-D-galactopyranosyl-D-glucono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
maltose + N-methylphenazonium methylsulfate
maltono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
12% activity compared to D-glucose
-
-
?
maltose + oxidized 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
maltose + oxidized 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
melibiose + N-methylphenazonium methylsulfate
melibiono-1,5-lactone + reduced N-methylphenazonium methylsulfate
-
5% activity compared to D-glucose
-
-
?
melibiose + oxidized 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
additional information
?
-
2-deoxy-D-glucose + oxidized 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
2-deoxy-D-glucose + oxidized 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
4% of the activity with D-glucose
-
-
?
3-O-methyl-D-glucose + oxidized 2,6-dichlorophenolindophenol
3-O-methyl-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
3-O-methyl-D-glucose + oxidized 2,6-dichlorophenolindophenol
3-O-methyl-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
81% of the activity with D-glucose
-
-
?
D-allose + oxidized 2,6-dichlorophenolindophenol
D-allono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-allose + oxidized 2,6-dichlorophenolindophenol
D-allono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
47% of the activity with D-glucose
-
-
?
D-galactose + oxidized 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-galactose + oxidized 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
11% of the activity with D-glucose
-
-
?
D-galactose + oxidized 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 13% activity compared to D-glucose
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
100% activity
-
-
?
D-mannose + oxidized 2,6-dichlorophenolindophenol
D-mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-mannose + oxidized 2,6-dichlorophenolindophenol
D-mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
13% of the activity with D-glucose
-
-
?
D-mannose + oxidized 2,6-dichlorophenolindophenol
D-mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 11% activity compared to D-glucose
-
-
?
D-xylose + oxidized 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-xylose + oxidized 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
7% of the activity with D-glucose
-
-
?
D-xylose + oxidized 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 9% activity compared to D-glucose
-
-
?
lactose + oxidized 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
lactose + oxidized 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
61% of the activity with D-glucose
-
-
?
lactose + oxidized 2,6-dichlorophenolindophenol
lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
lactose + oxidized 2,6-dichlorophenolindophenol
lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
61% of the activity with D-glucose
-
-
?
lactose + oxidized 2,6-dichlorophenolindophenol
lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 50% activity compared to D-glucose
-
-
?
maltose + oxidized 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
maltose + oxidized 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
61% of the activity with D-glucose
-
-
?
maltose + oxidized 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
maltose + oxidized 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
61% of the activity with D-glucose
-
-
?
maltose + oxidized 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 70% activity compared to D-glucose
-
-
?
additional information
?
-
-
kinetic mechanism of sGDH consists of (a) step(s) in which a fluorescing intermediate is formed, and a subsequent, irreversible step, determining the overall rate of the reductive half-reaction. The pH optimum determined for glucose oxidation appears to be 7.0, implying that reoxidation of sGDHred is rate-limiting with those electron acceptors displaying a different value under steady-state conditions.
-
-
?
additional information
?
-
-
mechanism comprises general base-catalyzed hydride transfer
-
-
?
additional information
?
-
-
the sequential steps in the mechanism of sGDH must be reversible substrate binding, direct transfer of a hydride ion (reversible or irreversible) from the C1 position of the beta-anomer of glucose to the C5 of PQQ, irreversible, rate-determining tautomerization of the fluorescing, C5-reduced PQQ to PQQH2 and release (or earlier) of the product, D-glucono-delta-lactone, and oxidation of PQQH2 by an electron acceptor. The PQQ-activating Ca2+ greatly facilitates the reactions occurring in the second step. His144 may also play a role in this by acting as a general base catalyst, initiating hydride transfer by abstracting a proton from the anomeric OH group of glucose
-
-
?
additional information
?
-
-
almost no activity with D-fructose
-
-
?
additional information
?
-
-
no activity with D-glucosamine, L-altrose, L-lyxose, L-talose, L-mannose, D-altrose, D-arabinose, D-talose, L-xylose, L-glucose, L-galactose, L-allose, sucrose, trehalose, and raffinose
-
-
?
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Ca2+
the enzyme binds three calcium ions per monomer, two of which are located in the dimer interface, crystallization data
Cd2+
-
or Ca2+, Sr2+, or Mn2+, required for binding of cofactor PQQ in soluble isoform sGDH. Mg2+, or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH
Mg2+
-
or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH. With Mg2+, 115% of the activity with Ca2+
Mn2+
-
or Ca2+, Sr2+, or Cd2+, required for binding of cofactor PQQ in soluble isoform sGDH. Mg2+, or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH
Ca2+
-
or Cd2+, Sr2+, or Mn2+, required for binding of cofactor PQQ in soluble isoform sGDH, 100% activity with Ca2+. Mg2+, or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH. 100% activity with Ca2+
Ca2+
-
study on interconversions of different enzyme species from monomeric apoenzyme to fully reconstituted enzyme, e.g. consisting of dimer with one firmly bound Ca2+ ion, dimer with two PQQ and two extra Ca2+ ions, or substitutes for Ca2+. Dimers consisting of two monomers with one firmly bound Ca2+ ion and dimers consisting of two monomers with one firmly bound Ca2+ ion and with two PQQ and two extra Ca2+ ions are very stable enzyme species regarding monomerization and inactivation by chelator, respectively, the bound Ca2+ being locked up in such a way that it is not accessible to chelator. The two Ca2+ ions required for activation of dimers consisting of two monomers with one firmly bound Ca2+ ion and with two PQQ, are even more firmly bound than the two required for dimerization of monomers and anchoring of PQQ
Ca2+
-
substituting the Ca2+ involved in activation of pyrroloquinoline quinone in soluble GDH by Sr2+ affects the cooperativity effect but not the two turnover rates of the hybrid enzyme for glucose
Ca2+
calcium is essential for dimerization and PQQ binding
Ca2+
reconstitution mechanism of the enzyme (sGDH) with its two cofactors, i.e., pyrroloquinoline quinone (PQQ) and Ca2+: pyrroloquinoline quinone first binds to apo-sGDH, it strongly impedes the access of Ca2+ to its enclosed position at the bottom of the enzyme binding site, thereby greatly slowing down the reconstitution rate of sGDH. The slow calcium insertion may purposely be accelerated by providing more flexibility to the Ca2+ binding loop through the specific mutation of the calcium-coordinating P248 proline residue, reducing thus the kinetic barrier to calcium ion insertion
Ca2+
the holoenzyme is reconstituted by incubating the apoenzyme in 5 mM MES buffer at pH 6.5 with 1 mM CaCl2 and 0.060 mM pyrroloquinoline quinone for 3 h at room temperature in the dark
Sr2+
-
or Ca2+, Cd2+, or Mn2+, required for binding of cofactor PQQ in soluble isoform sGDH, with Sr2+, 67% of the activity with Ca2+. Mg2+, or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH, with Sr2+, 70% of the activity with Ca2+
Sr2+
-
substituting the Ca2+ involved in activation of pyrroloquinoline quinone in soluble GDH by Sr2+ affects the cooperativity effect but not the two turnover rates of the hybrid enzyme for glucose
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D275E
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 6%, D-mannose 11%, D-allose 44%, 3-O-methyl-D-glucose 45%, D-galactose 12%, D-xylose 7%, D-lactose 52%, D-maltose 44%, respectively
D276E
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 13%, D-mannose 19%, D-allose 54%, 3-O-methyl-D-glucose 57%, D-galactose 26%, D-xylose 20%, D-lactose 75%, D-maltose 66%, respectively
D340F/Y418F
-
increase in temperature stability
D340F/Y418I
-
increase in temperature stability
D448N
-
substrate specificity: D-glucose 100% activity, 3-O-methyl-D-glucose 72%, D-allose 39%, D-galactose 14%, D-maltose 36%, D-lactose 48%, respectively
D456N
-
substrate specificity: D-glucose 100% activity, 3-O-methyl-D-glucose 78%, D-allose 43%, D-galactose 16%, D-maltose 41%, D-lactose 59%, respectively
DD457N
-
substrate specificity: D-glucose 100% activity, 3-O-methyl-D-glucose 80%, D-allose 46%, D-galactose 11%, D-maltose 32%, D-lactose 43%, respectively
E277A
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 11%, D-mannose 33%, D-allose 142%, 3-O-methyl-D-glucose 91%, D-galactose 46%, D-xylose 23%, D-lactose 83%, D-maltose 39%, respectively
E277D
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 9%, D-mannose 19%, D-allose 68%, 3-O-methyl-D-glucose 58%, D-galactose 21%, D-xylose 15%, D-lactose 87%, D-maltose 73%, respectively
E277G
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 15%, D-mannose 38%, D-allose 189%, 3-O-methyl-D-glucose 113%, D-galactose 59%, D-xylose 28%, D-lactose 100%, D-maltose 52%, respectively
E277H
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 3%, D-mannose 11%, D-allose 67%, 3-O-methyl-D-glucose 45%, D-galactose 12%, D-xylose 9%, D-lactose 57%, D-maltose 39%, respectively
E277K
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 7%, D-mannose 18%, D-allose 116%, 3-O-methyl-D-glucose 84%, D-galactose 28%, D-xylose 18%, D-lactose 79%, D-maltose 74%, respectively
E277N
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 8%, D-mannose 29%, D-allose 148%, 3-O-methyl-D-glucose 91%, D-galactose 43%, D-xylose 18%, D-lactose 86%, D-maltose 59%, respectively
E277Q
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 10%, D-mannose 31%, D-allose 134%, 3-O-methyl-D-glucose 80%, D-galactose 35%, D-xylose 25%, D-lactose 68%, D-maltose 54%, respectively
E277V
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 8%, D-mannose 29%, D-allose 150%, 3-O-methyl-D-glucose 101%, D-galactose 25%, D-xylose 19%, D-lactose 114%, D-maltose 65%, respectively
I278F
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 4%, D-mannose 14%, D-allose 54%, 3-O-methyl-D-glucose 47%, D-galactose 15%, D-xylose 12%, D-lactose 64%, D-maltose 49%, respectively
N279H
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 2%, D-mannose 6%, D-allose 49%, 3-O-methyl-D-glucose 50%, D-galactose 13%, D-xylose 8%, D-lactose 64%, D-maltose 61%, respectively
N452T
-
substrate specificity: D-glucose 100% activity, 3-O-methyl-D-glucose 59%, D-allose 33%, D-galactose 5%, D-maltose 30%, D-lactose 31%, respectively
N462H
-
substrate specificity: D-glucose 100% activity, 3-O-methyl-D-glucose 53%, D-allose 32%, D-galactose 2%, D-maltose 25%, D-lactose 31%, respectively
S231C
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 3%, D-mannose 8%, D-allose 46%, 3-O-methyl-D-glucose 76%, D-galactose 14%, D-xylose 8%, D-lactose 69%, D-maltose 69%, respectively
S231D
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 2%, D-mannose 9%, D-allose 38%, 3-O-methyl-D-glucose 71%, D-galactose 12%, D-xylose 8%, D-lactose 54%, D-maltose 38%, respectively
S231H
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 2%, D-mannose 12%, D-allose 57%, 3-O-methyl-D-glucose 86%, D-galactose 17%, D-xylose 7%, D-lactose 56%, D-maltose 38%, respectively
S231K
-
increase in thermal stability. Substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 5%, D-mannose 10%, D-allose 43%, 3-O-methyl-D-glucose 82%, D-galactose 15%, D-xylose 5%, D-lactose 59%, D-maltose 70%, respectively
S231L
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 6%, D-mannose 13%, D-allose 62%, 3-O-methyl-D-glucose 105%, D-galactose 20%, D-xylose 12%, D-lactose 73%, D-maltose 76%, respectively
S231M
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 5%, D-mannose 9%, D-allose 43%, 3-O-methyl-D-glucose 80%, D-galactose 10%, D-xylose 8%, D-lactose 56%, D-maltose 41%, respectively
S231N
-
substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 5%, D-mannose 12%, D-allose 61%, 3-O-methyl-D-glucose 109%, D-galactose 18%, D-xylose 15%, D-lactose 66%, D-maltose 51%, respectively
T416V/T417V
-
increase in temperature stability
N428C
the catalytic efficiency is increased by 47% compared to the wild type enzyme, the mutant shows increased affinity for pyrroloquinoline quinone and is twice more active toward D-glucose and more selective toward maltose than the wild type
N428C
the mutant shows almost twice the maximum catalytic activity compared to the wild type
additional information
-
constructed of heterodimeric PQQGDH-B composed of native wild-type and inactive mutant H168Q subunits. The heterodimeric wild-type/H168Q shows slightly decreased GDH activity and almost identical substrate specificity profile to the wild-type enzyme. The Hill coefficient of the heterodimer is calculated as 1.13, indicating positive cooperativity
additional information
-
expression in Pichia pastoris using the Saccharomyces cerevisiae alpha-factor signal sequence for secretion. The productivity of secreted PQQGDH-B achieves 218 kU/liter, i.e. 43 mg/liter. The secreted PQQGDH-B in Pichia pastoris is glycosylated but shows similar enzymatic properties as compared with those of recombinant PQQGDH-B produced in Escherichia coli
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Oubrie, A.; Rozeboom, H.J.; Kalk, K.H.; Duine, J.A.; Dijkstra, B.W.
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Acinetobacter calcoaceticus
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Igarashi, S.; Ohtera, T.; Yoshida, H.; Witarto, A.B.; Sode, K.
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Acinetobacter calcoaceticus
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Acinetobacter calcoaceticus
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Acinetobacter calcoaceticus
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Oubrie, A.
Structure and mechanism of soluble glucose dehydrogenase and other PQQ-dependent enzymes
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Acinetobacter calcoaceticus
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Acinetobacter calcoaceticus
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Acinetobacter calcoaceticus
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Dewanti, A.R.; Duine, J.A.
Ca2+-assisted, direct hydride transfer, and rate-determining tautomerization of C5-reduced PQQ to PQQH2, in the oxidation of beta -D-glucose by soluble, quinoprotein glucose dehydrogenase
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2000
Acinetobacter calcoaceticus
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Matsushita, K.; Toyama, H.; Ameyama, M.; Adachi, O.; Dewanti, A.; Duine, J.A.
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Kojima, K.; Witarto, A.B.; Sode, K.
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Acinetobacter calcoaceticus
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Olsthoorn, A.J.J.; Otsuki, T.; Duine, J.A.
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Acinetobacter calcoaceticus
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Olsthoorn, A.J.J.; Otsuki, T.; Duine, J.A.
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Schlunegger, M.P.; Gruetter, M.G.; Streiff, M.B.; Olsthoorn, A.J.J.; Duine, J.A.
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Flexer, V.; Durand, F.; Tsujimura, S.; Mano, N.
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Acinetobacter calcoaceticus (P13650), Acinetobacter calcoaceticus
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Durand, F.; Stines-Chaumeil, C.; Flexer, V.; Andre, I.; Mano, N.
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Schubart, I.; Gbel, G.; Lisdat, F.
A pyrroloquinolinequinone-dependent glucose dehydrogenase (PQQ-GDH)-electrode with direct electron transfer based on polyaniline modified carbon nanotubes for biofuel cell application
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Yu, Y.; Wei, P.; Zhu, X.; Huang, L.; Cai, J.; Xu, Z.
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Wired pyrroloquinoline quinone soluble glucose dehydrogenase enzyme electrodes operating at unprecedented low redox potential
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Acinetobacter calcoaceticus
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Stredansky, M.; Monosik, R.; Mastihuba, V.; Sturdik, E.
Monitoring of PQQ-dependent glucose dehydrogenase substrate specificity for its potential use in biocatalysis and bioanalysis
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Acinetobacter calcoaceticus
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Stines-Chaumeil, C.; Mavre, F.; Kauffmann, B.; Mano, N.; Limoges, B.
Mechanism of reconstitution/activation of the soluble PQQ-dependent glucose dehydrogenase from Acinetobacter calcoaceticus a comprehensive study
ACS Omega
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2015-2026
2020
Acinetobacter calcoaceticus (P05465)
brenda
Lisdat, F.
PQQ-GDH - Structure, function and application in bioelectrochemistry
Bioelectrochemistry
134
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Acinetobacter calcoaceticus (P05465)
brenda
Fusco, G.; Goebel, G.; Zanoni, R.; Bracciale, M.P.; Favero, G.; Mazzei, F.; Lisdat, F.
Aqueous polythiophene electrosynthesis A new route to an efficient electrode coupling of PQQ-dependent glucose dehydrogenase for sensing and bioenergetic applications
Biosens. Bioelectron.
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Acinetobacter calcoaceticus (P05465)
brenda
Vaitkute, G.; Bratkovskaja, I.; Casaite, V.; Stankeviciute, J.; Meskys, R.; Tetianec, L.
Electron transfer mediators for PQQ dependent soluble glucose dehydrogenase catalyzed lactose oxidation reaction
Chemija
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2019
Acinetobacter calcoaceticus (P05465)
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brenda