Construction of engineered water-soluble PQQ glucose dehydrogenase with improved substrate specificity

Sode, K.; Igarashi, S.; Morimoto, A.; Yoshida, H.; Biocatal. Biotransform. 20, 405-412 (2002)

 show all sequences of 1.1.5.2

Data extracted from this reference:

Application
Application Commentary Organism
biotechnology bioengineering of water-soluble isozyme PQQGDH-B production at industrial level Escherichia coli
Cloned(Commentary)
Commentary Organism
expression of wild-type and mutant isozymes PQQGDH-B Escherichia coli
Engineering
Amino acid exchange Commentary Organism
D448N site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
D456N site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
D457N site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N452D site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N452H site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N452I site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N452K site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N452T site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows narrowed substrate specificity, but unaltered catalytic efficiency, thermal stability, and EDTA tolerance compared to the wild-type isozyme PQQGDH-B Escherichia coli
N462D site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N462H site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N462K site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N462Y site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
KM Value [mM]
KM Value [mM] KM Value Maximum [mM] Substrate Commentary Organism Structure
2.7
-
 D-galactose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
3.7
-
 D-galactose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
5.3
-
 D-galactose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
12.3
-
 D-glucose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
12.5
-
 D-glucose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
16
-
 maltose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
18
-
 lactose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
18.9
-
 lactose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
25
-
 D-glucose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
26
-
 maltose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
27.6
-
 3-O-methyl-D-glucose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
28.7
-
 3-O-methyl-D-glucose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
28.8
-
 3-O-methyl-D-glucose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
32.5
-
 allose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
33.6
-
 lactose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
35.5
-
 allose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
38.7
-
 allose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
46.5
-
 maltose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
Localization
Localization Commentary Organism GeneOntology No. Textmining
soluble isoyzme PQQGDH-B Escherichia coli
-
-
Metals/Ions
Metals/Ions Commentary Organism Structure
Ca2+ required Escherichia coli
Organism
Organism Primary Accession No. (UniProt) Commentary Textmining
Escherichia coli
-
 isozyme PQQGDH-B
-
Reaction
Reaction Commentary Organism
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol active site structure contains a loop 6BC region which does not directly interact with the substrates Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Commentary Organism
additional information
-
-
 Escherichia coli
Substrates and Products (Substrate)
Substrates Commentary Substrates Literature (Substrates) Organism Products Commentary (Products) Literature (Products) Organism (Products) Reversibility
3-O-methyl-D-glucose + ubiquinone
-
 654398 Escherichia coli 3-O-methyl-D-glucono-1,5-lactone + ubiquinol
-
-
-
 ?
allose + ubiquinone
-
 654398 Escherichia coli ? + ubiquinol
-
-
-
 ?
D-galactose + ubiquinone low activity, recombinant wild-type and mutant isozymes PQQGDH-B 654398 Escherichia coli D-galactono-1,5-lactone + ubiquinol
-
-
-
 ?
D-glucose + ubiquinone best substrate, recombinant wild-type and mutant isozymes PQQGDH-B 654398 Escherichia coli D-glucono-1,5-lactone + ubiquinol
-
-
-
 ?
lactose + ubiquinone
-
 654398 Escherichia coli ? + ubiquinol
-
-
-
 ?
maltose + ubiquinone
-
 654398 Escherichia coli ? + ubiquinol
-
-
-
 ?
More substrate specificities of wild-type and mutant isozyme PQQGDH-B, overview 654398 Escherichia coli ?
-
-
-
-
Subunits
Subunits Commentary Organism
More 3D-model prediction for wild-type and mutant isozyme PQQGDH-B Escherichia coli
Temperature Optimum [°C]
Temperature Optimum [°C] Temperature Optimum Maximum [°C] Commentary Organism
25
-
 assay at Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Commentary Organism Structure
69
-
 D-galactose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
72
-
 D-galactose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
232
-
 D-galactose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
574
-
 lactose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
588
-
 maltose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
949
-
 allose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1002
-
 maltose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1035
-
 allose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1038
-
 lactose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1064
-
 3-O-methyl-D-glucose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1253
-
 3-O-methyl-D-glucose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1399
-
 D-glucose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1659
-
 lactose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1791
-
 D-glucose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1930
-
 maltose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
2509
-
 allose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
3011
-
 3-O-methyl-D-glucose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
3860
-
 D-glucose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
pH Optimum
pH Optimum Minimum pH Optimum Maximum Commentary Organism
7
-
 assay at Escherichia coli
Cofactor
Cofactor Commentary Organism Structure
pyrroloquinoline quinone prosthetic group Escherichia coli
Application (protein specific)
Application Commentary Organism
biotechnology bioengineering of water-soluble isozyme PQQGDH-B production at industrial level Escherichia coli
Cloned(Commentary) (protein specific)
Commentary Organism
expression of wild-type and mutant isozymes PQQGDH-B Escherichia coli
Cofactor (protein specific)
Cofactor Commentary Organism Structure
pyrroloquinoline quinone prosthetic group Escherichia coli
Engineering (protein specific)
Amino acid exchange Commentary Organism
D448N site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
D456N site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
D457N site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N452D site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N452H site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N452I site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N452K site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N452T site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows narrowed substrate specificity, but unaltered catalytic efficiency, thermal stability, and EDTA tolerance compared to the wild-type isozyme PQQGDH-B Escherichia coli
N462D site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N462H site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N462K site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
N462Y site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM] KM Value Maximum [mM] Substrate Commentary Organism Structure
2.7
-
 D-galactose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
3.7
-
 D-galactose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
5.3
-
 D-galactose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
12.3
-
 D-glucose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
12.5
-
 D-glucose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
16
-
 maltose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
18
-
 lactose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
18.9
-
 lactose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
25
-
 D-glucose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
26
-
 maltose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
27.6
-
 3-O-methyl-D-glucose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
28.7
-
 3-O-methyl-D-glucose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
28.8
-
 3-O-methyl-D-glucose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
32.5
-
 allose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
33.6
-
 lactose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
35.5
-
 allose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
38.7
-
 allose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
46.5
-
 maltose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
Localization (protein specific)
Localization Commentary Organism GeneOntology No. Textmining
soluble isoyzme PQQGDH-B Escherichia coli
-
-
Metals/Ions (protein specific)
Metals/Ions Commentary Organism Structure
Ca2+ required Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Commentary Organism
additional information
-
-
 Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates Commentary Substrates Literature (Substrates) Organism Products Commentary (Products) Literature (Products) Organism (Products) Reversibility
3-O-methyl-D-glucose + ubiquinone
-
 654398 Escherichia coli 3-O-methyl-D-glucono-1,5-lactone + ubiquinol
-
-
-
 ?
allose + ubiquinone
-
 654398 Escherichia coli ? + ubiquinol
-
-
-
 ?
D-galactose + ubiquinone low activity, recombinant wild-type and mutant isozymes PQQGDH-B 654398 Escherichia coli D-galactono-1,5-lactone + ubiquinol
-
-
-
 ?
D-glucose + ubiquinone best substrate, recombinant wild-type and mutant isozymes PQQGDH-B 654398 Escherichia coli D-glucono-1,5-lactone + ubiquinol
-
-
-
 ?
lactose + ubiquinone
-
 654398 Escherichia coli ? + ubiquinol
-
-
-
 ?
maltose + ubiquinone
-
 654398 Escherichia coli ? + ubiquinol
-
-
-
 ?
More substrate specificities of wild-type and mutant isozyme PQQGDH-B, overview 654398 Escherichia coli ?
-
-
-
-
Subunits (protein specific)
Subunits Commentary Organism
More 3D-model prediction for wild-type and mutant isozyme PQQGDH-B Escherichia coli
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C] Temperature Optimum Maximum [°C] Commentary Organism
25
-
 assay at Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Commentary Organism Structure
69
-
 D-galactose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
72
-
 D-galactose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
232
-
 D-galactose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
574
-
 lactose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
588
-
 maltose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
949
-
 allose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1002
-
 maltose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1035
-
 allose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1038
-
 lactose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1064
-
 3-O-methyl-D-glucose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1253
-
 3-O-methyl-D-glucose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1399
-
 D-glucose N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1659
-
 lactose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1791
-
 D-glucose N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
1930
-
 maltose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
2509
-
 allose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
3011
-
 3-O-methyl-D-glucose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
3860
-
 D-glucose wild-type isozyme PQQGDH-B, pH 7.0, 25°C Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum pH Optimum Maximum Commentary Organism
7
-
 assay at Escherichia coli

See also following references to EC number 1.1.5.2 (sorted by year of publication):
No.1st authorPub
Med		titleorganimsjournalvolumepagesyearActivating CompoundApplicationCloned(Commentary)Crystallization (Commentary)EngineeringGeneral StabilityInhibitorsKM Value [mM]LocalizationMetals/IonsMolecular Weight [Da]Natural Substrates/ Products (Substrates)Organic Solvent StabilityOrganismOxidation StabilityPosttranslational ModificationPurification (Commentary)ReactionRenatured (Commentary)Source TissueSpecific Activity [micromol/min/mg]Storage StabilitySubstrates and Products (Substrate)SubunitsTemperature Optimum [°C]Temperature Range [°C]Temperature Stability [°C]Turnover Number [1/s]pH OptimumpH RangepH StabilityCofactorKi Value [mM]pI ValueIC50 ValueActivating Compound (protein specific)Application (protein specific)Cloned(Commentary) (protein specific)Cofactor (protein specific)Crystallization (Commentary) (protein specific)Engineering (protein specific)General Stability (protein specific)IC50 Value (protein specific)Inhibitors (protein specific)Ki Value [mM] (protein specific)KM Value [mM] (protein specific)Localization (protein specific)Metals/Ions (protein specific)Molecular Weight [Da] (protein specific)Natural Substrates/ Products (Substrates) (protein specific)Organic Solvent Stability (protein specific)Oxidation Stability (protein specific)Posttranslational Modification (protein specific)Purification (Commentary) (protein specific)Renatured (Commentary) (protein specific)Source Tissue (protein specific)Specific Activity [micromol/min/mg] (protein specific)Storage Stability (protein specific)Substrates and Products (Substrate) (protein specific)Subunits (protein specific)Temperature Optimum [°C] (protein specific)Temperature Range [°C] (protein specific)Temperature Stability [°C] (protein specific)Turnover Number [1/s] (protein specific)pH Optimum (protein specific)pH Range (protein specific)pH Stability (protein specific)pI Value (protein specific)ExpressionGeneral InformationGeneral Information (protein specific)Expression (protein specific)KCat/KM [mM/s]KCat/KM [mM/s] (protein specific)
713001HoferCharacterization and engineeri ...Sorangium cellulosumMol. Biotechnol.47253-2612011--1-7--8-12--5--1-1---9-111811-1-----11-7----8-12----11---9-111811------88
711018SakurabaCatalytic properties and cryst ...Pyrobaculum aerophilumArch. Biochem. Biophys.50281-882010--11--16--21-4--1---1-1011-151-11-----111---1-6--21---1--1-1011-151-1-----99
712800SashidharHighly conserved Asp-204 and G ...Escherichia coliJ. Mol. Microbiol. Biotechnol.18109-1192010--1-16---1-11-2--1-----2--------1-----11-16-----1-11---1----2---------------
687745MustafaAmino acid residues interactin ...Escherichia coli, Escherichia coli YU423J. Biol. Chem.28322215-222212008--1-5---2----5--1-----2--------1-----11-5-----2------1----2----------11---
701173BuchMetabolic channeling of glucos ...Pseudomonas aeruginosa, Pseudomonas aeruginosa P4, Pseudomonas fluorescensRes. Microbiol.159635-6422008-------------3------3-2---------------------------------3-2---------------
702498MustafaFunction of a bound ubiquinone ...Escherichia coliBiofactors3223-292008----1---3----4-----------------1------1-1-----3----------------------11---
703434Laurinavicius-Behavior of PQQ glucose dehydr ...Erwinia sp.Electroanalysis201391-13952008-4-----------1--4--------------4----4-4--------------4--------------------
706361Bernardelli-Symbiotic phenotype of a membr ...Sinorhizobium melilotiPlant Soil313217-2252008-------------1------------------------------------------------------1111--
685698LauImproved specificity of reagen ...Acinetobacter calcoaceticusBiosens. Bioelectron.223014-30202007--1------1---3--------2---1----1-----11--------1----------2---1-----------
686370Ivnitski-Direct bioelectrocatalysis of ...Acinetobacter sp.Electroanalysis191562-15682007-----1-------1--------1--------1------1--1----------------1---------------
689259IkebukuroConstruction of target molecul ...Acinetobacter calcoaceticusNucleic Acids Symp. Ser.51401-40220072-----1------2---------------------2-------1------------------------------
689260IkebukuroSelection of DNA aptamers that ...Acinetobacter calcoaceticusNucleic Acids Symp. Ser.51403-4042007-1----1--11--2--------11-------1----1-1----1---11---------11--------------
671165Sanchez-WeatherbyCrystallization of quinoprotei ...Acinetobacter calcoaceticus, Escherichia coli, Streptomyces coelicolorActa Crystallogr.Sect.F62518-5212006---263------3-6--3-----3--------3------3263--------3---3----3---------------
671548HamamatsuModified substrate specificity ...Acinetobacter calcoaceticusAppl. Microbiol. Biotechnol.73607-6172006--1-23----111-2--1--1--41----1--1-----11-23------111---1-1--41----1---------
674663SouthallSoluble aldose sugar dehydroge ...Escherichia coliJ. Biol. Chem.28130650-306592006--11---3-111-4--1-----2-1--31--1-----111-----3-111---1----2-1--31---------
655127TanakaIncreasing stability of water- ...Acinetobacter calcoaceticusBMC Biochem.612005-11-3--311-1-3------4-221-1-1--1----111-3----311-1------4-221-1-1---------
654449OkudaPQQ glucose dehydrogenase with ...Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD79.41Biochem. Biophys. Res. Commun.314793-7972004-21-24--311-1-6--1-----41---11--1-1--211-24----311-1---1----41---11--1------
654936Lapenaite-Some quinone derivatives as re ...Erwinia sp., Erwinia sp. 34-1Biologia (Bratisl.)120-222004-------1-----2--------7--------1------1------1------------7---------------
654947IgarashiEngineering PQQ glucose dehydr ...Acinetobacter calcoaceticusBiomol. Eng.2181-892004-11-69--2811---2------1-12---1291--1----111-69----2811--------1-12---1291---------
655791ReddyMechanism of glucose oxidation ...Acinetobacter calcoaceticusJ. Am. Chem. Soc.1262431-24382004--------21---2---1----11-------1-1----1-------21----------11-------1------
655929IgarashiConstruction and characterizat ...Acinetobacter calcoaceticusJ. Biochem. Biophys. Methods61331-3382004--1-1--1211---1----24-3-71---21--1-----11-1----1211------24-3-71---21---------
654780IvanovaComparative kinetic study of D ...Erwinia sp.Biochemistry68407-4152003-------1-----3---4--4-1--------5------5------1----------4-1---------------
654863OubrieStructure and mechanism of sol ...Acinetobacter calcoaceticusBiochim. Biophys. Acta1647143-1512003---24----1--1-2---1----21-------1------124------1--1--------21--------------
654864YamadaEscherichia coli PQQ-containin ...Acinetobacter calcoaceticus, Escherichia coliBiochim. Biophys. Acta1647185-1922003--------42-4-4---2----62-------2------2-------42-4--------62--------------
654865JamesThe metal ion in the active si ...Escherichia coliBiochim. Biophys. Acta1647200-2052003----3-4924-1-3---1----10-1-8-1--11-----1-3--41924-1--------10-1-8-1---------
654938Laurinavicius-Comparative characterization o ...Acinetobacter calcoaceticus, Acinetobacter calcoaceticus L.M.D., Erwinia sp., Erwinia sp. 34-1Biologia (Bratisl.)231-342003-5---5-652---4------5-14-----6--2----5-2--5---652--------5-14-----6---------
655097KohSurface charge engineering of ...Acinetobacter calcoaceticusBiotechnol. Lett.251695-17012003-11-1--18-1---1--1-----7-1-1-1--1----111-1----18-1-----1----7-1-1-1---------
655101YoshidaImproved substrate specificity ...Escherichia coliBiotechnol. Lett.25301-3052003--1-1---11---2------1-9-----1--1-----11-1-----11--------1-9-----1---------
656767IgarashiStabilization of quaternary st ...Escherichia coliMol. Biotechnol.2497-1042003--1-1---1----2---------1--1----------1--1-----1------------1--1-----------
654398Sode-Construction of engineered wat ...Escherichia coliBiocatal. Biotransform.20405-4122002-11-12--1811---1---1--1-711--181--1----111-12----1811--------1-711--181---------
655363Yoshida-Secretion of water soluble pyr ...Acinetobacter calcoaceticusEnzyme Microb. Technol.30312-3182002-11---1-3----1-241---1-111--1-1--1----111----1--3-----241--1-111--1-1---------
639206BernardelliPeriplasmic PQQ-dependent gluc ...Rhizobium tropici, Sinorhizobium melilotiCurr. Microbiol.42310-3152001--------3----2-----19-----------3------3-------3--------19------------------
639207EliasC-terminal periplasmic domain ...Escherichia coliJ. Biol. Chem.27648356-483612001-------62--1-3--1---1-3----------------------62--1---1--1-3---------------
639208EliasFunctions of amino acid residu ...Escherichia coliJ. Biol. Chem.2757321-73262000----7--17-----4--------2--------1------1-7----17------------2---------------
639214HeubergerA spectroscopic assay for the ...Acinetobacter calcoaceticusEur. J. Biochem.267228-2342000-1-----31----1--------3--------1----1-1------31-----------3---------------
639215Iswantini-Kinetics and thermodynamics of ...Escherichia coliBiochem. J.350917-9232000--------12---1--------4--------1------1-------12----------4---------------
639218SodeIncreasing the thermal stabili ...Acinetobacter calcoaceticusEnzyme Microb. Technol.26491-4962000-1--7--------1----------------------1---7---------------------------------
639204OubrieThe 1.7 A crystal structure of ...Acinetobacter calcoaceticusJ. Mol. Biol.289319-3331999---24---------1-------------------------24----------------------------------
639205YoshidaEngineering a chimeric pyrrolo ...Acinetobacter calcoaceticus, Escherichia coliProtein Eng.1263-701999----25-1------6------------1-------------25--1------------------1-----------
639212Sode-Construction and characterizat ...Escherichia coliBiotechnol. Lett.21707-7101999----1--2-----1--1-----1---1----1------1-1----2-------1----1---1-----------
639213Cozier-Characterization of the membra ...Escherichia coliBiochem. J.340639-6471999----1--181----1--1-----15--------1------1-1----181------1----15---------------
639216IgarashiConstruction and characterizat ...Acinetobacter calcoaceticusBiochem. Biophys. Res. Commun.264820-8241999----10--27-----1--------10---118------------10----27------------10---118----------
639220OubrieActive-site structure of the s ...Acinetobacter calcoaceticusProc. Natl. Acad. Sci. USA9611787-117911999-------21-1---3------1-11--------1------1------21-1--------1-11---------------
639209OlsthoornOn the mechanism and specifici ...Acinetobacter calcoaceticusBiochemistry3713854-138611998-------------1--------1----11-----------------------------1----11---------
639210YamadaMutant isolation of the Escher ...Escherichia coliJ. Biol. Chem.27322021-220271998--1-8--10-1---3--1-----1--------1-----11-8----10-1-----1----1---------------
639219DewantiReconstitution of membrane.int ...Acinetobacter calcoaceticusBiochemistry376810-68181998---24--1------4--------1--------1------124---1--------------1---------------
639217OlsthoornProduction, characterization, ...Acinetobacter calcoaceticusArch. Biochem. Biophys.33642-481996--1-----11---4--1---1----------1-----11-------11-----1--1-----------------
639211YamadaTopological analysis of quinop ...Escherichia coliJ. Biol. Chem.26812812-128171993--------1--1-4------1-2--------1------1-------1--1------1-2---------------
639192Cleton-JansenCloning, mapping, and sequenci ...Escherichia coliJ. Bacteriol.1726308-63151990--1----------4-----------------1-----11-----------------------------------
639193HommesThe separate roles of PQQ and ...Klebsiella pneumoniaeArch. Microbiol.151257-2601989-----------1-1--------1--------1------1----------1--------1---------------
639196MatsushitaReactivity with ubiquinone of ...Gluconobacter oxydansJ. Biochem.105633-6371989--------1--2-4--1---1-4--------1------1-------1--2---1--1-4---------------
639197MatsushitaQuinoprotein D-glucose dehydro ...Acinetobacter calcoaceticusBiochemistry286276-62801989-------52----3--1---1-22----21-1------1------52------1--1-22----21--------
639198GeigerReversible thermal inactivatio ...Acinetobacter calcoaceticusBiochem. J.261415-4211989---------3---3--------1---2--------------------3----------1---2-----------
639199MatsushitaQuinoprotein D-glucose dehydro ...Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41Antonie Leeuwenhoek5663-721989-------112--1-2--1---2-62----21---------------112--1---1--2-62----21--------
639194Van Schie-PQQ-dependent production of gl ...Acinetobacter lwoffii, Agrobacterium tumefaciens, Azotobacter vinelandii, Rhizobium leguminosarumJ. Gen. Microbiol.133867-8751987---------10---4-----------------7------7--------10--------------------------
639195Dokter-The in vivo and in vitro subst ...Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41, Pseudomonas sp.FEMS Microbiol. Lett.43195-2001987-------7-----3--1-----8----------------------7-------1----8---------------
639190Geiger-Crystalline quinoprotein gluco ...Acinetobacter calcoaceticusBiochemistry256043-60481986---24--22--1--1--11--1-11-------1------124---2-2--1----1--1-11--------------
639191DokterPurification and characterizat ...Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41, Enterobacter aerogenes, Escherichia coli, Gluconobacter oxydans, Pseudomonas sp.Biochem. J.239163-1671986-------2--1--13--11--1-161----2--5------5------2--1----1--1-161----2---------
639200Matsushita-Immunological evidence for two ...Acetobacter aceti, Acinetobacter calcoaceticus, Escherichia coli, Gluconobacter oxydans, Klebsiella pneumoniae, Pseudomonas aeruginosaFEMS Microbiol. Lett.37141-1441986--------8----6-----------------6------6-------8---------------------------
639189DuineDetection and determination of ...Enterobacter aerogenes, Pseudomonas aeruginosaAnal. Biochem.133239-2431983-2-----------4-----------------2----2-2-----------------------------------
639201Matsushita-D-Glucose dehydrogenase from P ...Pseudomonas fluorescensMethods Enzymol.89149-1541982------292-1--1--1---1-111-------1------1----2-92-1----1--1-111--------------
639202Matsushita-Membrane-bound, electron trans ...Pseudomonas fluorescensAgric. Biol. Chem.461007-10111982------132----1--1-----6--------1------1----1-32------1----6---------------
639203Ameyama-L-Glucose dehydrogenase of Glu ...Gluconobacter oxydansAgric. Biol. Chem.45851-8611981----------1--1--1---1-9-----2111------1---------1----1--1-9-----211-------
639188DuineGlucose dehydrogenase from Aci ...Acinetobacter calcoaceticusFEBS Lett.108443-4461979-------------1--1--------------1------1--------------1--------------------