Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41
about
Structural requirements of pyrroloquinoline quinone dependent enzymatic reactionsActive-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complexCloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: evidence for the presence of a second enzymeStructure-guided mutagenesis for the improvement of substrate specificity of Bacillus megaterium glucose 1-dehydrogenase IVCa(2+) stabilizes the semiquinone radical of pyrroloquinoline quinoneCatalytic and molecular properties of the quinohemoprotein tetrahydrofurfuryl alcohol dehydrogenase from Ralstonia eutropha strain BoTwo distinct alcohol dehydrogenases participate in butane metabolism by Pseudomonas butanovora.Roles for the two 1-butanol dehydrogenases of Pseudomonas butanovora in butane and 1-butanol metabolism.Identification and characterization of a Pantoea citrea gene encoding glucose dehydrogenase that is essential for causing pink disease of pineapple.A novel pyrroloquinoline quinone-dependent 2-keto-D-glucose dehydrogenase from Pseudomonas aureofaciens.Determination of enzyme mechanisms by molecular dynamics: studies on quinoproteins, methanol dehydrogenase, and soluble glucose dehydrogenaseQuinoproteins: enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone or tryptophan-tryptophan quinone.Apoenzyme reconstitution as a chemical tool for structural enzymology and biotechnology.Electrochemical characterization of the pyranose 2-oxidase variant N593C shows a complete loss of the oxidase function with full preservation of substrate (dehydrogenase) activity.PQQ and quinoproteins: an important novel field in enzymology.Characterization of a group of pyrroloquinoline quinone-dependent dehydrogenases that are involved in the conversion of L-sorbose to 2-Keto-L-gulonic acid in Ketogulonicigenium vulgare WSH-001.Characterization of a thermostable glucose dehydrogenase with strict substrate specificity from a hyperthermophilic archaeon Thermoproteus sp. GDH-1.Reversible thermal inactivation of the quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus. Ca2+ ions are necessary for re-activation.Factors relevant in bacterial pyrroloquinoline quinone production.Cytochrome b-562 from Acinetobacter calcoaceticus L.M.D. 79.41. Its characteristics and role as electron acceptor for quinoprotein glucose dehydrogenase.Pyrroloquinoline quinone-dependent dehydrogenases from Ketogulonicigenium vulgare catalyze the direct conversion of L-sorbosone to L-ascorbic acid.Glucose dehydrogenase of a rhizobacterial strain of Enterobacter asburiae involved in mineral phosphate solubilization shares properties and sequence homology with other members of enterobacteriaceaePyrroloquinoline quinone-dependent carbohydrate dehydrogenase: activity enhancement and the role of artificial electron acceptors.Characterization of the mineral phosphate-solubilizing activity of Pantoea agglomerans MMB051 isolated from an iron-rich soil in southeastern Venezuela (Bolívar State).Cloning, characterization and DNA sequencing of the gene encoding the Mr 50,000 quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus.Characterization of a periplasmic quinoprotein from Sphingomonas wittichii that functions as aldehyde dehydrogenase.Modified substrate specificity of pyrroloquinoline quinone glucose dehydrogenase by biased mutation assembling with optimized amino acid substitution.The cooperativity effect in the reaction of soluble quinoprotein (PQQ-containing) glucose dehydrogenase is not due to subunit interaction but to substrate-assisted catalysis.Purification and characterization of the membrane-bound quinoprotein glucose dehydrogenase of Gluconacetobacter diazotrophicus PAL 5.Description of the kinetic mechanism and the enantioselectivity of quinohaemoprotein ethanol dehydrogenase from Comamonas testosteroni in the oxidation of alcohols and aldehydes.2-Keto-D-gluconate-yielding membrane-bound D-glucose dehydrogenase from Arthrobacter globiformis C224: purification and characterization.Characterization and engineering of a novel pyrroloquinoline quinone dependent glucose dehydrogenase from Sorangium cellulosum So ce56.Soluble aldose sugar dehydrogenase from Escherichia coli: a highly exposed active site conferring broad substrate specificity.Quinohaemoprotein ethanol dehydrogenase from Comamonas testosteroni. Purification, characterization, and reconstitution of the apoenzyme with pyrroloquinoline quinone analogues.Purification of a marine bacterial glucose dehydrogenase fromCytophaga marinoflava and its application for measurement of 1,5-anhydro-d-glucitol
P2860
Q24672096-E177001A-D130-439A-A6A2-7BD382AE55FDQ24675291-1D8C220D-FD3E-4B99-8225-883521D5DFD0Q24681871-DB3092CB-C5DC-40E3-B298-BD91FF6C4B22Q27681764-34D4804E-FB44-440F-9D44-FF2613E78223Q28344465-6AF0783B-A4BC-40FC-B017-9AD334DDC6CCQ33995784-9446E79A-5E3C-4C36-A24D-B47B966D59B3Q34308248-C2077DF8-ABF9-4882-82EC-D121D987D6BDQ34316898-20F12A15-8A93-48E4-9748-4AC332B3AC3EQ35196591-DB8BED29-A695-470C-8395-9BDF3D0D5C2BQ35214767-FCFE2AA6-9C43-451D-BF43-795900E8BC44Q35845163-DCFE7CFD-8201-45DC-8E89-3D6F0C5E4ED9Q36421148-A45C9799-6EE2-4D8F-A1DE-9B5A30074F33Q37376166-6191D927-D42A-4EF7-A2FE-906E39F86812Q37481303-5A429F2D-6CEA-45B6-96C8-D76398B08E3EQ38286747-8C3F62A2-28BC-4AC0-AC24-F53E445B6355Q39362629-ADF53DAA-98E1-4BDE-97AA-EA36FA4E6420Q41279945-45A8E5E6-F022-4E27-AA6D-6E358665480FQ41897755-A00563C9-6208-4559-B6B6-4A580CC9574FQ41937035-E8417DF5-01CB-43FA-9721-A3D7D7CB6AB2Q42076207-1DAD8E08-BBFD-4DC7-ABD2-9391C4726298Q42122323-A73E8214-04C0-4B26-8D2D-46D0B551469DQ42139249-3F37E741-005B-412F-AF4A-A57ECC472521Q42952863-DFB4C20C-F3FD-4173-8F8A-9C56F64F794CQ46208136-582DEB0E-7EE4-4AD8-8F1A-D3D6D4DB795BQ48295364-B1314E5D-67BB-47BB-8062-5B10B4D249ADQ50856902-1918F946-FB18-4FBC-B6F5-2CB3952CFE6DQ51138735-3D12AC04-C35E-486D-A2CF-6096390A87ECQ51594272-9944C1D9-8009-4584-BD66-1F6D88AD562AQ51667988-D6DE12D3-AFBB-4B0A-8EE1-D399B12D40A7Q52420453-7C4BEB68-9225-47B8-A09B-27275EAA2D17Q53340866-76D73BF4-8AF0-47D7-B565-246ABEBB8F31Q54378361-FADD7678-1244-4210-9151-85D8516A955AQ54459021-5B5A7973-3345-4C48-B07E-366F4EA73CFBQ54756618-A02F1A89-60A9-4A43-A89C-E16631C2DB08Q57583748-6C672515-02F9-4513-B1EE-620A1254A70F
P2860
Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41
description
1986 nî lūn-bûn
@nan
1986 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
name
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@ast
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@en
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@en-gb
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@nl
type
label
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@ast
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@en
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@en-gb
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@nl
prefLabel
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@ast
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@en
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@en-gb
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@nl
P2093
P2860
P356
P1433
P1476
Purification and characterizat ...... ter calcoaceticus L.M.D. 79.41
@en
P2093
P2860
P356
10.1042/BJ2390163
P407
P577
1986-10-01T00:00:00Z