BRENDA - Enzyme Database show
show all sequences of 1.1.2.8

The active (ADHa) and inactive (ADHi) forms of the PQQ-alcohol dehydrogenase from Gluconacetobacter diazotrophicus differ in their respective oligomeric structures and redox state of their corresponding prosthetic groups

Gomez-Manzo, S.; Gonzalez-Valdez, A.A.; Oria-Hernandez, J.; Reyes-Vivas, H.; Arreguin-Espinosa, R.; Kroneck, P.M.; Sosa-Torres, M.E.; Escamilla, J.E.; FEMS Microbiol. Lett. 328, 106-113 (2012)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
bound
Gluconacetobacter diazotrophicus
16020
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
one [2Fe-2S] cluster per enzyme
Gluconacetobacter diazotrophicus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE; 2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
Gluconacetobacter diazotrophicus
72000
-
1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE; 2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
Gluconacetobacter diazotrophicus
115000
-
inactive enzyme form, native PAGE
Gluconacetobacter diazotrophicus
120000
-
inactive enzyme form, gel filtration
Gluconacetobacter diazotrophicus
330000
-
active enzyme form, gel filtration
Gluconacetobacter diazotrophicus
345000
-
active enzyme form, native PAGE
Gluconacetobacter diazotrophicus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Gluconacetobacter diazotrophicus
-
-
-
Gluconacetobacter diazotrophicus PAL5
-
-
-
Purification (Commentary)
Commentary
Organism
native enzyme from membranes by two steps of anion exchange chormatography, hydroxyapatite chromatography, and gel filtration
Gluconacetobacter diazotrophicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
additional information
ADH is largely expressed in its active form
Gluconacetobacter diazotrophicus
-
Subunits
Subunits
Commentary
Organism
heterodimer
1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE
Gluconacetobacter diazotrophicus
heterotetramer
2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
Gluconacetobacter diazotrophicus
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome c
prosthetic groups, four per enzyme
Gluconacetobacter diazotrophicus
additional information
one [2Fe-2S] cluster per enzyme
Gluconacetobacter diazotrophicus
pyrroloquinoline quinone
prosthetic group, one per enzyme
Gluconacetobacter diazotrophicus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome c
prosthetic groups, four per enzyme
Gluconacetobacter diazotrophicus
additional information
one [2Fe-2S] cluster per enzyme
Gluconacetobacter diazotrophicus
pyrroloquinoline quinone
prosthetic group, one per enzyme
Gluconacetobacter diazotrophicus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
bound
Gluconacetobacter diazotrophicus
16020
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
one [2Fe-2S] cluster per enzyme
Gluconacetobacter diazotrophicus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE; 2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
Gluconacetobacter diazotrophicus
72000
-
1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE; 2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
Gluconacetobacter diazotrophicus
115000
-
inactive enzyme form, native PAGE
Gluconacetobacter diazotrophicus
120000
-
inactive enzyme form, gel filtration
Gluconacetobacter diazotrophicus
330000
-
active enzyme form, gel filtration
Gluconacetobacter diazotrophicus
345000
-
active enzyme form, native PAGE
Gluconacetobacter diazotrophicus
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme from membranes by two steps of anion exchange chormatography, hydroxyapatite chromatography, and gel filtration
Gluconacetobacter diazotrophicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
additional information
ADH is largely expressed in its active form
Gluconacetobacter diazotrophicus
-
Subunits (protein specific)
Subunits
Commentary
Organism
heterodimer
1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE
Gluconacetobacter diazotrophicus
heterotetramer
2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
Gluconacetobacter diazotrophicus
General Information
General Information
Commentary
Organism
additional information
the enzyme occurs in active and inactive forms, overview. Active ADHa is brought back by ethanol to its full reduction state, but in inactive ADHi, only one-quarter of the total heme c is reduced, pH dependencies and redox potentials of cofactors, overview
Gluconacetobacter diazotrophicus
General Information (protein specific)
General Information
Commentary
Organism
additional information
the enzyme occurs in active and inactive forms, overview. Active ADHa is brought back by ethanol to its full reduction state, but in inactive ADHi, only one-quarter of the total heme c is reduced, pH dependencies and redox potentials of cofactors, overview
Gluconacetobacter diazotrophicus
Other publictions for EC 1.1.2.8
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating 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)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
742793
Good
Pyrroloquinoline quinone etha ...
Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
J. Bacteriol.
198
3109-3118
2016
2
-
1
-
1
-
-
-
-
3
1
6
-
16
-
-
1
-
-
1
-
-
8
1
1
-
-
-
1
-
-
3
-
-
-
2
-
1
3
-
1
-
-
-
-
-
-
3
1
6
-
-
-
1
-
1
-
-
8
1
1
-
-
-
1
-
-
-
-
3
3
-
-
-
743174
Simon
Analysis of the molecular res ...
Pseudomonas putida, Pseudomonas putida KT 2240
J. Proteomics
122
11-25
2015
-
-
-
-
1
-
-
-
1
-
-
8
-
4
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
4
-
2
-
-
-
-
-
2
-
-
8
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
2
4
-
-
-
742110
Takeda
Effect of amines as activator ...
Pseudomonas putida, Pseudomonas putida KT 2240
Biosci. Biotechnol. Biochem.
78
1195-1198
2014
15
-
-
-
-
-
2
4
1
1
-
-
-
44
-
-
-
-
-
-
-
-
6
-
1
-
-
4
1
-
-
3
2
-
-
15
-
-
3
-
-
-
-
2
2
4
1
1
-
-
-
-
-
-
-
-
-
-
6
-
1
-
-
4
1
-
-
-
-
1
1
-
4
4
741733
Zhang
Isolation and characterizatio ...
Pseudomonas mendocina, Pseudomonas mendocina YMP, Pseudomonas sp., Pseudomonas sp. J51, Pseudomonas stutzeri, Pseudomonas stutzeri ATCC 14405
Appl. Microbiol. Biotechnol.
97
4095-4104
2013
-
1
3
-
-
-
-
-
-
-
-
6
-
8
-
-
-
-
-
-
-
-
6
2
-
-
-
-
-
-
-
3
-
2
-
-
1
3
3
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
6
2
-
-
-
-
-
-
-
2
1
6
6
1
-
-
725041
Gomez-Manzo
The active (ADHa) and inactive ...
Gluconacetobacter diazotrophicus, Gluconacetobacter diazotrophicus PAL5
FEMS Microbiol. Lett.
328
106-113
2012
-
-
-
-
-
-
-
-
1
1
6
-
-
3
-
-
1
-
-
1
-
-
-
2
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
1
1
6
-
-
-
-
1
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
724042
Kanchanarach
Characterization of thermotole ...
Acetobacter pasteurianus, Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus SKU1108
Appl. Microbiol. Biotechnol.
85
741-751
2010
-
-
1
-
-
-
-
-
-
-
-
16
1
16
-
-
1
-
-
1
-
-
16
-
2
-
-
-
1
-
-
1
-
-
-
-
-
5
8
-
-
-
-
-
-
-
-
-
-
16
8
-
-
8
-
8
-
-
16
-
8
-
-
-
8
-
-
-
-
1
8
-
-
-
725154
Masud
Cloning and functional analysi ...
Acetobacter pasteurianus, Acetobacter pasteurianus SKU1108
Int. J. Food Microbiol.
138
39-49
2010
1
-
-
-
9
-
-
-
1
1
-
2
-
6
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
1
-
-
-
1
-
-
1
-
9
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
1
1
1
1
-
-
674560
Kay
Structure of the pyrroloquinol ...
Pseudomonas aeruginosa
J. Biol. Chem.
281
1470-1476
2006
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
676857
Kay
Substrate binding in quinoprot ...
Pseudomonas aeruginosa
Proc. Natl. Acad. Sci. USA
103
5267-5272
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389959
Keitel
X-ray structure of the quinopr ...
Pseudomonas aeruginosa
J. Mol. Biol.
297
961-974
2000
-
-
-
1
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389964
Diehl
Quinoprotein ethanol dehydroge ...
Pseudomonas aeruginosa
Eur. J. Biochem.
257
409-419
1998
-
-
1
1
1
-
-
-
-
-
2
-
-
1
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
1
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
702114
Schrover
Quaternary structure of quinop ...
Pseudomonas aeruginosa
Biochem. J.
290 (Pt 1)
123-127
1993
-
-
-
-
-
-
-
-
-
1
3
-
-
1
-
-
1
-
-
-
1
-
1
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
3
-
-
-
-
1
-
-
1
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
701600
Mutzel
-
Quinoprotein ethanol dehydroge ...
Pseudomonas aeruginosa
Agric. Biol. Chem.
55
1721-1726
1991
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
705106
Stezowski
Preliminary X-ray crystallogra ...
Pseudomonas aeruginosa
J. Mol. Biol.
205
617-618
1989
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-