BRENDA - Enzyme Database show
show all sequences of 1.1.2.7

A rapid method for the purification of methanol dehydrogenase from Methylobacterium extorquens

Liu, Q.; Kirchhoff, J.R.; Faehnle, C.R.; Viola, R.E.; Hudson, R.A.; Protein Expr. Purif. 46, 316-320 (2006)

Data extracted from this reference:

General Stability
General Stability
Organism
EDTA, DTT, and Ca2+ are slightly stabilizing
Methylorubrum extorquens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
bound to the active site, required for catalytic activity
Methylorubrum extorquens
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
7500
-
x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE
Methylorubrum extorquens
62000
-
x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE
Methylorubrum extorquens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methylorubrum extorquens
P16027 and P14775
P16027 (large subunit, alpha) and P14775 (small subunit, beta)
-
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
P16027 and P14775
P16027 (large subunit, alpha) and P14775 (small subunit, beta)
-
Purification (Commentary)
Commentary
Organism
native enzyme 22fold from strain AM1 in a single cation exchange chromatographical step, followed by ultrafiltration and buffer exchange, over 97% purity
Methylorubrum extorquens
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
5.4
-
purified enzyme
Methylorubrum extorquens
Storage Stability
Storage Stability
Organism
-80°C, purified native enzyme, 20 mM phosphate, pH 7.0, negligible loss of activity in 6 months
Methylorubrum extorquens
4°C, purified native enzyme, 20 mM phosphate, pH 7.0, loss of 80% activity within 1 week
Methylorubrum extorquens
Subunits
Subunits
Commentary
Organism
?
x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE
Methylorubrum extorquens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Methylorubrum extorquens
Cofactor
Cofactor
Commentary
Organism
Structure
pyrroloquinoline quinone
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
Methylorubrum extorquens
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Methylorubrum extorquens
sequence calculation
-
8.8
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyrroloquinoline quinone
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
Methylorubrum extorquens
General Stability (protein specific)
General Stability
Organism
EDTA, DTT, and Ca2+ are slightly stabilizing
Methylorubrum extorquens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
bound to the active site, required for catalytic activity
Methylorubrum extorquens
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
7500
-
x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE
Methylorubrum extorquens
62000
-
x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE
Methylorubrum extorquens
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme 22fold from strain AM1 in a single cation exchange chromatographical step, followed by ultrafiltration and buffer exchange, over 97% purity
Methylorubrum extorquens
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
5.4
-
purified enzyme
Methylorubrum extorquens
Storage Stability (protein specific)
Storage Stability
Organism
-80°C, purified native enzyme, 20 mM phosphate, pH 7.0, negligible loss of activity in 6 months
Methylorubrum extorquens
4°C, purified native enzyme, 20 mM phosphate, pH 7.0, loss of 80% activity within 1 week
Methylorubrum extorquens
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE
Methylorubrum extorquens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Methylorubrum extorquens
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Methylorubrum extorquens
sequence calculation
-
8.8
Other publictions for EC 1.1.2.7
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)
724402
Gvozdev
Quinone-dependent alcohol dehy ...
Diplococcus sp., Methylophilus methylotrophus, Methylophilus methylotrophus W3A1, Methylorubrum extorquens, Paracoccus denitrificans, Paracoccus pantotrophus, Pseudomonas sp., Rhodoblastus acidophilus
Biochemistry
77
843-856
2012
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14
7
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8
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45
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7
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24
7
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7
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7
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14
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24
7
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725300
Kim
Comparative analysis of two ty ...
Methylophaga aminisulfidivorans, Methylophaga aminisulfidivorans MPT
J. Basic Microbiol.
52
141-149
2012
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1
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4
2
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3
4
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7
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1
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12
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1
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8
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12
6
2
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8
2
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4
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1
2
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723854
Choi
Purification, crystallization ...
Methylophaga aminisulfidivorans, Methylophaga aminisulfidivorans MPT
Acta Crystallogr. Sect. F
67
513-516
2011
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1
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1
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2
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3
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1
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2
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2
2
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1
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1
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724176
Li
The enzymatic reaction-induced ...
Methylophilus methylotrophus, Methylophilus methylotrophus W3A1
Biochem. Biophys. Res. Commun.
406
621-626
2011
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-
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1
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1
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2
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1
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2
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1
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2
2
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1
1
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712855
Idupulapati
Quantum chemical modeling of m ...
Methylorubrum extorquens
J. Phys. Chem. A
114
1887-1896
2010
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1
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1
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1
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687417
Kalyuzhnaya
Characterization of a novel me ...
Methylibium petroleiphilum, Methyloversatilis universalis, Methyloversatilis universalis FAM5
J. Bacteriol.
190
3817-3823
2008
2
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2
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8
2
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3
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10
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15
2
2
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2
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4
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2
4
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8
2
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15
2
2
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2
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673047
Leopoldini
The preferred reaction path fo ...
Methylophilus methylotrophus, Methylophilus methylotrophus W3A1
Chem. Eur. J.
13
2109-2117
2007
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1
1
1
2
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39
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1
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1
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1
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1
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676902
Zhang
Mechanism of methanol oxidatio ...
Methylophilus methylotrophus
Proc. Natl. Acad. Sci. USA
104
745-749
2007
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667721
Nojiri
Crystal structures of cytochro ...
Hyphomicrobium denitrificans, Hyphomicrobium denitrificans A3151
Biochemistry
45
3481-3492
2006
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1
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7
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3
4
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9
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1
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6
1
1
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8
1
1
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2
1
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7
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4
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1
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6
1
1
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8
1
1
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670785
Liu
A rapid method for the purific ...
Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
Protein Expr. Purif.
46
316-320
2006
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1
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1
2
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688333
Williams
The 1.6A X-ray structure of th ...
Methylorubrum extorquens
J. Mol. Biol.
357
151-162
2006
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671068
Williams
The atomic resolution structur ...
Methylorubrum extorquens
Acta Crystallogr. Sect. D
D61
75-79
2005
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673048
Nojiri
-
Preparation and characterizati ...
Hyphomicrobium denitrificans, Hyphomicrobium denitrificans A3151
Chem. Lett.
34
1036-1037
2005
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684666
Anthony
The quinoprotein dehydrogenase ...
Methylophilus sp., Methylorubrum extorquens
Arch. Biochem. Biophys.
428
2-9
2004
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685313
Anthony
The structure and mechanism of ...
Methylophilus sp., Methylorubrum extorquens
Biochim. Biophys. Acta
1647
18-23
2003
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687993
Jongejan
Direct hydride transfer in the ...
Methylophilus methylotrophus, Methylorubrum extorquens
J. Comput. Chem.
22
1732-1749
2001
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689818
Zheng
Catalytic mechanism of quinopr ...
Methylophilus methylotrophus, Methylophilus methylotrophus W3A1
Proc. Natl. Acad. Sci. USA
98
432-434
2001
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687432
Grosse
Purification and properties of ...
Methylosinus sp., Methylosinus sp. WI 14
J. Basic Microbiol.
38
189-196
1998
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689815
Zheng
Conformation of coenzyme pyrro ...
Methylophilus methylotrophus, Methylophilus methylotrophus W3A1
Proc. Natl. Acad. Sci. USA
94
11881-11886
1997
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684950
Goodwin
Reconstitution of the quinopro ...
Methylorubrum extorquens
Biochem. J.
319
839-842
1996
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684948
Avezoux
The role of the novel disulphi ...
Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
Biochem. J.
307
735-741
1995
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