BRENDA - Enzyme Database
show all sequences of 1.5.8.1

Dehydrogenases of methylotrophic bacteria as possible models for electron transfer in iron-sulfur flavoproteins

Beinert, H.; Shaw, R.W.; Steenkamp, D.J.; Singer, T.P.; Stevenson, R.; Dunham, W.R.; Sands, R.H.; Dev. Biochem. 21, 727-735 (1982)
No PubMed abstract available

Data extracted from this reference:

Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
the enzyme as a possible model for electron transfer in iron-sulfur flavoproteins
Hyphomicrobium sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Hyphomicrobium sp.
-
X
-
Hyphomicrobium sp. X
-
X
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
the enzyme as a possible model for electron transfer in iron-sulfur flavoproteins
Hyphomicrobium sp.
Other publictions for EC 1.5.8.1
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)
711031
Liffourrena
Pseudomonas putida A ATCC 1263 ...
Pseudomonas putida, Pseudomonas putida ATCC 12633
Arch. Microbiol.
192
471-476
2010
-
-
-
-
-
-
-
-
-
-
-
2
-
5
-
-
-
-
-
2
-
-
2
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
393894
Kim
A novel denitrifying bacterial ...
Paracoccus sp.
Arch. Microbiol.
176
271-277
2001
-
-
-
-
-
-
-
-
-
-
-
4
-
6
-
-
-
-
-
-
2
-
6
-
1
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-
-
1
-
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2
-
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-
2
-
-
-
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-
-
-
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4
-
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-
2
-
6
-
1
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-
-
1
-
-
-
-
-
-
-
-
-
393877
Yang
The primary structure of Hypho ...
Hyphomicrobium sp., Hyphomicrobium sp. X
Eur. J. Biochem.
232
264-271
1995
-
-
1
-
-
-
-
-
-
-
1
-
-
14
-
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1
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-
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-
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1
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-
-
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-
-
-
-
-
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-
1
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1
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-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
393879
Kasprzak
Identity of the subunits and t ...
Hyphomicrobium sp., Hyphomicrobium sp. X
Biochem. J.
211
535-541
1983
-
-
-
-
-
-
-
-
-
1
-
-
-
13
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
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-
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-
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1
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-
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1
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-
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-
-
-
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-
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-
-
1
-
-
-
-
-
-
-
-
-
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-
-
-
-
393884
Kasprzak
Localization of the major dehy ...
Hyphomicrobium sp., Hyphomicrobium sp. X
J. Bacteriol.
156
348-353
1983
-
-
-
-
-
-
-
-
1
-
-
-
-
11
-
-
-
-
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1
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-
393878
Steenkamp
Mechanistic studies on the deh ...
Hyphomicrobium sp., Hyphomicrobium sp. X
Biochem. J.
207
241-252
1982
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-
-
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-
-
1
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-
-
15
-
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-
1
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1
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1
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-
-
-
-
-
-
-
393883
Beinert
-
Dehydrogenases of methylotroph ...
Hyphomicrobium sp., Hyphomicrobium sp. X
Dev. Biochem.
21
727-735
1982
-
-
-
-
-
-
-
-
-
1
-
-
-
11
-
-
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-
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-
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1
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-
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393880
Meiberg
-
Dimethylamine dehydrogenase fr ...
Hyphomicrobium sp., Hyphomicrobium sp. X
J. Gen. Microbiol.
115
49-58
1979
-
-
-
-
-
1
4
3
-
-
2
-
-
11
-
-
1
-
-
1
1
2
18
1
-
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-
-
1
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1
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4
-
3
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-
2
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1
-
1
1
2
18
1
-
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-
-
1
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-
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393881
Steenkamp
Identification of the prosthet ...
Hyphomicrobium sp., Hyphomicrobium sp. X
Biochem. Biophys. Res. Commun.
88
244-250
1979
-
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1
1
-
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12
-
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1
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-
1
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1
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1
1
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1
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393882
Large
-
Cytochrome cCO is not a primar ...
Hyphomicrobium sp., Hyphomicrobium sp. X
FEMS Microbiol. Lett.
5
281-286
1979
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2
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11
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4
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2
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4
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