BRENDA - Enzyme Database show
show all sequences of 1.3.5.4

Oxidation of reduced menaquinone by the fumarate reductase complex in Escherichia coli requires the hydrophobic FrdD peptide

Cecchini, G.; Thompson, C.R.; Ackrell, B.A.; Westenberg, D.J.; Dean, N.; Gunsalus, R.P.; Proc. Natl. Acad. Sci. USA 83, 8898-8902 (1986)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
isolation of a mutant in the frdD gene encoding the hydrophic subunit of the fumarate reductase complex. In this mutant, fumarate reductase is not as tightly bound to the membrane. The mutation in the FrdD peptide causes an almost total loss of the ability of the enzyme to oxidize either menaquinol-6, or reduced benzyl viologen. The mutation does not impair the ability of the membrane-bound fumarate reductase complex to function with succinate as substrate
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
isolation of a mutant in the frdD gene encoding the hydrophic subunit of the fumarate reductase complex. In this mutant, fumarate reductase is not as tightly bound to the membrane. The mutation in the FrdD peptide causes an almost total loss of the ability of the enzyme to oxidize either menaquinol-6, or reduced benzyl viologen. The mutation does not impair the ability of the membrane-bound fumarate reductase complex to function with succinate as substrate
Escherichia coli
General Information
General Information
Commentary
Organism
physiological function
the FrdD subunit has an essential role both in the interaction of the enzyme with reduced menaquinone and thus in anaerobic respiration with fumarate as electron acceptor, and in binding the enzyme to the membrane
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the FrdD subunit has an essential role both in the interaction of the enzyme with reduced menaquinone and thus in anaerobic respiration with fumarate as electron acceptor, and in binding the enzyme to the membrane
Escherichia coli
Other publictions for EC 1.3.5.4
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)
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742846
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288
24293-24301
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1
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743059
Nasiri
Design, synthesis, and biolog ...
Wolinella succinogenes, Wolinella succinogenes DSM 1740
J. Med. Chem.
56
9530-9541
2013
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724561
Herzog
Hydrogen-bonded networks along ...
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Biophys. J.
103
1305-1314
2012
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3
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725316
Shimizu
Crystal structure of mitochond ...
Ascaris suum
J. Biochem.
151
589-592
2012
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700278
Juhnke
Production, characterization a ...
Campylobacter jejuni, Wolinella succinogenes
Mol. Microbiol.
71
1088-1101
2009
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707545
Xin
Purification, characterization ...
Chloroflexus aurantiacus
Biochim. Biophys. Acta
1787
86-96
2009
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707949
Garcia
The succinate:menaquinone redu ...
Bacillus cereus
Can. J. Microbiol.
54
456-466
2008
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674532
Maklashina
Fumarate reductase and succina ...
Escherichia coli
J. Biol. Chem.
281
11357-11365
2006
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674634
Maklashina
Differences in protonation of ...
Escherichia coli
J. Biol. Chem.
281
26655-26664
2006
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7
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707470
Madej
Experimental evidence for prot ...
Bacillus licheniformis
Biochemistry
45
15049-15055
2006
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671694
Fernandes
Quinone reduction by Rhodother ...
Rhodothermus marinus
Biochem. Biophys. Res. Commun.
330
565-570
2005
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654820
Cecchini
Succinate dehydrogenase and fu ...
Escherichia coli
Biochim. Biophys. Acta
1553
140-157
2002
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708975
Iverson
Crystallographic studies of th ...
Escherichia coli
J. Biol. Chem.
277
16124-16130
2002
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708368
Schnorpfeil
Generation of a proton potenti ...
Bacillus subtilis
Eur. J. Biochem.
268
3069-3074
2001
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1
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391149
Lancaster
Succinate:quinone oxidoreducta ...
Escherichia coli, Wolinella succinogenes
Biochim. Biophys. Acta
1459
422-431
2000
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1
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1
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1
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2
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2
2
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708909
Maklashina
Anaerobic expression of Escher ...
Escherichia coli
J. Bacteriol.
180
5989-5996
1998
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1
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708966
Schroder
Identification of active site ...
Escherichia coli
J. Biol. Chem.
266
13572-13579
1991
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4
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391090
Körtner
Wolinella succinogenes fumarat ...
Wolinella succinogenes
Mol. Microbiol.
4
855-860
1990
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1
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391089
Lauterbach
Cloning and expression of the ...
Wolinella succinogenes
Eur. J. Biochem.
166
447-452
1987
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1
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391106
Weiner
A mutant of Escherichia coli f ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
83
2056-2060
1986
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391147
Gottfried
Reconstitution of a functional ...
Wolinella succinogenes
Methods Enzymol.
126
387-399
1986
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4
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710440
Cecchini
Oxidation of reduced menaquino ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
83
8898-8902
1986
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1
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391094
Unden
-
Redox potentials and kinetic p ...
Wolinella succinogenes
Biochim. Biophys. Acta
767
460-469
1984
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391084
Unden
The function of the subunits o ...
Wolinella succinogenes
Eur. J. Biochem.
120
577-584
1981
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2
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1
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1
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391092
Unden
Isolation and functional aspec ...
Wolinella succinogenes
Biochim. Biophys. Acta
591
275-288
1980
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6
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2
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6
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2
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391116
Kröger
The orientation of the substra ...
Wolinella succinogenes
Biochim. Biophys. Acta
589
118-136
1980
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707291
Van der Beek
Fumarate reduction in Proteus ...
Proteus mirabilis
Arch. Microbiol.
110
195-206
1976
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2
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708369
Kroeger
-
The function of menaquinone, c ...
Wolinella succinogenes
Eur. J. Biochem.
69
487-495
1976
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