BRENDA - Enzyme Database show
show all sequences of 7.1.1.1

Properties of a cysteine-free proton-pumping nicotinamide nucleotide transhydrogenase

Meuller, J.; Zhang, J.; Hou, C.; Bragg, P.D.; Rydstrom, J.; Biochem. J. 324, 681-687 (1997)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
C292T/C339T/C395S/C397T/C435S
cysteine of the alpha subunits replaced, similar activity as wild-type
Escherichia coli
C292T/C339T/C395S/C397T/C435S/C147S/C260S
all 7 cysteines of the enzyme, 5 localized in the alpha subunit and 2 in the beta subunit, are replaced, the cysteine-free mutant shows about 5fold more activity in the reduction of acetylpyridine adenine dinucleotide by NADH than wild-type, the cyclic reduction of acetylpyridine adenine dinucleotide by NADH via NADPH is 2-2.5fold more activ
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
N-ethylmaleimide
cysteine-free mutant enzyme is not inhibited
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0017
-
NADH
wild-type enzyme
Escherichia coli
0.002
-
NADH
cysteine-free enzyme
Escherichia coli
0.0051
-
NADPH
cysteine-free enzyme
Escherichia coli
0.008
-
thio-NADP+
wild-type enzyme
Escherichia coli
0.015
-
NADPH
wild-type enzyme
Escherichia coli
0.018
-
thio-NADP+
cysteine-free enzyme
Escherichia coli
0.02
-
oxidized acetylpyridine adenine dinucleotide
cysteine-free enzyme
Escherichia coli
0.026
-
oxidized acetylpyridine adenine dinucleotide
wild-type enzyme
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
0.2
-
reduction of NADP+ by NADH driven by electron transport, cysteine-free enzyme reconstituted in membrane vesicles
Escherichia coli
0.42
-
reduction of NADP+ by NADH driven by electron transport, wild-type enzyme reconstituted in membrane vesicles
Escherichia coli
1.9
-
reduction of acetylpyridine adenine dinucleotide by NADPH, cysteine-free enzyme reconstituted in membrane vesicles
Escherichia coli
3
-
reduction of acetylpyridine adenine dinucleotide by NADPH, wild-type enzyme reconstituted in membrane vesicles
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
NADH
-
Escherichia coli
NADP+
-
Escherichia coli
NADPH
-
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
NADH
-
Escherichia coli
NADP+
-
Escherichia coli
NADPH
-
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C292T/C339T/C395S/C397T/C435S
cysteine of the alpha subunits replaced, similar activity as wild-type
Escherichia coli
C292T/C339T/C395S/C397T/C435S/C147S/C260S
all 7 cysteines of the enzyme, 5 localized in the alpha subunit and 2 in the beta subunit, are replaced, the cysteine-free mutant shows about 5fold more activity in the reduction of acetylpyridine adenine dinucleotide by NADH than wild-type, the cyclic reduction of acetylpyridine adenine dinucleotide by NADH via NADPH is 2-2.5fold more activ
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
N-ethylmaleimide
cysteine-free mutant enzyme is not inhibited
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0017
-
NADH
wild-type enzyme
Escherichia coli
0.002
-
NADH
cysteine-free enzyme
Escherichia coli
0.0051
-
NADPH
cysteine-free enzyme
Escherichia coli
0.008
-
thio-NADP+
wild-type enzyme
Escherichia coli
0.015
-
NADPH
wild-type enzyme
Escherichia coli
0.018
-
thio-NADP+
cysteine-free enzyme
Escherichia coli
0.02
-
oxidized acetylpyridine adenine dinucleotide
cysteine-free enzyme
Escherichia coli
0.026
-
oxidized acetylpyridine adenine dinucleotide
wild-type enzyme
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
0.2
-
reduction of NADP+ by NADH driven by electron transport, cysteine-free enzyme reconstituted in membrane vesicles
Escherichia coli
0.42
-
reduction of NADP+ by NADH driven by electron transport, wild-type enzyme reconstituted in membrane vesicles
Escherichia coli
1.9
-
reduction of acetylpyridine adenine dinucleotide by NADPH, cysteine-free enzyme reconstituted in membrane vesicles
Escherichia coli
3
-
reduction of acetylpyridine adenine dinucleotide by NADPH, wild-type enzyme reconstituted in membrane vesicles
Escherichia coli
Other publictions for EC 7.1.1.1
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)
742240
Murphy
Redox modulation by reversal ...
Mus musculus, Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Cell Metab.
22
363-365
2015
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743841
Leung
Structural biology. Division ...
Thermus thermophilus
Science
347
178-181
2015
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733380
Jackson J.B
A review of the binding-change ...
Escherichia coli, Rhodospirillum rubrum
Biochim. Biophys. Acta
1817
1839-1846
2012
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733378
Huxley
The specificity of proton-tran ...
Rhodospirillum rubrum
Biochim. Biophys. Acta
1807
85-94
2011
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1
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4
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698677
Pedersen
Proton-translocating transhydr ...
Escherichia coli, Rhodospirillum rubrum
J. Bioenerg. Biomembr.
40
463-473
2008
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4
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6
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6
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685140
Bhakta
Structures of the dI2dIII1 com ...
Rhodospirillum rubrum
Biochemistry
46
3304-3318
2007
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1
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687656
Obiozo
Substitution of tyrosine 146 i ...
Rhodospirillum rubrum
J. Biol. Chem.
282
36434-36443
2007
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1
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2
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689135
Pestov
Purification of recombinant me ...
Escherichia coli
Nat. Protoc.
2
198-202
2007
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674194
Iwaki
Molecular recognition between ...
Escherichia coli
J. Am. Chem. Soc.
128
2621-2629
2006
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674550
Brondijk
The role of invariant amino ac ...
Rhodospirillum rubrum
J. Biol. Chem.
281
13345-13354
2006
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1
7
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659725
Sundaresan
Conformational diversity in NA ...
Rhodospirillum rubrum
J. Mol. Biol.
346
617-629
2005
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672321
Pedersen
Titration of E. coli transhydr ...
Escherichia coli
Biochim. Biophys. Acta
1707
254-258
2005
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1
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672325
Bizouarn
Nucleotide binding affinities ...
Escherichia coli
Biochim. Biophys. Acta
1708
404-410
2005
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673613
Whitehead
Zinc ions selectively inhibit ...
Rhodospirillum rubrum
FEBS Lett.
579
2863-2867
2005
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675352
Johansson
X-ray structure of domain I of ...
Escherichia coli
J. Mol. Biol.
352
299-312
2005
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657468
Oswald
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. D
60
743-745
2004
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1
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658022
Mather
Active-site conformational cha ...
Homo sapiens, Rhodospirillum rubrum
Biochemistry
43
10952-10964
2004
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2
2
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658197
Althage
Cross-linking of transmembrane ...
Escherichia coli
Biochim. Biophys. Acta
1659
73-82
2004
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659437
Sauer
The soluble and membrane-bound ...
Escherichia coli
J. Biol. Chem.
279
6613-6619
2004
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1
1
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660435
Egorov
Purification of a recombinant ...
Escherichia coli
Protein Expr. Purif.
36
31-39
2004
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1
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1
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1
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1
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1
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1
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1
1
3
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1
1
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2
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1
2
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1
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1
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1
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1
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1
1
3
-
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1
1
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657960
van Boxel
Glutamine 132 in the NAD(H)-bi ...
Rhodospirillum rubrum
Biochemistry
42
1217-1226
2003
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1
1
2
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1
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2
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1
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1
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3
1
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2
1
2
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1
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3
1
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658003
Karlsson
Roles of individual amino acid ...
Escherichia coli
Biochemistry
42
6575-6581
2003
-
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1
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23
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1
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2
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1
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1
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3
1
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2
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1
2
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23
-
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The organization of the membra ...
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Properties of a proton-translo ...
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Interactions of the NADP(H)-bi ...
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Bizouarn
Proton translocating nicotinam ...
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Jeeves
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Solution structure of the NADP ...
Rhodospirillum rubrum
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Bragg
The presence of an aqueous cav ...
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2000
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Jeeves
Solution structure of the NADP ...
Rhodospirillum rubrum
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Fjellstr÷m
Mapping of residues in the NAD ...
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Hu
Site-directed mutagenesis of c ...
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Biochemistry
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Fjellstrom
Catalytic properties of hybrid ...
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Biochemistry
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1999
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Anderlund
Expression of the Escherichia ...
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Quirk
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Glavas
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Clarke
Cloning and expression of the ...
Escherichia coli, Escherichia coli MV-12
J. Bacteriol.
162
367-373
1985
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392627
McFadden
Resolution and reconstitution ...
Rhodospirillum rubrum
Arch. Biochem. Biophys.
190
820-828
1978
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