BRENDA - Enzyme Database show
show all sequences of 7.1.1.1

Kinetic resolution of the reaction catalysed by proton-translocating transhydrogenase from Escherichia coli as revealed by experiments with analogues of the nucleotide substrates

Hutton, M.; Day, J.M.; Bizouarn, T.; Jackson, J.B.; Eur. J. Biochem. 219, 1041-1051 (1994)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli JM83 cells
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
N,N'-dicyclohexylcarbodiimide
modification of the enzyme with N,N'-dicyclohexylcarbodiimide leads to inhibition of the rate of release of NADP+ and NADPH from the enzyme, but has a much smaller effect on the binding and release of NAD+, NADH and their analogues and on the interconversion of the ternary complexes of the enzyme with its substrates
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
49000
-
1 * 54000 + 1 * 49000, SDS-PAGE
Escherichia coli
54000
-
1 * 54000 + 1 * 49000, SDS-PAGE
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
NADPH + NAD+ + H+[side 1]
Escherichia coli
-
NADP+ + NADH + H+[side 2]
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
phenyl-Sepharose column chromatography and DEAE-Trisacryl M column chromatography
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.11
-
with oxidized acetyl pyridine adenine dinucleotide and deamino-NADPH as substrates, at pH 6.0 and 25C
Escherichia coli
0.47
-
with oxidized acetyl pyridine adenine dinucleotide and 1-N6-etheno-NADPH as substrates, at pH 6.0 and 25C
Escherichia coli
1.46
-
with oxidized acetyl pyridine adenine dinucleotide and NADPH as substrates, at pH 6.0 and 25C
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,N6-etheno-NADPH + NAD+ + H+[side 1]
-
733762
Escherichia coli
1,N6-etheno-NADP+ + NADH + H+[side 2]
-
-
-
r
1,N6-etheno-NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
-
733762
Escherichia coli
1,N6-etheno-NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
-
-
r
deamino-NADPH + NAD+ + H+[side 1]
-
733762
Escherichia coli
deamino-NADP+ + NADH + H+[side 2]
-
-
-
r
deamino-NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
-
733762
Escherichia coli
deamino-NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
-
-
r
NADPH + NAD+ + H+[side 1]
-
733762
Escherichia coli
NADP+ + NADH + H+[side 2]
-
-
-
r
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
-
733762
Escherichia coli
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
-
-
r
Subunits
Subunits
Commentary
Organism
heterodimer
1 * 54000 + 1 * 49000, SDS-PAGE
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli JM83 cells
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
N,N'-dicyclohexylcarbodiimide
modification of the enzyme with N,N'-dicyclohexylcarbodiimide leads to inhibition of the rate of release of NADP+ and NADPH from the enzyme, but has a much smaller effect on the binding and release of NAD+, NADH and their analogues and on the interconversion of the ternary complexes of the enzyme with its substrates
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
49000
-
1 * 54000 + 1 * 49000, SDS-PAGE
Escherichia coli
54000
-
1 * 54000 + 1 * 49000, SDS-PAGE
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
NADPH + NAD+ + H+[side 1]
Escherichia coli
-
NADP+ + NADH + H+[side 2]
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
phenyl-Sepharose column chromatography and DEAE-Trisacryl M column chromatography
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.11
-
with oxidized acetyl pyridine adenine dinucleotide and deamino-NADPH as substrates, at pH 6.0 and 25C
Escherichia coli
0.47
-
with oxidized acetyl pyridine adenine dinucleotide and 1-N6-etheno-NADPH as substrates, at pH 6.0 and 25C
Escherichia coli
1.46
-
with oxidized acetyl pyridine adenine dinucleotide and NADPH as substrates, at pH 6.0 and 25C
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,N6-etheno-NADPH + NAD+ + H+[side 1]
-
733762
Escherichia coli
1,N6-etheno-NADP+ + NADH + H+[side 2]
-
-
-
r
1,N6-etheno-NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
-
733762
Escherichia coli
1,N6-etheno-NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
-
-
r
deamino-NADPH + NAD+ + H+[side 1]
-
733762
Escherichia coli
deamino-NADP+ + NADH + H+[side 2]
-
-
-
r
deamino-NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
-
733762
Escherichia coli
deamino-NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
-
-
r
NADPH + NAD+ + H+[side 1]
-
733762
Escherichia coli
NADP+ + NADH + H+[side 2]
-
-
-
r
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
-
733762
Escherichia coli
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
heterodimer
1 * 54000 + 1 * 49000, SDS-PAGE
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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1
1
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2
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3
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3
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1
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3
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1
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1
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743841
Leung
Structural biology. Division ...
Thermus thermophilus
Science
347
178-181
2015
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1
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1
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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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2
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2
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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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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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4
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1
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2
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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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2
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2
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6
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2
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2
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4
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2
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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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1
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2
1
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1
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2
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1
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1
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2
2
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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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1
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1
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1
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1
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7
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1
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659725
Sundaresan
Conformational diversity in NA ...
Rhodospirillum rubrum
J. Mol. Biol.
346
617-629
2005
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1
1
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1
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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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1
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673613
Whitehead
Zinc ions selectively inhibit ...
Rhodospirillum rubrum
FEBS Lett.
579
2863-2867
2005
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1
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2
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1
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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
1
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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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2
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3
-
3
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1
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2
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2
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5
2
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658197
Althage
Cross-linking of transmembrane ...
Escherichia coli
Biochim. Biophys. Acta
1659
73-82
2004
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1
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7
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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
1
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2
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1
2
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7
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1
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1
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1
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2
1
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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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van Boxel
Glutamine 132 in the NAD(H)-bi ...
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Biochemistry
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2003
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Karlsson
Roles of individual amino acid ...
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Biochemistry
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Proton translocation by transh ...
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Prasad
Crystal structures of transhyd ...
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658162
Rodrigues
A conformational change in the ...
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Biochim. Biophys. Acta
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2002
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Bizouarn
The organization of the membra ...
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2002
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Redox-sensitive loops D and E ...
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The crystal structure of an as ...
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2001
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392672
Meuller
Properties of a proton-translo ...
Escherichia coli
Biochim. Biophys. Acta
1506
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2001
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Rodrigues
A change in ionization of the ...
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2001
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Bergkvist
Interactions of the NADP(H)-bi ...
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Biochemistry
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2000
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Bizouarn
Proton translocating nicotinam ...
Escherichia coli
Biochim. Biophys. Acta
1457
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2000
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Jeeves
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Solution structure of the NADP ...
Rhodospirillum rubrum
Biochim. Biophys. Acta
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248-257
2000
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Bragg
The presence of an aqueous cav ...
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Arch. Biochem. Biophys.
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2000
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Jeeves
Solution structure of the NADP ...
Rhodospirillum rubrum
Biochim. Biophys. Acta
1459
248-257
2000
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Fjellstrm
Mapping of residues in the NAD ...
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Hu
Site-directed mutagenesis of c ...
Escherichia coli
Biochemistry
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1999
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392665
Fjellstrom
Catalytic properties of hybrid ...
Escherichia coli, Rhodospirillum rubrum
Biochemistry
38
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1999
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Anderlund
Expression of the Escherichia ...
Escherichia coli
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1999
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Quirk
Structural changes in the reco ...
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Jackson
Structure and mechanism of pro ...
Escherichia coli, Homo sapiens, Rhodospirillum rubrum
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Meuller
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Grimley
Role of methionine-239, an ami ...
Rhodospirillum rubrum
Biochemistry
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Bizouarn
The pH dependences of reaction ...
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Glavas
Involvement of histidine-91 of ...
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Bizouarn
The involvement of NADP(H) bin ...
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1
-
-
-
-
-
-
-
5
8
-
-
1
-
-
5
1
-
1
-
6
8
2
1
3
2
-
-
-
-
1
-
-
1
1
1
1
-
-
-
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392599
Cotton
The coupling between protonmot ...
Rhodobacter capsulatus
Eur. J. Biochem.
182
593-603
1989
1
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-
-
-
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-
13
-
4
-
-
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1
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-
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-
-
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1
-
-
-
-
-
-
-
-
4
-
-
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1
-
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4
-
-
-
-
-
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13
-
4
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
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392618
Clarke
Purification and properties of ...
Escherichia coli, Escherichia coli W-6
Eur. J. Biochem.
149
517-523
1985
-
-
1
-
-
-
2
4
1
-
2
2
-
2
-
-
1
-
-
-
6
1
6
1
-
-
-
-
-
-
-
4
-
-
-
-
-
1
4
-
-
-
-
2
-
4
1
-
2
2
-
-
-
1
-
-
6
1
6
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
392619
Clarke
Cloning and expression of the ...
Escherichia coli, Escherichia coli MV-12
J. Bacteriol.
162
367-373
1985
-
-
1
-
-
-
-
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1
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2
2
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2
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-
-
-
-
-
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4
1
-
-
-
-
-
-
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4
-
-
-
-
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1
4
-
-
-
-
-
-
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1
-
2
2
-
-
-
-
-
-
-
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4
1
-
-
-
-
-
-
-
-
-
-
-
-
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-
392627
McFadden
Resolution and reconstitution ...
Rhodospirillum rubrum
Arch. Biochem. Biophys.
190
820-828
1978
-
-
-
-
-
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1
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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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-
-
-
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-
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4
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4
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-
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1
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1
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