BRENDA - Enzyme Database show
show all sequences of 2.7.1.86

Orientation and reactivity of NADH kinase in proteoliposomes

Iwahashi, Y.; Nakamura, T.; J. Biochem. 105, 922-926 (1989)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
acetate
maximal enhancement of activity, about 7fold is observed with 100 mM acetate, enzyme reconstituted in liposomes, maximal enhancement of solubilized enzyme with 400 mM acetate
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
phosphoenolpyruvate
20 mM, 63% inhibition, reconstituted enzyme. Solubilized enzyme is inhibited 55% by 30 mM
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.027
-
NADH
NADH kinase reconstituted in liposomes
Saccharomyces cerevisiae
0.105
-
NADH
solubilized enzyme form
Saccharomyces cerevisiae
0.133
-
ATP
NADH kinase reconstituted in liposomes
Saccharomyces cerevisiae
2.1
-
ATP
solubilized enzyme form
Saccharomyces cerevisiae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae X2181-1A
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + NADH
-
642065
Saccharomyces cerevisiae
ADP + NADPH
-
642065
Saccharomyces cerevisiae
?
ATP + NADH
-
642065
Saccharomyces cerevisiae X2181-1A
ADP + NADPH
-
642065
Saccharomyces cerevisiae X2181-1A
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
NADH kinase reconstituted in liposomes
Saccharomyces cerevisiae
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
acetate
maximal enhancement of activity, about 7fold is observed with 100 mM acetate, enzyme reconstituted in liposomes, maximal enhancement of solubilized enzyme with 400 mM acetate
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
phosphoenolpyruvate
20 mM, 63% inhibition, reconstituted enzyme. Solubilized enzyme is inhibited 55% by 30 mM
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.027
-
NADH
NADH kinase reconstituted in liposomes
Saccharomyces cerevisiae
0.105
-
NADH
solubilized enzyme form
Saccharomyces cerevisiae
0.133
-
ATP
NADH kinase reconstituted in liposomes
Saccharomyces cerevisiae
2.1
-
ATP
solubilized enzyme form
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + NADH
-
642065
Saccharomyces cerevisiae
ADP + NADPH
-
642065
Saccharomyces cerevisiae
?
ATP + NADH
-
642065
Saccharomyces cerevisiae X2181-1A
ADP + NADPH
-
642065
Saccharomyces cerevisiae X2181-1A
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
NADH kinase reconstituted in liposomes
Saccharomyces cerevisiae
Other publictions for EC 2.7.1.86
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)
721390
Lee
Effects of NADH kinase on NADP ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae CEN.PK2-1D
Appl. Microbiol. Biotechnol.
97
1561-1569
2013
-
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1
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1
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1
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1
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-
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721392
Lee
Engineering of NADPH regenerat ...
Saccharomyces cerevisiae
Appl. Microbiol. Biotechnol.
97
2761-2772
2013
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1
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1
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1
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721139
Shi
Role of mitochondrial NADH kin ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
Acta Biochim. Biophys. Sin.
43
989-995
2011
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-
-
-
-
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2
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24
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2
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2
2
-
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-
722719
Ando
Structural determinants of dis ...
Saccharomyces cerevisiae
J. Biol. Chem.
286
29984-29992
2011
-
-
1
1
3
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-
4
2
-
1
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3
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1
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2
1
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4
2
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1
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1
3
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4
2
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1
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1
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2
1
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4
2
-
-
-
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-
-
-
4
4
706395
Waller
Subcellular and tissue localiz ...
Arabidopsis thaliana
Planta
231
305-317
2010
-
-
1
-
-
-
-
-
1
-
-
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3
-
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3
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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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3
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1
-
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-
-
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-
1
-
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1
-
-
722693
Pain
Mitochondrial NADH kinase, Pos ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
J. Biol. Chem.
285
39409-39424
2010
-
-
1
-
-
-
-
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2
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59
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1
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1
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2
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2
2
-
-
-
695829
Hou
Impact of overexpressing NADH ...
Saccharomyces cerevisiae
Appl. Microbiol. Biotechnol.
82
909-919
2009
-
-
-
-
-
-
-
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2
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1
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4
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4
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4
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705593
Stuart
Transcriptional response to mi ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH925
Mitochondrion
9
211-221
2009
-
-
-
-
-
-
-
-
2
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3
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1
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1
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2
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2
-
-
-
-
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-
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1
1
-
-
-
691390
Kawai
Structure and function of NAD ...
Arabidopsis thaliana, Saccharomyces cerevisiae
Biosci. Biotechnol. Biochem.
72
919-930
2008
-
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-
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1
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2
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2
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4
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2
-
-
2
-
-
693998
Panagiotou
Overexpression of a novel endo ...
Aspergillus nidulans, Aspergillus nidulans CBS 513.88 / FGSC A1513
Metab. Eng.
11
31-39
2008
-
-
1
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1
2
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4
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706568
Panagiotou
-
Identification of NADH kinase ...
Fusarium oxysporum, Fusarium oxysporum F3
Process Biochem.
43
1114-1120
2008
-
-
-
-
-
-
8
2
-
1
2
-
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6
-
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1
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1
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4
1
1
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1
2
1
1
1
1
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1
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1
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8
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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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4
1
1
-
1
2
1
1
1
1
-
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674616
Bieganowski
Synthetic lethal and biochemic ...
Saccharomyces cerevisiae
J. Biol. Chem.
281
22439-22445
2006
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1
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2
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1
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1
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6
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1
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1
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1
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3
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6
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676516
Chai
NADK3, a novel cytoplasmic sou ...
Arabidopsis thaliana
Plant J.
47
665-674
2006
-
-
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-
-
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1
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2
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5
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1
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1
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1
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1
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5
-
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1
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-
657853
Turner
Identification, molecular clon ...
Arabidopsis thaliana
Biochem. J.
385
217-223
2005
-
-
1
-
-
-
2
6
2
4
2
-
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5
-
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1
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-
3
3
-
8
1
-
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-
1
-
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1
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2
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6
2
4
2
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1
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3
3
-
8
1
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1
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661696
Shi
Identification of ATP-NADH kin ...
Saccharomyces cerevisiae
FEBS J.
272
3337-3349
2005
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1
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3
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2
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1
1
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662376
Mori
Molecular conversion of NAD Ki ...
Micrococcus flavus, Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
280
24104-24112
2005
-
-
2
-
1
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8
-
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161
-
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2
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4
-
6
1
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2
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2
2
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1
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8
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4
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6
1
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676008
Berrin
Stress induces the expression ...
Arabidopsis thaliana
Mol. Genet. Genomics
273
10-19
2005
1
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1
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2
2
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1
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1
2
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2
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1
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1
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2
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2
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649040
Strand
POS5 gene of Saccharomyces cer ...
Saccharomyces cerevisiae
Eukaryot. Cell
2
809-820
2003
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1
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2
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1
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4
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3
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649041
Outten
A novel NADH kinase is the mit ...
Saccharomyces cerevisiae
EMBO J.
22
2015-2024
2003
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1
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2
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1
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2
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3
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642063
Ohno
-
Specific amplification of NADH ...
Pichia membranifaciens
Biosci. Biotechnol. Biochem.
58
976-977
1994
-
1
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1
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1
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1
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3
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642064
Iwahashi
Localization of the NADH kinas ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2181-1A
J. Biochem.
105
916-921
1989
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2
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3
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5
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642065
Iwahashi
Orientation and reactivity of ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2181-1A
J. Biochem.
105
922-926
1989
1
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1
4
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4
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2
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1
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4
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2
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1
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642066
Iwahashi
Characterization of NADH kinas ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2181-1A
J. Biochem.
105
588-593
1989
1
-
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6
2
1
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1
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5
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1
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1
2
4
1
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2
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1
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6
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2
1
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1
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1
2
4
1
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2
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1
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642062
Griffiths
Purification and properties of ...
Saccharomyces cerevisiae
J. Biol. Chem.
247
1473-1478
1972
1
-
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1
3
2
3
2
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1
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2
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1
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1
1
6
-
-
-
-
-
1
1
-
-
-
-
-
1
-
-
-
-
-
1
-
3
-
2
3
2
-
1
-
-
-
1
-
-
1
1
6
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-