BRENDA - Enzyme Database show
show all sequences of 1.1.5.4

Cofactor requirements of the L-malate dehydrogenase of Pseudomonas ovalis Chester

Phizackerley, P.J.; Francis, M.J.; Biochem. J. 101, 524-535 (1966)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Phospholipid
the nature of the phospholipid required to activate the enzyme depends on the nature of the quinone used in the assay system. When 2-methyl-1,4-naphthoquinone is used, a wide variety of phospholipids, including all these isolated from the organism, will activate the enzyme, but when coenzyme Q9 is used the phospholipid specificity of the enzyme is much more restricted, and the most effective activator is the unsaturated phosphatidylethanolamine isolated from the organism
Pseudomonas putida
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0024
-
ubiquinone 9
pH 7.0, 20°C
Pseudomonas putida
0.45
-
(S)-malate
pH 7.0, 20°C
Pseudomonas putida
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
bound to the cell-wall membrane
Pseudomonas putida
16020
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
Chester
-
Pseudomonas putida Chester
-
Chester
-
Purification (Commentary)
Commentary
Organism
partial
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + oxidized 2,6-dichlorophenol indophenol
-
696072
Pseudomonas putida
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
?
(S)-malate + oxidized 2,6-dichlorophenol indophenol
-
696072
Pseudomonas putida Chester
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
?
(S)-malate + ubiquinone-9
in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to these obtained with 2,6-dichlorophenol-indophenol as terminal acceptor
696072
Pseudomonas putida
oxaloacetate + ubiquinol-9
-
-
-
?
(S)-malate + ubiquinone-9
in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to these obtained with 2,6-dichlorophenol-indophenol as terminal acceptor
696072
Pseudomonas putida Chester
oxaloacetate + ubiquinol-9
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Pseudomonas putida
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Pseudomonas putida
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
triple cofactor requirement for FAD, quinone and phospholipid. The formation of reduced forms of FAD is not detected, but in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to the rate obtained with 2,6-dichlorophenol-indophenol as terminal acceptor. Km-value for FAD is 0.0004 mM
Pseudomonas putida
menadione
triple cofactor requirement for FAD, quinone and phospholipid. Maximum rate when phosphatidylethanolamine is added to the enzyme before the quinone
Pseudomonas putida
ubiquinone-0
triple cofactor requirement for FAD, quinone and phospholipid. Maximum activation rate when phosphatidylethanolamine is added to the enzyme before the quinone
Pseudomonas putida
ubiquinone-9
triple cofactor requirement for FAD, quinone and phospholipid. The formation of reduced forms of FAD is not detected, but in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to the rate obtained with 2,6-dichlorophenol-indophenol as terminal acceptor. The quinone is identified as ubiquinone 9. Km-value for ubiquinone 9 is 0.0024 mM
Pseudomonas putida
vitamin K1
with both vitamin K1 and ubiquinone-9, maximum rates are obtained by exposing the enzyme to phospholipid and quinone simultaneously, but, when phosphatidylethanolamine is added to the enzyme before either of these quinones, the rates are much lower
Pseudomonas putida
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Phospholipid
the nature of the phospholipid required to activate the enzyme depends on the nature of the quinone used in the assay system. When 2-methyl-1,4-naphthoquinone is used, a wide variety of phospholipids, including all these isolated from the organism, will activate the enzyme, but when coenzyme Q9 is used the phospholipid specificity of the enzyme is much more restricted, and the most effective activator is the unsaturated phosphatidylethanolamine isolated from the organism
Pseudomonas putida
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
triple cofactor requirement for FAD, quinone and phospholipid. The formation of reduced forms of FAD is not detected, but in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to the rate obtained with 2,6-dichlorophenol-indophenol as terminal acceptor. Km-value for FAD is 0.0004 mM
Pseudomonas putida
menadione
triple cofactor requirement for FAD, quinone and phospholipid. Maximum rate when phosphatidylethanolamine is added to the enzyme before the quinone
Pseudomonas putida
ubiquinone-0
triple cofactor requirement for FAD, quinone and phospholipid. Maximum activation rate when phosphatidylethanolamine is added to the enzyme before the quinone
Pseudomonas putida
ubiquinone-9
triple cofactor requirement for FAD, quinone and phospholipid. The formation of reduced forms of FAD is not detected, but in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to the rate obtained with 2,6-dichlorophenol-indophenol as terminal acceptor. The quinone is identified as ubiquinone 9. Km-value for ubiquinone 9 is 0.0024 mM
Pseudomonas putida
vitamin K1
with both vitamin K1 and ubiquinone-9, maximum rates are obtained by exposing the enzyme to phospholipid and quinone simultaneously, but, when phosphatidylethanolamine is added to the enzyme before either of these quinones, the rates are much lower
Pseudomonas putida
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0024
-
ubiquinone 9
pH 7.0, 20°C
Pseudomonas putida
0.45
-
(S)-malate
pH 7.0, 20°C
Pseudomonas putida
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
bound to the cell-wall membrane
Pseudomonas putida
16020
-
Purification (Commentary) (protein specific)
Commentary
Organism
partial
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + oxidized 2,6-dichlorophenol indophenol
-
696072
Pseudomonas putida
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
?
(S)-malate + oxidized 2,6-dichlorophenol indophenol
-
696072
Pseudomonas putida Chester
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
?
(S)-malate + ubiquinone-9
in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to these obtained with 2,6-dichlorophenol-indophenol as terminal acceptor
696072
Pseudomonas putida
oxaloacetate + ubiquinol-9
-
-
-
?
(S)-malate + ubiquinone-9
in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to these obtained with 2,6-dichlorophenol-indophenol as terminal acceptor
696072
Pseudomonas putida Chester
oxaloacetate + ubiquinol-9
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Pseudomonas putida
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Pseudomonas putida
Other publictions for EC 1.1.5.4
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)
722575
Kabashima
Purification and characterizat ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) PS3
J. Bioenerg. Biomembr.
45
131-136
2013
-
-
1
-
-
-
8
-
-
-
2
2
-
17
-
-
-
-
-
-
-
-
11
1
1
-
-
-
1
-
-
4
-
-
-
-
-
1
4
-
-
-
-
8
-
-
-
-
2
2
-
-
-
-
-
-
-
-
11
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
721563
Igeno
Metabolic adaptation of Pseudo ...
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes CECT 5344
Biochem. Soc. Trans.
39
1849-1853
2011
-
-
-
-
-
-
-
-
-
-
-
2
-
3
-
-
-
-
-
1
-
-
2
-
-
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-
-
-
-
-
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-
2
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-
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-
-
1
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-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
723124
Luque-Almagro
Cyanide degradation by Pseudom ...
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes CECT 5344
Microbiology
157
739-746
2011
-
-
-
-
-
-
-
-
1
-
-
2
-
6
-
-
-
-
-
-
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4
-
1
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1
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2
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2
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-
1
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2
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-
-
-
-
4
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
698612
Mellgren
Mqo, a tricarboxylic acid cycl ...
Pseudomonas syringae
J. Bacteriol.
191
3132-3141
2009
-
-
-
-
-
-
-
-
-
-
-
1
-
9
-
-
-
-
-
-
-
-
1
-
-
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-
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1
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-
-
-
-
-
-
-
-
-
-
698670
Mogi
Polymyxin B identified as an i ...
Mycolicibacterium smegmatis
J. Biochem.
146
491-499
2009
-
-
-
-
-
-
3
2
-
-
-
-
-
3
-
-
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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
3
1
2
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1
-
1
-
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1
-
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-
-
-
-
-
-
-
687185
Fleige
Localisation of gluconeogenesi ...
Toxoplasma gondii
Int. J. Parasitol.
38
1121-1132
2008
-
-
1
-
-
-
-
-
1
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-
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1
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679906
Diaz-Perez
Identification of the aceA gen ...
Pseudomonas aeruginosa
FEMS Microbiol. Lett.
269
309-316
2007
-
-
-
-
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1
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1
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-
696805
Mitsuhashi
Disruption of malate:quinone o ...
Corynebacterium glutamicum
Biosci. Biotechnol. Biochem.
70
2803-2806
2006
-
1
-
-
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-
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1
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2
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1
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1
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-
-
-
673714
Foerster-Fromme
Malate:quinone oxidoreductase ...
Pseudomonas aeruginosa, Pseudomonas citronellolis
FEMS Microbiol. Lett.
246
25-31
2005
-
-
2
-
2
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2
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2
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6
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4
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2
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2
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2
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2
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2
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4
-
2
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2
-
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-
287737
Kather
Another unusual type of citric ...
Helicobacter pylori
J. Bacteriol.
182
3204-3209
2000
-
-
1
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1
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1
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6
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2
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287738
Molenaar
Functions of the membrane-asso ...
Corynebacterium glutamicum
J. Bacteriol.
182
6884-6891
2000
-
-
-
-
-
-
-
-
3
-
-
1
-
3
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1
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3
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1
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698558
van der Rest
Functions of the membrane-asso ...
Escherichia coli
J. Bacteriol.
182
6892-6899
2000
-
-
-
-
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-
-
-
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1
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1
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287733
Molenaar
Biochemical and genetic charac ...
Corynebacterium glutamicum
Eur. J. Biochem.
254
395-403
1998
6
-
1
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1
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2
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1
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6
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1
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3
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1
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6
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1
1
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1
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1
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1
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2
3
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287734
Imai
FAD-dependent malate dehydroge ...
Mycobacterium sp., Mycobacterium sp. Takeo
Biochim. Biophys. Acta
523
37-46
1978
2
-
-
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1
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1
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287730
Imai
-
A phospholipid-requiring enzym ...
Mycolicibacterium phlei
J. Biol. Chem.
248
7487-7494
1973
1
-
-
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3
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1
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1
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1
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1
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287619
Phizackerley
-
Malate dehydrogenase (FAD-link ...
Pseudomonas putida, Pseudomonas putida Chester
Methods Enzymol.
13
135-140
1969
1
-
-
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1
3
1
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4
-
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1
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1
2
11
-
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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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3
1
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1
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1
2
11
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
696072
Phizackerley
Cofactor requirements of the L ...
Pseudomonas putida, Pseudomonas putida Chester
Biochem. J.
101
524-535
1966
1
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2
1
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1
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4
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1
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5
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5
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1
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