BRENDA - Enzyme Database
show all sequences of 1.5.1.7

Determinants of substrate specificity for saccharopine dehydrogenase from Saccharomyces cerevisiae

Xu, H.; West, A.H.; Cook, P.F.; Biochemistry 46, 7625-7636 (2007)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
2',3'-cyclic NADP
-
Saccharomyces cerevisiae
2',3'-cyclic NADP+
-
Saccharomyces cerevisiae
adenosine
-
Saccharomyces cerevisiae
adipate
-
Saccharomyces cerevisiae
ADP
-
Saccharomyces cerevisiae
ADP-ribose
-
Saccharomyces cerevisiae
alpha-ketoadipate
-
Saccharomyces cerevisiae
alpha-ketoglutarate
-
Saccharomyces cerevisiae
alpha-ketoisovalerate
-
Saccharomyces cerevisiae
alpha-ketomalonate
-
Saccharomyces cerevisiae
alpha-ketopimelate
-
Saccharomyces cerevisiae
AMP
-
Saccharomyces cerevisiae
D-Lysine
-
Saccharomyces cerevisiae
Glutarate
-
Saccharomyces cerevisiae
L-arginine
-
Saccharomyces cerevisiae
L-glutamine
-
Saccharomyces cerevisiae
L-isoleucine
-
Saccharomyces cerevisiae
L-leucine
dead-end inhibition by L-leucine is uncompetitive versus NADPH
Saccharomyces cerevisiae
L-lysine
-
Saccharomyces cerevisiae
L-methionine
-
Saccharomyces cerevisiae
L-norvaline
-
Saccharomyces cerevisiae
L-ornithine
-
Saccharomyces cerevisiae
L-valine
-
Saccharomyces cerevisiae
malonate
-
Saccharomyces cerevisiae
additional information
not inhibited by L-asparagine at pH 7.0
Saccharomyces cerevisiae
NAD+
-
Saccharomyces cerevisiae
NADH
-
Saccharomyces cerevisiae
NADP+
NADP+ is competitive versus NADPH when NADPH serves as the coenzyme
Saccharomyces cerevisiae
NMN
-
Saccharomyces cerevisiae
oxalate
-
Saccharomyces cerevisiae
oxaloacetate
-
Saccharomyces cerevisiae
oxalylglycine
-
Saccharomyces cerevisiae
pyridine 2,3-dicarboxylate
-
Saccharomyces cerevisiae
Pyridine 2,4-dicarboxylate
-
Saccharomyces cerevisiae
succinate
-
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.11
-
2-oxoglutarate
at pH 7.0
Saccharomyces cerevisiae
4.1
-
pyruvate
at pH 7.0
Saccharomyces cerevisiae
5.3
-
alpha-ketoadipate
at pH 7.0
Saccharomyces cerevisiae
6.4
-
glyoxylate
at pH 7.0
Saccharomyces cerevisiae
24
-
alpha-ketomalonate
at pH 7.0
Saccharomyces cerevisiae
94
-
alpha-ketovalerate
at pH 7.0
Saccharomyces cerevisiae
153
-
alpha-Ketobutyrate
at pH 7.0
Saccharomyces cerevisiae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-lysine + alpha-ketoadipate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
L-lysine + alpha-ketobutyrate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
L-lysine + alpha-ketomalonate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
L-lysine + alpha-ketovalerate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
L-lysine + glyoxylate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
L-lysine + pyruvate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
additional information
3-acetylpyridine adenine dinucleotide, 3-pyridinealdehyde adenine dinucleotide, and thionicotinamide adenine dinucleotide can serve as a substrate in the oxidative deamination reaction, as can glyoxylate, pyruvate, alpha-ketobutyrate, alpha-ketovalerate, alpha-ketomalonate, and alpha-ketoadipate in the reverse reaction
685171
Saccharomyces cerevisiae
?
-
-
-
-
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
the enzyme is specific for L-lysine
685171
Saccharomyces cerevisiae
L-lysine + 2-oxoglutarate + NADH + H+
-
-
-
r
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Saccharomyces cerevisiae
NADH
-
Saccharomyces cerevisiae
NADPH
NADPH can substitute for NADH
Saccharomyces cerevisiae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.018
-
NADH
at pH 7.0
Saccharomyces cerevisiae
0.055
-
AMP
at pH 7.0
Saccharomyces cerevisiae
0.093
-
ADP
at pH 7.0
Saccharomyces cerevisiae
0.1
-
oxalylglycine
at pH 7.0
Saccharomyces cerevisiae
0.125
-
L-leucine
at pH 6.0
Saccharomyces cerevisiae
0.29
-
ADP-ribose
at pH 7.0
Saccharomyces cerevisiae
0.42
-
adenosine
at pH 7.0
Saccharomyces cerevisiae
0.6
-
alpha-ketoglutarate
at pH 7.0
Saccharomyces cerevisiae
1
-
Glutarate
at pH 7.0
Saccharomyces cerevisiae
1.1
-
L-lysine
at pH 7.0
Saccharomyces cerevisiae
1.1
-
Pyridine 2,4-dicarboxylate
at pH 7.0
Saccharomyces cerevisiae
1.13
-
L-norvaline
at pH 7.0
Saccharomyces cerevisiae
1.2
-
NADP
at pH 7.0
Saccharomyces cerevisiae
1.5
-
2',3'-cyclic NADP
at pH 7.0
Saccharomyces cerevisiae
1.56
-
NAD+
at pH 7.0
Saccharomyces cerevisiae
3.12
-
L-methionine
at pH 7.0
Saccharomyces cerevisiae
3.5
-
NADP+
at pH 7.0
Saccharomyces cerevisiae
5
-
L-ornithine
at pH 7.0
Saccharomyces cerevisiae
5.3
-
alpha-ketoadipate
at pH 7.0
Saccharomyces cerevisiae
5.5
-
D-Lysine
at pH 7.0
Saccharomyces cerevisiae
5.6
-
L-leucine
at pH 7.0
Saccharomyces cerevisiae
6.4
-
oxaloacetate
at pH 7.0
Saccharomyces cerevisiae
7.2
-
NMN
at pH 7.0
Saccharomyces cerevisiae
16
-
L-glutamine
at pH 7.0
Saccharomyces cerevisiae
16.4
-
L-arginine
at pH 7.0
Saccharomyces cerevisiae
18
-
alpha-ketopimelate
at pH 7.0
Saccharomyces cerevisiae
18.3
-
pyridine 2,3-dicarboxylate
at pH 7.0
Saccharomyces cerevisiae
21
-
succinate
at pH 7.0
Saccharomyces cerevisiae
22
-
L-isoleucine
at pH 7.0
Saccharomyces cerevisiae
24
-
alpha-ketomalonate
at pH 7.0
Saccharomyces cerevisiae
24
-
malonate
at pH 7.0
Saccharomyces cerevisiae
36
-
alpha-ketoisovalerate
at pH 7.0
Saccharomyces cerevisiae
36
-
oxalate
at pH 7.0
Saccharomyces cerevisiae
50
-
adipate
at pH 7.0
Saccharomyces cerevisiae
140
-
L-valine
at pH 7.0
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Saccharomyces cerevisiae
NADH
-
Saccharomyces cerevisiae
NADPH
NADPH can substitute for NADH
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2',3'-cyclic NADP
-
Saccharomyces cerevisiae
2',3'-cyclic NADP+
-
Saccharomyces cerevisiae
adenosine
-
Saccharomyces cerevisiae
adipate
-
Saccharomyces cerevisiae
ADP
-
Saccharomyces cerevisiae
ADP-ribose
-
Saccharomyces cerevisiae
alpha-ketoadipate
-
Saccharomyces cerevisiae
alpha-ketoglutarate
-
Saccharomyces cerevisiae
alpha-ketoisovalerate
-
Saccharomyces cerevisiae
alpha-ketomalonate
-
Saccharomyces cerevisiae
alpha-ketopimelate
-
Saccharomyces cerevisiae
AMP
-
Saccharomyces cerevisiae
D-Lysine
-
Saccharomyces cerevisiae
Glutarate
-
Saccharomyces cerevisiae
L-arginine
-
Saccharomyces cerevisiae
L-glutamine
-
Saccharomyces cerevisiae
L-isoleucine
-
Saccharomyces cerevisiae
L-leucine
dead-end inhibition by L-leucine is uncompetitive versus NADPH
Saccharomyces cerevisiae
L-lysine
-
Saccharomyces cerevisiae
L-methionine
-
Saccharomyces cerevisiae
L-norvaline
-
Saccharomyces cerevisiae
L-ornithine
-
Saccharomyces cerevisiae
L-valine
-
Saccharomyces cerevisiae
malonate
-
Saccharomyces cerevisiae
additional information
not inhibited by L-asparagine at pH 7.0
Saccharomyces cerevisiae
NAD+
-
Saccharomyces cerevisiae
NADH
-
Saccharomyces cerevisiae
NADP+
NADP+ is competitive versus NADPH when NADPH serves as the coenzyme
Saccharomyces cerevisiae
NMN
-
Saccharomyces cerevisiae
oxalate
-
Saccharomyces cerevisiae
oxaloacetate
-
Saccharomyces cerevisiae
oxalylglycine
-
Saccharomyces cerevisiae
pyridine 2,3-dicarboxylate
-
Saccharomyces cerevisiae
Pyridine 2,4-dicarboxylate
-
Saccharomyces cerevisiae
succinate
-
Saccharomyces cerevisiae
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.018
-
NADH
at pH 7.0
Saccharomyces cerevisiae
0.055
-
AMP
at pH 7.0
Saccharomyces cerevisiae
0.093
-
ADP
at pH 7.0
Saccharomyces cerevisiae
0.1
-
oxalylglycine
at pH 7.0
Saccharomyces cerevisiae
0.125
-
L-leucine
at pH 6.0
Saccharomyces cerevisiae
0.29
-
ADP-ribose
at pH 7.0
Saccharomyces cerevisiae
0.42
-
adenosine
at pH 7.0
Saccharomyces cerevisiae
0.6
-
alpha-ketoglutarate
at pH 7.0
Saccharomyces cerevisiae
1
-
Glutarate
at pH 7.0
Saccharomyces cerevisiae
1.1
-
L-lysine
at pH 7.0
Saccharomyces cerevisiae
1.1
-
Pyridine 2,4-dicarboxylate
at pH 7.0
Saccharomyces cerevisiae
1.13
-
L-norvaline
at pH 7.0
Saccharomyces cerevisiae
1.2
-
NADP
at pH 7.0
Saccharomyces cerevisiae
1.5
-
2',3'-cyclic NADP
at pH 7.0
Saccharomyces cerevisiae
1.56
-
NAD+
at pH 7.0
Saccharomyces cerevisiae
3.12
-
L-methionine
at pH 7.0
Saccharomyces cerevisiae
3.5
-
NADP+
at pH 7.0
Saccharomyces cerevisiae
5
-
L-ornithine
at pH 7.0
Saccharomyces cerevisiae
5.3
-
alpha-ketoadipate
at pH 7.0
Saccharomyces cerevisiae
5.5
-
D-Lysine
at pH 7.0
Saccharomyces cerevisiae
5.6
-
L-leucine
at pH 7.0
Saccharomyces cerevisiae
6.4
-
oxaloacetate
at pH 7.0
Saccharomyces cerevisiae
7.2
-
NMN
at pH 7.0
Saccharomyces cerevisiae
16
-
L-glutamine
at pH 7.0
Saccharomyces cerevisiae
16.4
-
L-arginine
at pH 7.0
Saccharomyces cerevisiae
18
-
alpha-ketopimelate
at pH 7.0
Saccharomyces cerevisiae
18.3
-
pyridine 2,3-dicarboxylate
at pH 7.0
Saccharomyces cerevisiae
21
-
succinate
at pH 7.0
Saccharomyces cerevisiae
22
-
L-isoleucine
at pH 7.0
Saccharomyces cerevisiae
24
-
alpha-ketomalonate
at pH 7.0
Saccharomyces cerevisiae
24
-
malonate
at pH 7.0
Saccharomyces cerevisiae
36
-
alpha-ketoisovalerate
at pH 7.0
Saccharomyces cerevisiae
36
-
oxalate
at pH 7.0
Saccharomyces cerevisiae
50
-
adipate
at pH 7.0
Saccharomyces cerevisiae
140
-
L-valine
at pH 7.0
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.11
-
2-oxoglutarate
at pH 7.0
Saccharomyces cerevisiae
4.1
-
pyruvate
at pH 7.0
Saccharomyces cerevisiae
5.3
-
alpha-ketoadipate
at pH 7.0
Saccharomyces cerevisiae
6.4
-
glyoxylate
at pH 7.0
Saccharomyces cerevisiae
24
-
alpha-ketomalonate
at pH 7.0
Saccharomyces cerevisiae
94
-
alpha-ketovalerate
at pH 7.0
Saccharomyces cerevisiae
153
-
alpha-Ketobutyrate
at pH 7.0
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-lysine + alpha-ketoadipate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
L-lysine + alpha-ketobutyrate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
L-lysine + alpha-ketomalonate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
L-lysine + alpha-ketovalerate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
L-lysine + glyoxylate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
L-lysine + pyruvate + NADH
-
685171
Saccharomyces cerevisiae
?
-
-
-
?
additional information
3-acetylpyridine adenine dinucleotide, 3-pyridinealdehyde adenine dinucleotide, and thionicotinamide adenine dinucleotide can serve as a substrate in the oxidative deamination reaction, as can glyoxylate, pyruvate, alpha-ketobutyrate, alpha-ketovalerate, alpha-ketomalonate, and alpha-ketoadipate in the reverse reaction
685171
Saccharomyces cerevisiae
?
-
-
-
-
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
the enzyme is specific for L-lysine
685171
Saccharomyces cerevisiae
L-lysine + 2-oxoglutarate + NADH + H+
-
-
-
r
Other publictions for EC 1.5.1.7
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)
725754
Sheng
Theoretical study on the proto ...
Saccharomyces cerevisiae
J. Mol. Graph. Model.
44
17-25
2013
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
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-
-
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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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1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
724121
Kumar
Supporting role of lysine 13 a ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
522
57-61
2012
-
-
1
-
2
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
1
1
-
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-
-
-
-
-
1
-
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1
1
-
2
-
-
-
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-
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-
-
1
-
-
-
1
-
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-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
724358
Kumar
Evidence in support of lysine ...
Saccharomyces cerevisiae
Biochemistry
51
857-866
2012
-
-
1
1
3
-
-
8
-
-
-
1
-
1
-
-
1
-
-
-
-
1
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
1
3
-
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-
-
8
-
-
-
1
-
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-
1
-
-
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
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-
724117
Bobyk
The oxidation state of active ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
513
71-80
2011
-
-
1
-
2
-
1
14
-
-
1
2
-
1
-
-
1
-
-
-
-
-
2
1
-
-
-
-
1
-
-
1
3
-
-
-
-
1
1
-
2
-
-
1
3
14
-
-
1
2
-
-
-
1
-
-
-
-
2
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
712442
Ekanayake
Glutamates 78 and 122 in the a ...
Saccharomyces cerevisiae
J. Biol. Chem.
285
20756-20768
2010
-
-
-
-
6
-
3
27
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
6
-
-
3
7
27
-
-
-
-
-
-
-
-
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-
-
-
2
-
-
-
-
-
-
-
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-
672274
Xu
A proposed proton shuttle mech ...
Saccharomyces cerevisiae
Biochemistry
46
871-882
2007
-
-
-
-
-
-
4
1
-
-
-
-
-
1
-
-
-
1
-
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-
-
1
-
-
-
-
-
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-
1
-
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1
-
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-
-
4
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685104
Andi
Crystal structures of ligand-b ...
Saccharomyces cerevisiae
Biochemistry
46
12512-12521
2007
-
-
1
1
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
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-
1
1
1
-
-
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-
-
-
-
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-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685171
Xu
Determinants of substrate spec ...
Saccharomyces cerevisiae
Biochemistry
46
7625-7636
2007
-
-
-
-
-
-
35
7
-
-
-
-
-
1
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
3
35
-
-
-
-
-
3
-
-
-
-
35
35
7
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688383
Burk
Structural studies of the fina ...
Saccharomyces cerevisiae
J. Mol. Biol.
373
745-754
2007
-
1
1
1
-
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-
-
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-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
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-
-
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-
-
-
-
-
-
-
672073
Xu
Overall kinetic mechanism of s ...
Saccharomyces cerevisiae
Biochemistry
45
12156-12166
2006
-
-
-
-
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-
4
4
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
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4
2
4
-
-
-
-
-
-
-
-
-
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Schmidt
Regulation of the lysine biosy ...
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Lysine biosynthesis pathway an ...
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Fujioka
Chemical mechanism of saccharo ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
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396556
Fujioka
Active-site residues of saccha ...
Saccharomyces cerevisiae
Biochem. Soc. Trans.
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1981
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396557
Fujioka
Role of arginine residue in sa ...
Saccharomyces cerevisiae
Biochemistry
20
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1981
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396558
Ogawa
The reaction of pyridoxal 5-ph ...
Saccharomyces cerevisiae
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1980
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396559
Fujioka
The inactivation of saccharopi ...
Saccharomyces cerevisiae
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396560
Fujioka
Stereospecificity of hydrogen ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
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1979
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396561
Ogawa
Chemical modification of the a ...
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396562
Hanke
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Charakterisierung der Saccharo ...
Phycomyces blakesleeanus
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1979
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396563
Sugimoto
The reaction of pyruvate with ...
Saccharomyces cerevisiae
Eur. J. Biochem.
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1978
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Ogawa
Purification and characterizat ...
Saccharomyces cerevisiae
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1978
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396565
Fujioka
Saccharopine dehydrogenase. Su ...
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Fujioka
Saccharopine dehydrogenase. A ...
Saccharomyces cerevisiae
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Fujioka
Saccharopine dehydrogenase. In ...
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396569
Broquist
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Saccharopine dehydrogenase ...
Saccharomyces cerevisiae
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1971
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Fujioka
A kinetic study of saccharopin ...
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Saunders
Saccharopine, an intermediate ...
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