BRENDA - Enzyme Database show
show all sequences of 1.2.1.31

delta1-piperideine-6-carboxylic acid and alpha-aminoadipic acid delta-semialdehyde

Rodwell, V.W.; Methods Enzymol. 17B, 188-199 (1971)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
ATP
30% inhibition at 1 mM
Pseudomonas putida
Carbonyl reagents
e.g.: hydroxylamine, KCN, in the presence of substrate
Pseudomonas putida
HSO3-
in presence of substrate
Pseudomonas putida
hydroxylamine
in presence of substrate
Pseudomonas putida
KCN
in presence of substrate
Pseudomonas putida
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
DELTA1-piperidine 6-carboxylate
-
Pseudomonas putida
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
no metal cofactor required
Pseudomonas putida
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-2-aminoadipate-semialdehyde + NAD+
Pseudomonas putida
degradative enzyme
L-2-aminoadipate + NADH
-
Pseudomonas putida
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Purification (Commentary)
Commentary
Organism
using protamine sulfate treatment, ammonium sulfate fractionation and treatment with calcium phosphate gel
Pseudomonas putida
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
4.9
-
after purification, gel fraction
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD+ + H2O
-
288194
Pseudomonas putida
L-2-aminoadipate + NADH
-
288194
Pseudomonas putida
ir
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
-
288194
Pseudomonas putida
L-2-aminoadipate + NADH
-
288194
Pseudomonas putida
ir
L-2-aminoadipate-semialdehyde + NAD+
degradative enzyme
288194
Pseudomonas putida
L-2-aminoadipate + NADH
-
288194
Pseudomonas putida
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.1
-
L-alpha-aminoadipate-semialdehyde reduction
Pseudomonas putida
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Pseudomonas putida
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Pseudomonas putida
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ATP
30% inhibition at 1 mM
Pseudomonas putida
Carbonyl reagents
e.g.: hydroxylamine, KCN, in the presence of substrate
Pseudomonas putida
HSO3-
in presence of substrate
Pseudomonas putida
hydroxylamine
in presence of substrate
Pseudomonas putida
KCN
in presence of substrate
Pseudomonas putida
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
DELTA1-piperidine 6-carboxylate
-
Pseudomonas putida
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
no metal cofactor required
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-2-aminoadipate-semialdehyde + NAD+
Pseudomonas putida
degradative enzyme
L-2-aminoadipate + NADH
-
Pseudomonas putida
?
Purification (Commentary) (protein specific)
Commentary
Organism
using protamine sulfate treatment, ammonium sulfate fractionation and treatment with calcium phosphate gel
Pseudomonas putida
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
4.9
-
after purification, gel fraction
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD+ + H2O
-
288194
Pseudomonas putida
L-2-aminoadipate + NADH
-
288194
Pseudomonas putida
ir
L-2-aminoadipate 6-semialdehyde + NAD+ + H2O
-
288194
Pseudomonas putida
L-2-aminoadipate + NADH
-
288194
Pseudomonas putida
ir
L-2-aminoadipate-semialdehyde + NAD+
degradative enzyme
288194
Pseudomonas putida
L-2-aminoadipate + NADH
-
288194
Pseudomonas putida
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.1
-
L-alpha-aminoadipate-semialdehyde reduction
Pseudomonas putida
Other publictions for EC 1.2.1.31
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)
712017
Struys
Metabolism of lysine in alpha- ...
Homo sapiens
FEBS Lett.
584
181-186
2010
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1
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1
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1
1
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-
690142
Alnouti
Tissue distribution, ontogeny, ...
Mus musculus
Toxicol. Sci.
101
51-64
2008
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2
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1
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15
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1
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1
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1
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2
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15
-
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1
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693281
Isobe
Analysis of selective producti ...
Rhodococcus sp., Rhodococcus sp. AIU Z-35-1
J. Biosci. Bioeng.
105
152-156
2008
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2
2
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4
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1
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1
1
1
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1
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2
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2
2
2
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1
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1
-
2
-
1
1
1
-
1
1
1
-
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-
-
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-
689379
Marchitti
Neurotoxicity and metabolism o ...
Homo sapiens
Pharmacol. Rev.
59
125-150
2007
-
-
-
-
-
-
1
-
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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1
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1
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1
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2
-
-
1
-
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-
-
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-
-
-
-
694191
Struys
Alpha-aminoadipic semialdehyde ...
Homo sapiens
Mol. Genet. Metab.
91
405
2007
-
1
-
-
1
-
-
-
-
-
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-
-
1
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1
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1
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675897
Wang
Cloning and characterization o ...
Homo sapiens
Mol. Biol. Rep.
32
47-53
2005
-
-
1
-
-
-
-
-
-
-
-
1
-
3
-
-
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-
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24
-
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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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24
-
-
1
-
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-
676142
Felton
Biochemistry: role of PQQ as a ...
Mammalia
Nature
433
E10
2005
-
-
-
-
-
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-
-
-
-
-
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1
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1
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1
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676143
Rucker
Biochemistry: Is pyrroloquinol ...
Mus musculus, Rattus norvegicus
Nature
433
E10-1
2005
-
-
-
-
-
-
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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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657420
Guo
Posttranslational activation, ...
Schizosaccharomyces pombe
Yeast
21
1279-1288
2004
1
-
1
-
16
-
-
-
-
-
-
1
-
7
-
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1
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2
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1
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1
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1
1
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16
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1
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1
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-
2
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-
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-
-
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-
656194
Hijarrubia
Domain structure characterizat ...
Penicillium chrysogenum
J. Biol. Chem.
278
8250-8256
2003
1
-
-
-
-
-
1
3
-
2
2
-
-
2
-
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1
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1
1
2
1
1
-
3
1
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
-
2
2
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1
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1
1
2
1
1
-
3
1
1
-
-
-
-
-
-
-
-
-
657417
Alberti
LYS2 gene and its mutation in ...
Kluyveromyces lactis
Yeast
20
1171-1175
2003
-
-
1
-
-
-
-
-
-
-
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1
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1
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654293
Hijarrubia
Nitrate regulation of alpha-am ...
Acremonium chrysogenum, Penicillium chrysogenum
Appl. Microbiol. Biotechnol.
59
270-277
2002
-
-
-
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2
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2
-
6
-
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2
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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
-
-
4
-
-
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-
288202
Praphanphoj
Identification of the.alpha-Am ...
Homo sapiens
Mol. Genet. Metab.
72
336-342
2001
-
-
1
-
-
-
-
-
-
-
-
-
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1
-
1
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-
-
16
-
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-
1
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1
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16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288203
Hijarrubia
Characterization of the lys2 g ...
Acremonium chrysogenum
Mol. Gen. Genet.
264
755-762
2001
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
1
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1
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3
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2
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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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3
-
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288204
Guo
Novel posttranslational activa ...
Candida albicans
J. Bacteriol.
183
7120-7125
2001
-
-
1
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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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1
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2
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1
-
1
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288201
Ehmann
Lysine biosynthesis in Sacchar ...
Saccharomyces cerevisiae
Biochemistry
38
6171-6177
1999
-
-
1
-
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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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3
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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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2
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3
-
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1
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288199
Suvarna
Molecular analysis of the LYS2 ...
Candida albicans, Saccharomyces cerevisiae
Curr. Genet.
33
268-275
1998
-
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1
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3
-
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2
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2
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2
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288200
Casqueiro
Characterization of the lys2 g ...
Penicillium chrysogenum
Mol. Gen. Genet.
259
549-556
1998
-
-
1
-
-
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-
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1
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1
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1
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288198
Ford
Molecular properties of the ly ...
Saccharomyces cerevisiae, Schizosaccharomyces pombe
Curr. Genet.
28
131-137
1995
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-
1
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2
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2
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1
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1
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288185
Schmidt
Inhibition of alpha-aminoadipa ...
Blastobotrys adeninivorans
FEMS Microbiol. Lett.
70
41-44
1990
-
-
-
-
-
-
3
4
-
1
-
2
-
2
-
-
1
-
-
-
1
-
4
-
-
-
-
-
1
-
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1
3
-
-
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-
-
1
-
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3
3
4
-
1
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2
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1
-
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1
-
4
-
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-
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1
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-
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288186
Chang
L-pipecolic acid metabolism in ...
Homo sapiens
Biochim. Biophys. Acta
1038
300-305
1990
3
-
-
-
-
-
5
2
1
3
-
-
-
3
-
-
-
-
-
2
1
1
1
-
-
-
-
-
1
-
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1
-
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-
3
-
-
1
-
-
-
-
5
-
2
1
3
-
-
-
-
-
-
-
2
1
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
288187
Samsonova
Auxotrophic mutants of the yea ...
Blastobotrys adeninivorans
J. Basic Microbiol.
29
675-683
1989
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288188
Schmidt
-
Isolation and characterization ...
Candida maltosa, Meyerozyma guilliermondii
FEMS Microbiol. Lett.
60
201-204
1989
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6
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288189
Storts
Properties of revertants of ly ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
161
182-186
1989
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288190
Ye
Lysine biosynthesis pathway an ...
Schizosaccharomyces pombe
J. Bacteriol.
170
5968-5970
1988
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288196
Fleig
Construction of LYS2 cartridge ...
Saccharomyces cerevisiae
Gene
46
237-245
1986
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1
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288197
Barnes
Genetic manipulation of Saccha ...
Saccharomyces cerevisiae
Mol. Cell. Biol.
6
2828-2838
1986
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1
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288192
Schmidt
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Lysine biosynthesis in the yea ...
Candida maltosa
J. Basic Microbiol.
25
675-681
1985
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288191
Eibel
Identification of the cloned S ...
Saccharomyces cerevisiae
Mol. Gen. Genet.
191
66-73
1983
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1
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288193
Tsai
Degradation of O-phosphohydrox ...
Rattus norvegicus
J. Biol. Chem.
249
5790-5792
1974
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288194
Rodwell
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delta1-piperideine-6-carboxyli ...
Pseudomonas putida
Methods Enzymol.
17B
188-199
1971
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288195
Calvert
Metabolism of pipecolic acid i ...
Pseudomonas sp.
J. Biol. Chem.
241
409-414
1966
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