BRENDA - Enzyme Database show
show all sequences of 1.13.11.6

Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis

Zhang, Y.; Colabroy, K.L.; Begley, T.P.; Ealick, S.E.; Biochemistry 44, 7632-7643 (2005)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
hanging drop method
Cupriavidus metallidurans
Engineering
Amino acid exchange
Commentary
Organism
E110A
kcat/Km is 954fold lower than wild-type enzyme
Cupriavidus metallidurans
R47A
kcat/Km is 7440fold lower than wild-type enzyme. Mutant enzyme shows substrate inhibition
Cupriavidus metallidurans
R99A
kcat/Km is 22320fold lower than wild-type enzyme
Cupriavidus metallidurans
Inhibitors
Inhibitors
Commentary
Organism
Structure
4-Chloro-3-hydroxyanthranilate
-
Cupriavidus metallidurans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0102
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme E110A
Cupriavidus metallidurans
0.0224
-
3-Hydroxyanthranilate
pH 7.2, wild-type enzyme
Cupriavidus metallidurans
0.147
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme R47A
Cupriavidus metallidurans
0.872
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme R99A
Cupriavidus metallidurans
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe
each monomer contains two iron binding sites. The catalytic iron is buried deep inside the beta-barrel with His51, Glu57, and His95 serving as ligands. The other iron site forms an FeS4 center close to the solvent surface in which the sulfur atoms are provided by Cys125, Cys128, Cys162, and Cys165. The two iron sites are separated by 24 A
Cupriavidus metallidurans
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cupriavidus metallidurans
-
recombinantly expressed in Escherichia coli
-
Purification (Commentary)
Commentary
Organism
-
Cupriavidus metallidurans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-hydroxyanthranilate + O2
-
672037
Cupriavidus metallidurans
2-amino-3-carboxymuconate semialdehyde
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0046
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme R99A
Cupriavidus metallidurans
0.012
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme E110A
Cupriavidus metallidurans
0.022
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme R47A
Cupriavidus metallidurans
25
-
3-Hydroxyanthranilate
pH 7.2, wild-type enzyme
Cupriavidus metallidurans
Crystallization (Commentary) (protein specific)
Crystallization
Organism
hanging drop method
Cupriavidus metallidurans
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E110A
kcat/Km is 954fold lower than wild-type enzyme
Cupriavidus metallidurans
R47A
kcat/Km is 7440fold lower than wild-type enzyme. Mutant enzyme shows substrate inhibition
Cupriavidus metallidurans
R99A
kcat/Km is 22320fold lower than wild-type enzyme
Cupriavidus metallidurans
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
4-Chloro-3-hydroxyanthranilate
-
Cupriavidus metallidurans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0102
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme E110A
Cupriavidus metallidurans
0.0224
-
3-Hydroxyanthranilate
pH 7.2, wild-type enzyme
Cupriavidus metallidurans
0.147
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme R47A
Cupriavidus metallidurans
0.872
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme R99A
Cupriavidus metallidurans
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe
each monomer contains two iron binding sites. The catalytic iron is buried deep inside the beta-barrel with His51, Glu57, and His95 serving as ligands. The other iron site forms an FeS4 center close to the solvent surface in which the sulfur atoms are provided by Cys125, Cys128, Cys162, and Cys165. The two iron sites are separated by 24 A
Cupriavidus metallidurans
Purification (Commentary) (protein specific)
Commentary
Organism
-
Cupriavidus metallidurans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-hydroxyanthranilate + O2
-
672037
Cupriavidus metallidurans
2-amino-3-carboxymuconate semialdehyde
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0046
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme R99A
Cupriavidus metallidurans
0.012
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme E110A
Cupriavidus metallidurans
0.022
-
3-Hydroxyanthranilate
pH 7.2, mutant enzyme R47A
Cupriavidus metallidurans
25
-
3-Hydroxyanthranilate
pH 7.2, wild-type enzyme
Cupriavidus metallidurans
Other publictions for EC 1.13.11.6
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)
741516
Pidugu
Crystal structures of human 3 ...
Homo sapiens
Acta Crystallogr. Sect. D
73
340-348
2017
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2
1
1
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1
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2
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1
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2
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1
1
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1
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-
-
-
-
-
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3
3
-
-
-
743276
Brkic
Human 3-hydroxyanthranilate 3 ...
Homo sapiens
Mol. Biosyst.
11
898-907
2015
-
1
-
-
3
-
-
-
-
1
-
1
-
2
-
-
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1
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1
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1
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2
2
-
-
-
723950
Chakraborty
Aromatic ring cleavage of 2-am ...
Pseudomonas pseudoalcaligenes
Angew. Chem. Int. Ed. Engl.
52
920-924
2013
-
-
-
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1
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1
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-
-
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3
3
-
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-
696784
Dilovic
Crystal structure of bovine 3- ...
Bos taurus
Biopolymers
91
1189-1195
2009
-
-
-
1
-
-
-
-
-
-
1
1
-
4
-
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1
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2
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1
1
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1
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1
1
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1
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1
1
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-
-
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-
675557
Yates Jennifer
4-chloro-3-hydroxyanthranilate ...
Cavia porcellus, Cavia porcellus Hartley
J. Neurotrauma
23
866-881
2006
-
-
-
-
-
-
1
-
-
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-
11
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-
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675782
Maharaj
Acetylsalicylic acid and aceta ...
Rattus norvegicus, Rattus norvegicus Wistar
Metab. Brain Dis.
21
189-199
2006
-
-
-
-
-
-
2
-
-
-
-
-
-
168
-
-
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-
1
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2
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1
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2
-
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677020
Li
Crystal structure of 3-hydroxy ...
Saccharomyces cerevisiae
Protein Sci.
15
761-773
2006
-
-
1
1
-
-
-
-
-
2
-
1
-
1
-
-
1
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1
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1
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1
1
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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-
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-
-
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-
672036
Colabroy
The mechanism of inactivation ...
Cupriavidus metallidurans
Biochemistry
44
7623-7631
2005
-
-
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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
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-
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-
672037
Zhang
Structural studies on 3-hydrox ...
Cupriavidus metallidurans
Biochemistry
44
7632-7643
2005
-
-
-
1
3
-
1
4
-
1
-
-
-
1
-
-
1
-
-
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1
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4
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1
3
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1
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4
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1
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1
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-
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1
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-
4
-
-
-
-
-
-
-
-
-
-
673130
Comai
The effect of age on the enzym ...
Rattus norvegicus
Clin. Chim. Acta
360
67-80
2005
-
-
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649382
Muraki
Prokaryotic homologs of the eu ...
Pseudomonas fluorescens, Pseudomonas fluorescens KU-7
Appl. Environ. Microbiol.
69
1564-1572
2003
-
-
1
-
3
-
13
-
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1
2
2
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5
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1
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4
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1
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3
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13
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1
2
2
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1
-
4
-
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658927
Nandi
Purification and inactivation ...
Bos taurus
Int. J. Biochem. Cell Biol.
35
1085-1097
2003
-
-
-
-
-
-
3
2
-
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4
1
-
2
-
-
1
-
-
2
1
-
2
1
-
-
1
-
1
-
-
-
5
2
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-
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-
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-
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3
5
2
-
-
4
1
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1
-
2
1
-
2
1
-
-
1
-
1
-
-
2
-
-
-
-
-
-
439377
Calderone
Cloning of human 3-hydroxyanth ...
Homo sapiens
Biochim. Biophys. Acta
1596
283-292
2002
-
-
1
-
-
-
3
-
1
1
1
1
-
3
-
-
-
1
-
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2
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-
1
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1
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3
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1
1
1
1
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-
2
-
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-
1
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439378
Agrawal
QSAR study on inhibition of br ...
Rattus norvegicus
Bioorg. Med. Chem.
9
3295-3299
2001
-
-
-
-
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1
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2
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1
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1
-
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439373
Fornstedt-Wallin
3-Hydroxyanthranilic acid accu ...
Rattus norvegicus
Eur. J. Pharmacol.
386
15-24
1999
-
-
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1
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1
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3
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1
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1
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439376
Chiarugi
Effects of mitochondria and o- ...
Mus musculus
J. Neurochem.
72
1125-1132
1999
-
-
-
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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
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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
1
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439379
Kucharczyk
The yeast gene YJR025c encodes ...
Escherichia coli, Saccharomyces cerevisiae
FEBS Lett.
424
127-130
1998
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2
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2
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4
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439375
Cesura
Molecular characterization of ...
Rattus norvegicus
Adv. Exp. Med. Biol.
398
477-483
1996
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1
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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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1
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1
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1
1
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1
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-
439374
Roberts
3-Hydroxyanthranilic acid oxyg ...
Rattus norvegicus
J. Neurosci.
15
1150-1161
1995
-
-
-
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2
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1
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1
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439371
Malherbe
Molecular cloning and function ...
Rattus norvegicus
J. Biol. Chem.
269
13792-13797
1994
-
1
1
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-
-
-
-
-
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1
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3
-
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1
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1
1
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1
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1
1
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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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439372
Roberts
Immunocytochemical localizatio ...
Rattus norvegicus
Brain Res.
650
229-238
1994
-
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-
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