BRENDA - Enzyme Database
show all sequences of 4.1.1.45

Tissue expression and biochemical characterization of human 2-amino 3-carboxymuconate 6-semialdehyde decarboxylase, a key enzyme in tryptophan catabolism

Pucci, L.; Perozzi, S.; Cimadamore, F.; Orsomando, G.; Raffaelli, N.; FEBS J. 274, 827-840 (2007)

Data extracted from this reference:

Application
Application
Commentary
Organism
medicine
the enzyme is an therapeutic target for treating disorders associated with increased levels of tryptophan metabolites
Homo sapiens
Cloned(Commentary)
Commentary
Organism
expressed in Pichia pastoris GS115 cells
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
H6A
activity decreases by about 82%
Homo sapiens
H8A
activity decreases by about 50%
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cd2+
0.5 mM, reduces the enzymatic activity to 25%
Homo sapiens
Cr3+
0.5 mM, reduces the enzymatic activity to 35%
Homo sapiens
Fe3+
0.1 mM, reduces the enzymatic activity to 15%
Homo sapiens
Kynurenic acid
1 mM, 59% residual activity
Homo sapiens
Picolinic acid
1 mM, 47% residual activity
Homo sapiens
quinolinic acid
1 mM, 61% residual activity
Homo sapiens
Zn2+
0.1 mM, reduces the enzymatic activity to 6%
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0065
-
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25°C
Homo sapiens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
1.0 mM, increases activity to 130%
Homo sapiens
Fe2+
0.1 mM, increases activity to 124%
Homo sapiens
additional information
not influenced by 1 mM Mg2+, Mn2+, Ni2+ or Ca2+; the pure enzyme is 100% active in the absence of any metal ion
Homo sapiens
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
SDS-PAGE
Homo sapiens
50000
-
gel filtration
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Homo sapiens
plays a key role in tryptophan catabolism, the enzyme regulates NAD biosynthesis from the amino acid, directly affecting quinolinate and picolinate formation
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Purification (Commentary)
Commentary
Organism
hydroxyapatite column chromatography, MonoQ column chromatography and Superose 12 gel filtration
Homo sapiens
Source Tissue
Source Tissue
Commentary
Organism
Textmining
brain
-
Homo sapiens
-
kidney
-
Homo sapiens
-
liver
-
Homo sapiens
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.006
-
crude cell extract, in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25°C
Homo sapiens
1.39
-
after 231fold purification, in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25°C
Homo sapiens
Storage Stability
Storage Stability
Organism
4°C, 10 mM Tris-HCl, pH 8.0, 0.13 m NaCl, several weeks, remains stable
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
679800
Homo sapiens
2-aminomuconate-6-semialdehyde + CO2
-
-
-
?
additional information
plays a key role in tryptophan catabolism, the enzyme regulates NAD biosynthesis from the amino acid, directly affecting quinolinate and picolinate formation
679800
Homo sapiens
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
-
Homo sapiens
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
-20
-
the purified protein is sensitive to freezing at -20°C
Homo sapiens
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1
-
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25°C
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
8
-
Homo sapiens
Application (protein specific)
Application
Commentary
Organism
medicine
the enzyme is an therapeutic target for treating disorders associated with increased levels of tryptophan metabolites
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Pichia pastoris GS115 cells
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H6A
activity decreases by about 82%
Homo sapiens
H8A
activity decreases by about 50%
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cd2+
0.5 mM, reduces the enzymatic activity to 25%
Homo sapiens
Cr3+
0.5 mM, reduces the enzymatic activity to 35%
Homo sapiens
Fe3+
0.1 mM, reduces the enzymatic activity to 15%
Homo sapiens
Kynurenic acid
1 mM, 59% residual activity
Homo sapiens
Picolinic acid
1 mM, 47% residual activity
Homo sapiens
quinolinic acid
1 mM, 61% residual activity
Homo sapiens
Zn2+
0.1 mM, reduces the enzymatic activity to 6%
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0065
-
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25°C
Homo sapiens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
1.0 mM, increases activity to 130%
Homo sapiens
Fe2+
0.1 mM, increases activity to 124%
Homo sapiens
additional information
not influenced by 1 mM Mg2+, Mn2+, Ni2+ or Ca2+; the pure enzyme is 100% active in the absence of any metal ion
Homo sapiens
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
SDS-PAGE
Homo sapiens
50000
-
gel filtration
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Homo sapiens
plays a key role in tryptophan catabolism, the enzyme regulates NAD biosynthesis from the amino acid, directly affecting quinolinate and picolinate formation
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
hydroxyapatite column chromatography, MonoQ column chromatography and Superose 12 gel filtration
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
brain
-
Homo sapiens
-
kidney
-
Homo sapiens
-
liver
-
Homo sapiens
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.006
-
crude cell extract, in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25°C
Homo sapiens
1.39
-
after 231fold purification, in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25°C
Homo sapiens
Storage Stability (protein specific)
Storage Stability
Organism
4°C, 10 mM Tris-HCl, pH 8.0, 0.13 m NaCl, several weeks, remains stable
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
-
679800
Homo sapiens
2-aminomuconate-6-semialdehyde + CO2
-
-
-
?
additional information
plays a key role in tryptophan catabolism, the enzyme regulates NAD biosynthesis from the amino acid, directly affecting quinolinate and picolinate formation
679800
Homo sapiens
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
-
Homo sapiens
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
-20
-
the purified protein is sensitive to freezing at -20°C
Homo sapiens
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1
-
2-amino-3-(3-oxoprop-2-enyl)-but-2-enedioate
in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25°C
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
8
-
Homo sapiens
Other publictions for EC 4.1.1.45
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)
748372
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2
1
1
2
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1416-1419
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727961
Huo
The power of two: arginine 51 ...
Pseudomonas fluorescens
J. Biol. Chem.
288
30862-30871
2013
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1
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4
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1
1
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1
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1
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Huo
Evidence for a dual role of an ...
Pseudomonas fluorescens
Biochemistry
51
5811-5821
2012
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691974
Gaetjens
Corroborative cobalt and zinc ...
Pseudomonas fluorescens
Dalton Trans.
2009
51-62
2009
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692186
Sasaki
Production of L-tryptophan-der ...
Rattus norvegicus
Eur. J. Nutr.
48
145-153
2009
1
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703670
Garavaglia
The crystal structure of human ...
Homo sapiens
FEBS J.
276
6615-6623
2009
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692185
Sasaki
Down-regulation of alpha-amino ...
Rattus norvegicus
Eur. J. Nutr.
47
80-86
2008
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679800
Pucci
Tissue expression and biochemi ...
Homo sapiens
FEBS J.
274
827-840
2007
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680375
Li
Detection of transient interme ...
Pseudomonas fluorescens
J. Am. Chem. Soc.
129
9278-9279
2007
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678136
Liu
Transition metal-catalyzed non ...
Pseudomonas fluorescens
Biochemistry
45
10407-10411
2006
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5
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678137
Martynowski
Crystal structure of alpha-ami ...
Pseudomonas fluorescens
Biochemistry
45
10412-10421
2006
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1
1
1
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1
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678194
Li
Alpha-amino-beta-carboxymuconi ...
Pseudomonas fluorescens
Biochemistry
45
6628-6634
2006
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1
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5
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6
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6
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682014
Shin
Regulation of mouse hepatic al ...
Mus musculus
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