BRENDA - Enzyme Database show
show all sequences of 1.13.11.3

The effects of trace elements, cations, and environmental conditions on protocatechuate 3,4-dioxygenase activity

Da Silva, A.; Jacques, R.; Andreazza, R.; Bento, F.; Camargo, F.; Sci. Agric. (Piracicaba, Braz.) 70, 68-73 (2013)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
phylogenetic tree
Leifsonia sp.
Engineering
Amino acid exchange
Commentary
Organism
additional information
immobilization of the enzyme, the immobilized extract exhibited higher enzyme activity than the cell-free extract in the presence of trace elements and cations
Leifsonia sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Cu2+
increases enzyme activity for both cell-free and immobilized extracts by 8% and 44%, respectively
Leifsonia sp.
Fe3+
increases enzyme activity for both cell-free and immobilized extracts by 16% and 99%, respectively
Leifsonia sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3,4-dihydroxybenzoate + O2
Leifsonia sp.
-
3-carboxy-cis,cis-muconate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Leifsonia sp.
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
culture condition:phenanthrene-grown cell
-
Leifsonia sp.
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,4-dihydroxybenzoate + O2
-
726481
Leifsonia sp.
3-carboxy-cis,cis-muconate
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
optimum for the cell-free enzyme extract
Leifsonia sp.
55
-
optimum for the immobilized enzyme extract
Leifsonia sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Leifsonia sp.
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4
9
activity range, profile overview
Leifsonia sp.
6.5
8
80% of maximal activity within this range
Leifsonia sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
phylogenetic tree
Leifsonia sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
immobilization of the enzyme, the immobilized extract exhibited higher enzyme activity than the cell-free extract in the presence of trace elements and cations
Leifsonia sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Cu2+
increases enzyme activity for both cell-free and immobilized extracts by 8% and 44%, respectively
Leifsonia sp.
Fe3+
increases enzyme activity for both cell-free and immobilized extracts by 16% and 99%, respectively
Leifsonia sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3,4-dihydroxybenzoate + O2
Leifsonia sp.
-
3-carboxy-cis,cis-muconate
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
culture condition:phenanthrene-grown cell
-
Leifsonia sp.
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,4-dihydroxybenzoate + O2
-
726481
Leifsonia sp.
3-carboxy-cis,cis-muconate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
optimum for the cell-free enzyme extract
Leifsonia sp.
55
-
optimum for the immobilized enzyme extract
Leifsonia sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Leifsonia sp.
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4
9
activity range, profile overview
Leifsonia sp.
6.5
8
80% of maximal activity within this range
Leifsonia sp.
Other publictions for EC 1.13.11.3
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)
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Guzik
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2014
138768
2014
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1
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3
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Protocatechuate 3,4-dioxygena ...
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
J. Mol. Microbiol. Biotechnol.
24
150-160
2014
4
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725655
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Purification and characterizat ...
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes KF707
J. Korean Soc. Appl. Biol. Chem.
56
401-408
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16
1
1
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1
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726481
Da Silva
-
The effects of trace elements, ...
Leifsonia sp.
Sci. Agric. (Piracicaba, Braz.)
70
68-73
2013
-
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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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726535
Guzik
Influence of metal ions on bio ...
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
World J. Microbiol. Biotechnol.
29
267-273
2013
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8
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712295
Zhao
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Corynebacterium glutamicum
J. Bacteriol.
192
1565-1572
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702976
Guzik
Isolation and characterization ...
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
Braz. J. Microbiol.
40
285-291
2009
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704290
Zimmermann
Role of Acinetobacter baylyi C ...
Acinetobacter baylyi, Acinetobacter baylyi Crc
J. Bacteriol.
191
2834-2842
2009
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686803
Kim
Molecular cloning and function ...
Chromohalobacter sp. HS-2, Chromohalobacter sp. HS2
FEMS Microbiol. Lett.
280
235-241
2008
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697244
Bubinas
-
Degradation of naphthalene by ...
Geobacillus sp.
Cent. Eur. J. Biol.
3
61-68
2008
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685485
Bubinas
-
Protocatechuate 3,4-dioxygenas ...
Geobacillus sp.
Biologija (Vilnius)
53
31-34
2007
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687286
Pau
Spectroscopic and electronic s ...
Brevibacterium fuscum, Pseudomonas putida
J. Am. Chem. Soc.
129
1944-1958
2007
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671470
Gore
Deletion mutations caused by D ...
Acinetobacter baylyi, Acinetobacter baylyi ADP1
Appl. Environ. Microbiol.
72
5239-5245
2006
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674004
Kurahashi
Trigonal-bipyramidal geometry ...
Pseudomonas putida
Inorg. Chem.
45
7709-7721
2006
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674180
Borowski
Mechanism for Catechol Ring Cl ...
Pseudomonas putida
J. Am. Chem. Soc.
128
12941-12953
2006
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671672
Parulekar
-
Multiple pathways for the biod ...
Pseudomonas mendocina
Asian J. Microbiol. Biotechnol. Environ. Sci.
7
85-89
2005
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671966
Valley
Roles of the equatorial tyrosy ...
Pseudomonas putida
Biochemistry
44
11024-11039
2005
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677115
Shen
Key enzymes of the protocatech ...
Corynebacterium glutamicum
Sci. China C Life Sci.
48
241-249
2005
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Diverse organization of genes ...
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Cloning of the genes for a 4-s ...
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Key aromatic-ring-cleaving enz ...
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The use of protocatechuate dio ...
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Substitution, insertion, delet ...
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439508
Frazee
The axial tyrosinate Fe3+ liga ...
no activity in Pseudomonas fluorescens, Pseudomonas putida
Biochemistry
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1998
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439506
Orville
Crystal structures of substrat ...
Pseudomonas putida
Biochemistry
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1997
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Orville
Cyanide and nitric oxide bindi ...
Pseudomonas putida
Biochemistry
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1997
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Hammer
Purification and characterizat ...
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Ohlendorf
Structure of protocatechuate 3 ...
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Immobilization of protocatechu ...
Pleurotus ostreatus
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The primary structure of the b ...
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Durham
Intergeneric evolutionary homo ...
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Mohan
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Purification and properties of ...
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439495
May
Protocatechuate 3,4-dioxygenas ...
Pseudomonas aeruginosa
Biochemistry
18
5933-5939
1979
-
-
-
-
-
-
6
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
6
6
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439487
May
Interaction of protocatechuate ...
Pseudomonas putida
Biochemistry
17
1853-1860
1978
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
3
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439486
Que
Protocatechuate 3,4-dioxygenas ...
Pseudomonas putida
Biochim. Biophys. Acta
485
60-74
1977
-
-
-
-
-
-
14
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
13
-
-
-
-
-
-
-
-
-
-
14
13
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439500
Hou
Protocatechuate 3, 4-dioxygena ...
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus 80-1
Biochemistry
15
582-588
1976
-
-
-
-
-
-
19
2
-
1
1
-
-
5
-
-
1
-
-
1
1
1
2
-
1
-
1
-
1
-
1
-
7
-
-
-
-
-
-
-
-
-
-
19
7
2
-
1
1
-
-
-
-
1
-
1
1
1
2
-
1
-
1
-
1
-
1
-
-
-
-
-
-
-
439485
Zaborsky
Immobilization of protocatechu ...
Pseudomonas aeruginosa
Biochim. Biophys. Acta
289
68-76
1972
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
2
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
2
-
2
-
-
-
-
-
-
-
-
-
439480
Gibson
-
Assay of enzymes of aromatic m ...
Pseudomonas sp.
Methods Enzymol.
6A
463-478
1971
-
-
-
1
-
1
1
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439483
Fujisawa
Protocatechuate 3,4-dioxygenas ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa B-10
J. Biol. Chem.
243
2673-2681
1968
-
-
-
1
-
-
4
2
-
1
1
-
-
2
-
-
1
-
-
-
1
-
11
-
-
-
1
1
1
-
1
-
1
-
-
-
-
-
-
1
-
-
-
4
1
2
-
1
1
-
-
-
-
1
-
-
1
-
11
-
-
-
1
1
1
-
1
-
-
-
-
-
-
-
439481
Stanier
Protocatechuic acid oxidase ...
Pseudomonas fluorescens, Pseudomonas fluorescens A.3.12.
J. Biol. Chem.
210
799-808
1954
-
-
-
-
-
-
3
-
-
-
-
-
-
2
-
-
1
-
-
-
1
1
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
1
1
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
439482
Gross
The metabolism of protocatechu ...
Neurospora crassa
J. Biol. Chem.
219
781-796
1954
-
-
-
-
-
2
3
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
1
1
-
-
-
2
-
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-
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-
-