BRENDA - Enzyme Database
show all sequences of 4.2.1.80

Determination of the metal ion dependence and substrate specificity of a hydratase involved in the degradation pathway of biphenyl/chlorobiphenyl

Wang, P.; Seah, S.Y.K.; FEBS J. 272, 966-974 (2005)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli
Paraburkholderia xenovorans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0317
-
2-hydroxypent-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
0.0386
-
2-hydroxypent-2,4-dienoate
activated by Mn2+
Paraburkholderia xenovorans
0.0408
-
2-hydroxyhexa-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
0.0459
-
5-chloro-2-hydroxypent-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Paraburkholderia xenovorans
Co2+
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Paraburkholderia xenovorans
Mg2+
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Paraburkholderia xenovorans
Mn2+
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Paraburkholderia xenovorans
Zn2+
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Paraburkholderia xenovorans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27000
-
8 * 27000, SDS-PAGE
Paraburkholderia xenovorans
221000
-
gel filtration
Paraburkholderia xenovorans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
2-hydroxypent-2,4-dienoate
Paraburkholderia xenovorans
reaction in the catabolic pathway of numerous aromatic compounds, including polychlorinated biphenyls
2-keto-4-hydroxypentanoate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Paraburkholderia xenovorans
-
LB400
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant
Paraburkholderia xenovorans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
2-hydroxyhexa-2,4-dienoate + H2O
-
661714
Paraburkholderia xenovorans
2-keto-4-hydroxyhexanoate
-
-
-
?
2-hydroxypent-2,4-dienoate
reaction in the catabolic pathway of numerous aromatic compounds, including polychlorinated biphenyls
661714
Paraburkholderia xenovorans
2-keto-4-hydroxypentanoate
-
-
-
?
2-hydroxypent-2,4-dienoate + H2O
-
661714
Paraburkholderia xenovorans
2-keto-4-hydroxypentanoate
-
-
-
?
5-chloro-2-hydroxypent-2,4-dienoate
-
661714
Paraburkholderia xenovorans
5-chloro-2-keto-4-hydroxypentanoate
-
-
-
?
Subunits
Subunits
Commentary
Organism
octamer
8 * 27000, SDS-PAGE
Paraburkholderia xenovorans
Synonyms
Synonyms
Commentary
Organism
BphH
-
Paraburkholderia xenovorans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
7.7
-
5-chloro-2-hydroxypent-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
60.5
-
2-hydroxyhexa-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
215
-
2-hydroxypent-2,4-dienoate
activated by Mn2+
Paraburkholderia xenovorans
361
-
2-hydroxypent-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
8
-
Paraburkholderia xenovorans
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Paraburkholderia xenovorans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0317
-
2-hydroxypent-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
0.0386
-
2-hydroxypent-2,4-dienoate
activated by Mn2+
Paraburkholderia xenovorans
0.0408
-
2-hydroxyhexa-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
0.0459
-
5-chloro-2-hydroxypent-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Paraburkholderia xenovorans
Co2+
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Paraburkholderia xenovorans
Mg2+
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Paraburkholderia xenovorans
Mn2+
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Paraburkholderia xenovorans
Zn2+
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Paraburkholderia xenovorans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27000
-
8 * 27000, SDS-PAGE
Paraburkholderia xenovorans
221000
-
gel filtration
Paraburkholderia xenovorans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
2-hydroxypent-2,4-dienoate
Paraburkholderia xenovorans
reaction in the catabolic pathway of numerous aromatic compounds, including polychlorinated biphenyls
2-keto-4-hydroxypentanoate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant
Paraburkholderia xenovorans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
2-hydroxyhexa-2,4-dienoate + H2O
-
661714
Paraburkholderia xenovorans
2-keto-4-hydroxyhexanoate
-
-
-
?
2-hydroxypent-2,4-dienoate
reaction in the catabolic pathway of numerous aromatic compounds, including polychlorinated biphenyls
661714
Paraburkholderia xenovorans
2-keto-4-hydroxypentanoate
-
-
-
?
2-hydroxypent-2,4-dienoate + H2O
-
661714
Paraburkholderia xenovorans
2-keto-4-hydroxypentanoate
-
-
-
?
5-chloro-2-hydroxypent-2,4-dienoate
-
661714
Paraburkholderia xenovorans
5-chloro-2-keto-4-hydroxypentanoate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
octamer
8 * 27000, SDS-PAGE
Paraburkholderia xenovorans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
7.7
-
5-chloro-2-hydroxypent-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
60.5
-
2-hydroxyhexa-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
215
-
2-hydroxypent-2,4-dienoate
activated by Mn2+
Paraburkholderia xenovorans
361
-
2-hydroxypent-2,4-dienoate
activated by Mg2+
Paraburkholderia xenovorans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
8
-
Paraburkholderia xenovorans
Other publictions for EC 4.2.1.80
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
Synonyms
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)
747105
Johnson
Stereochemical consequences o ...
Leptothrix cholodnii, Leptothrix cholodnii SP-6, Pseudomonas putida
Biochemistry
55
4055-4064
2016
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
6
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
705177
Montgomery
Assembly of a 20-nm protein ca ...
Escherichia coli K-12
J. Mol. Biol.
396
1379-1391
2010
-
-
1
1
-
-
-
-
-
1
3
-
-
2
-
-
1
-
-
-
-
-
-
1
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
1
3
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
672682
Orii
Metabolism of 4-amino-3-hydrox ...
Bordetella sp. 10d, Bordetella sp.
Biosci. Biotechnol. Biochem.
70
2653-2661
2006
-
-
-
-
-
-
-
-
-
1
-
-
-
3
-
-
1
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
661714
Wang
Determination of the metal ion ...
Paraburkholderia xenovorans
FEBS J.
272
966-974
2005
-
-
1
-
-
-
-
4
-
5
2
1
-
1
-
-
1
-
-
-
-
-
4
1
1
-
-
-
4
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
4
-
5
2
1
-
-
-
1
-
-
-
-
4
1
-
-
-
4
1
-
-
-
-
-
-
-
-
-
648402
Lim
Characterization of the pcbE g ...
Pseudomonas sp., Pseudomonas sp. DJ-12
Arch. Pharm. Res.
23
187-195
2000
-
-
1
-
-
-
-
-
-
-
1
-
-
6
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
648399
Romine
-
Complete sequence of a 184-kil ...
Novosphingobium aromaticivorans, Novosphingobium aromaticivorans F199
J. Bacteriol.
181
1282-1602
1999
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
648401
Pollard
Purification, characterization ...
Escherichia coli
Eur. J. Biochem.
251
98-106
1998
-
-
1
-
-
-
2
1
-
1
1
-
-
3
-
-
1
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
2
1
1
-
1
1
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
648400
Kim
Localization and sequence anal ...
Pseudomonas sp., Pseudomonas sp. DJ77
Biochem. Biophys. Res. Commun.
238
56-60
1997
-
-
-
-
-
-
-
-
-
-
1
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
648398
Harayama
-
Physically associated enzymes ...
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
J. Bacteriol.
171
6221-6228
1989
-
-
1
-
-
-
-
1
-
2
1
-
-
19
-
-
1
-
-
-
2
-
2
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
2
1
-
-
-
-
1
-
-
2
-
2
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
648397
Kunz
Metabolism of allylglycine and ...
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182, Pseudomonas sp.
J. Bacteriol.
148
72-82
1981
-
-
-
-
-
-
-
-
-
-
-
-
-
20
-
-
1
-
-
-
2
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-