BRENDA - Enzyme Database show
show all sequences of 5.3.3.4

Purification and partial amino acid sequence of the cyanogen bromide fragments of muconolactone isomerase from Pseudomonas putida

Meagher, R.B.; Biochim. Biophys. Acta 494, 33-47 (1977)

Data extracted from this reference:

General Stability
General Stability
Organism
resistant to proteolytic cleavage by trypsin
Pseudomonas putida
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
additional information
-
partial amino acid sequence of cyanogen bromide fragments of the enzyme
Pseudomonas putida
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Pseudomonas putida PRS2113
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
muconolactone
-
2973
Pseudomonas putida
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid
-
2973
Pseudomonas putida
-
muconolactone
-
2973
Pseudomonas putida PRS2113
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid
-
2973
Pseudomonas putida PRS2113
-
General Stability (protein specific)
General Stability
Organism
resistant to proteolytic cleavage by trypsin
Pseudomonas putida
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
additional information
-
partial amino acid sequence of cyanogen bromide fragments of the enzyme
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
muconolactone
-
2973
Pseudomonas putida
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid
-
2973
Pseudomonas putida
-
muconolactone
-
2973
Pseudomonas putida PRS2113
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid
-
2973
Pseudomonas putida PRS2113
-
Other publictions for EC 5.3.3.4
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)
716709
de Moreno
Cloning, characterization and ...
Halomonas organivorans
PLoS ONE
6
e21049
2011
-
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1
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
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-
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-
-
-
-
-
-
-
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-
1
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1
-
-
-
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-
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-
-
-
-
-
-
-
-
1
-
-
1
-
-
704325
Marin
Modified 3-oxoadipate pathway ...
Pseudomonas reinekei
J. Bacteriol.
192
1543-1552
2010
-
-
1
-
-
-
-
-
-
-
1
3
-
3
-
-
1
-
-
-
-
-
3
-
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1
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1
3
-
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1
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3
-
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-
-
-
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-
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-
1
1
-
-
-
661015
Matsumura
Constitutive expression of cat ...
Rhodococcus sp., Rhodococcus sp. AN-22
Biochem. J.
393
219-226
2006
-
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1
-
-
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-
1
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2
2
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2
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1
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1
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4
1
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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
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1
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4
1
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2
1
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1
-
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-
-
-
-
-
651709
Skiba
Formation of protoanemonin fro ...
Cupriavidus necator, Cupriavidus necator JMP 134-1
J. Bacteriol.
184
5402-5409
2002
-
-
-
-
-
-
-
4
-
-
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2
-
27
-
-
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10
-
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5
-
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-
-
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4
-
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2
-
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-
-
-
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-
10
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
2979
Prucha
Evidence for an isomeric mucon ...
Cupriavidus necator, Cupriavidus necator JMP 134-1
Arch. Microbiol.
168
33-38
1997
-
-
-
-
-
-
-
3
-
-
2
-
-
27
-
-
1
-
-
1
1
-
8
1
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
2
-
-
-
-
1
-
1
1
-
8
1
-
-
-
3
-
-
-
-
-
-
-
-
-
-
2981
Prucha
Muconolactone isomerase of the ...
Cupriavidus necator, Cupriavidus necator JMP 134-1
Eur. J. Biochem.
237
350-356
1996
-
-
-
-
-
-
1
3
-
-
1
2
-
28
-
-
1
-
-
1
-
1
10
1
-
-
3
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
1
2
-
-
-
1
-
1
-
1
10
1
-
-
3
3
1
-
-
-
-
-
-
-
-
-
2980
Meagher
Muconolactone isomerase ...
Pseudomonas putida
Methods Enzymol.
188
130-133
1990
-
-
-
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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-
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-
-
-
-
2982
Katti
Crystal structure of muconolac ...
Pseudomonas putida
J. Mol. Biol.
205
557-571
1989
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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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-
-
-
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-
-
-
2978
Aldrich
Transcriptional regulation, nu ...
Pseudomonas putida
J. Bacteriol.
170
1297-1304
1988
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1
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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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2
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-
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2977
Chari
-
Absolute stereochemical course ...
Acinetobacter calcoaceticus, Pseudomonas putida
J. Am. Chem. Soc.
109
5520-5521
1987
-
-
-
-
-
-
-
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2
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2
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2
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2
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-
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2976
Shanley
Cloning and expression of Acin ...
Acinetobacter calcoaceticus
J. Bacteriol.
165
557-563
1986
-
-
1
-
-
-
-
-
-
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-
1
-
5
-
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-
2
-
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1
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1
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2
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-
2975
Katz
Low resolution crystal structu ...
Pseudomonas putida
J. Mol. Biol.
184
311-318
1985
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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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1
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1
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1
1
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-
2974
Parke
Structural comparison of gamma ...
Pseudomonas putida
Biochim. Biophys. Acta
578
145-154
1979
-
-
-
-
-
-
-
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-
2
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-
2
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1
2
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2
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1
2
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-
-
-
-
-
-
-
2973
Meagher
Purification and partial amino ...
Pseudomonas putida, Pseudomonas putida PRS2113
Biochim. Biophys. Acta
494
33-47
1977
-
-
-
-
-
1
-
-
-
-
1
-
-
3
-
-
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-
-
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2
-
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-
-
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-
1
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1
-
-
-
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-
-
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-
-
2
-
-
-
-
-
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2971
Patel
Relationship among enzymes of ...
Acinetobacter calcoaceticus, Pseudomonas putida
J. Biol. Chem.
249
7410-7419
1974
-
-
-
-
-
-
-
-
-
-
4
2
-
6
-
-
1
-
-
-
1
-
4
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
2
-
-
-
1
-
-
1
-
4
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2970
Meagher
Relationships among enzymes of ...
Pseudomonas putida
Biochemistry
12
3523-3530
1973
-
-
-
1
-
-
-
-
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-
1
1
-
3
-
-
1
-
-
1
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
1
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2972
Ornston
-
Conversion of catechol and pro ...
Pseudomonas putida
Methods Enzymol.
17A
529-549
1970
-
-
-
1
-
-
-
1
-
-
1
2
-
1
-
-
1
-
-
-
1
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
2
-
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-
1
-
-
1
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2969
Ornston
The conversion of catechol and ...
Pseudomonas putida
J. Biol. Chem.
241
3795-3799
1966
-
-
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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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2
-
1
1
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-
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-
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-
1
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-
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-
-
1
-
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1
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1
-
1
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2
-
1
1
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