BRENDA - Enzyme Database show
show all sequences of 5.1.3.37

Pseudomonas aeruginosa C5-mannuronan epimerase: steady-state kinetics and characterization of the product

Jerga, A.; Raychaudhuri, A.; Tipton, P.A.; Biochemistry 45, 552-560 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
erxpression in Escherichia coli
Pseudomonas aeruginosa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
the Km decreases from 80 microM for substrate containing fewer than 15 residues to 4 microM for substrate containing over 100 residues, pH 7.3
Pseudomonas aeruginosa
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
no Ca2+ ions required for activity, and the Ca2+-alginate complex is not a substrate for the enzyme
Pseudomonas aeruginosa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas aeruginosa
-
-
-
Storage Stability
Storage Stability
Organism
-80 C, 10% (v/v) glycerol, retains full catalytic activity for at least two months
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the minimal substrate contains 9 monosaccharide residues. Tracts of adjacent guluronate residues are readily formed. The reaction reaches an apparent equilibrium when the guluronate composition of the polymer is 75%
733323
Pseudomonas aeruginosa
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Pseudomonas aeruginosa
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
the maximum velocity of the reaction increases from 0.0018 per s to 0.0218 per s as the substrate size increases from 10 to 20 residues, and no additional increase in kcat is observed for substrates up to 100 residues in length, pH 7.3, temperature not specified in the publication
Pseudomonas aeruginosa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Pseudomonas aeruginosa
Cloned(Commentary) (protein specific)
Commentary
Organism
erxpression in Escherichia coli
Pseudomonas aeruginosa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
the Km decreases from 80 microM for substrate containing fewer than 15 residues to 4 microM for substrate containing over 100 residues, pH 7.3
Pseudomonas aeruginosa
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
no Ca2+ ions required for activity, and the Ca2+-alginate complex is not a substrate for the enzyme
Pseudomonas aeruginosa
Storage Stability (protein specific)
Storage Stability
Organism
-80 C, 10% (v/v) glycerol, retains full catalytic activity for at least two months
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the minimal substrate contains 9 monosaccharide residues. Tracts of adjacent guluronate residues are readily formed. The reaction reaches an apparent equilibrium when the guluronate composition of the polymer is 75%
733323
Pseudomonas aeruginosa
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Pseudomonas aeruginosa
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
the maximum velocity of the reaction increases from 0.0018 per s to 0.0218 per s as the substrate size increases from 10 to 20 residues, and no additional increase in kcat is observed for substrates up to 100 residues in length, pH 7.3, temperature not specified in the publication
Pseudomonas aeruginosa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Pseudomonas aeruginosa
Other publictions for EC 5.1.3.37
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)
747457
Stanisci
Overall size of mannuronan C5 ...
Azotobacter vinelandii
Carbohydr. Polym.
180
256-263
2018
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746698
Inoue
-
Functional heterologous expre ...
Saccharina japonica
Algal Res.
16
282-291
2016
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2
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747915
Fischl
The cell-wall active mannuron ...
Ectocarpus siliculosus
Glycobiology
26
973-983
2016
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1
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24
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14
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1
1
36
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25
1
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3
36
-
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734293
Wolfram
Catalytic mechanism and mode o ...
Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. tomato DC3000
J. Biol. Chem.
289
6006-6019
2014
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1
1
22
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1
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6
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748180
Buchinger
Structural and functional cha ...
Azotobacter vinelandii
J. Biol. Chem.
289
31382-31396
2014
-
-
1
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1
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-
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-
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-
2
-
4
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1
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4
1
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2
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4
2
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3
6
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733461
Tondervik
Mannuronan C-5 epimerases suit ...
Azotobacter vinelandii
Biomacromolecules
14
2657-2666
2013
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1
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1
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733474
Andreassen
1H, 13C and 15N resonances of ...
Azotobacter vinelandii
Biomol. NMR Assign.
5
147-149
2011
-
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1
1
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733738
Steigedal
The Azotobacter vinelandii Alg ...
Azotobacter vinelandii
Environ. Microbiol.
10
1760-1770
2008
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1
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1
2
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734159
Rozeboom
Structural and mutational char ...
Azotobacter vinelandii
J. Biol. Chem.
283
23819-23828
2008
-
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1
19
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2
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733323
Jerga
Pseudomonas aeruginosa C5-mann ...
Pseudomonas aeruginosa
Biochemistry
45
552-560
2006
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733324
Jerga
Chemical mechanism and specifi ...
Pseudomonas aeruginosa
Biochemistry
45
9138-9144
2006
-
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2
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733606
Hartmann
-
Enzymatic modification of algi ...
Azotobacter vinelandii
Carbohydr. Polym.
63
257-262
2006
-
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734068
Gimmestad
Identification and characteriz ...
Azotobacter vinelandii
J. Bacteriol.
188
5551-5560
2006
-
-
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1
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1
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734155
Aachmann
NMR structure of the R-module: ...
Azotobacter vinelandii
J. Biol. Chem.
281
7350-7356
2006
-
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733610
Sletmoen
Mapping enzymatic functionalit ...
Azotobacter vinelandii
Carbohydr. Res.
340
2782-2795
2005
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733283
Campa
Biochemical analysis of the pr ...
Azotobacter vinelandii
Biochem. J.
381
155-164
2004
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733462
Sletmoen
Single-molecular pair unbindin ...
Azotobacter vinelandii
Biomacromolecules
5
1288-1295
2004
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1
1
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734063
Gimmestad
The Pseudomonas fluorescens Al ...
Pseudomonas fluorescens
J. Bacteriol.
185
3515-3523
2003
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652156
Svanem
The catalytic activities of th ...
Azotobacter vinelandii
J. Biol. Chem.
276
31542-31550
2001
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5
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733928
Morea
Characterization of algG encod ...
Pseudomonas fluorescens
Gene
278
107-114
2001
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734060
Ertesvag
The A modules of the Azotobact ...
Azotobacter vinelandii
J. Bacteriol.
181
3033-3038
1999
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1
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734129
Hoidal
The recombinant Azotobacter vi ...
Azotobacter vinelandii
J. Biol. Chem.
274
12316-12322
1999
-
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1
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3
1
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2
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3
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1
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2
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1
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1
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734128
Ertesvag
The Azotobacter vinelandii man ...
Azotobacter vinelandii
J. Biol. Chem.
273
30927-30932
1998
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1
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3
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1
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