BRENDA - Enzyme Database show
show all sequences of 5.1.3.37

Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii

Rozeboom, H.J.; Bjerkan, T.M.; Kalk, K.H.; Ertesvag, H.; Holtan, S.; Aachmann, F.L.; Valla, S.; Dijkstra, B.W.; J. Biol. Chem. 283, 23819-23828 (2008)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
to 2.1 A resolution. Isoform AlgE4A folds into a right-handed parallel beta-helix structure. The alpha-helix is composed of four parallel beta-sheets, comprising 12 complete turns, and has an amphipathic alpha-helix near the N terminus. The catalytic site is positioned in a positively charged cleft formed by loops extending from the surface encompassing Asp152, an amino acid important for the reaction
Azotobacter vinelandii
Engineering
Amino acid exchange
Commentary
Organism
D173E
54% residual activity
Azotobacter vinelandii
D178E
complete loss of activity
Azotobacter vinelandii
D178N
complete loss of activity
Azotobacter vinelandii
F122Y
65% residual activity
Azotobacter vinelandii
H154F
complete loss of activity
Azotobacter vinelandii
H154R
complete loss of activity
Azotobacter vinelandii
K117 R
24% residual activity
Azotobacter vinelandii
K117A
16% residual activity
Azotobacter vinelandii
K255A
8% residual activity
Azotobacter vinelandii
K255R
51% residual activity
Azotobacter vinelandii
P153A
10% residual activity
Azotobacter vinelandii
P153A/D173E
4% residual activity
Azotobacter vinelandii
Q156A
10% residual activity
Azotobacter vinelandii
Q225A
9% residual activity
Azotobacter vinelandii
Q225E
4% residual activity
Azotobacter vinelandii
Q225N
6% residual activity
Azotobacter vinelandii
R249A
46% residual activity
Azotobacter vinelandii
Y149F
complete loss of activity
Azotobacter vinelandii
Y149H
complete loss of activity
Azotobacter vinelandii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Azotobacter vinelandii
Q44493
-
-
Crystallization (Commentary) (protein specific)
Crystallization
Organism
to 2.1 A resolution. Isoform AlgE4A folds into a right-handed parallel beta-helix structure. The alpha-helix is composed of four parallel beta-sheets, comprising 12 complete turns, and has an amphipathic alpha-helix near the N terminus. The catalytic site is positioned in a positively charged cleft formed by loops extending from the surface encompassing Asp152, an amino acid important for the reaction
Azotobacter vinelandii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D173E
54% residual activity
Azotobacter vinelandii
D178E
complete loss of activity
Azotobacter vinelandii
D178N
complete loss of activity
Azotobacter vinelandii
F122Y
65% residual activity
Azotobacter vinelandii
H154F
complete loss of activity
Azotobacter vinelandii
H154R
complete loss of activity
Azotobacter vinelandii
K117 R
24% residual activity
Azotobacter vinelandii
K117A
16% residual activity
Azotobacter vinelandii
K255A
8% residual activity
Azotobacter vinelandii
K255R
51% residual activity
Azotobacter vinelandii
P153A
10% residual activity
Azotobacter vinelandii
P153A/D173E
4% residual activity
Azotobacter vinelandii
Q156A
10% residual activity
Azotobacter vinelandii
Q225A
9% residual activity
Azotobacter vinelandii
Q225E
4% residual activity
Azotobacter vinelandii
Q225N
6% residual activity
Azotobacter vinelandii
R249A
46% residual activity
Azotobacter vinelandii
Y149F
complete loss of activity
Azotobacter vinelandii
Y149H
complete loss of activity
Azotobacter vinelandii
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
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Functional heterologous expre ...
Saccharina japonica
Algal Res.
16
282-291
2016
1
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1
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1
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2
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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36
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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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748180
Buchinger
Structural and functional cha ...
Azotobacter vinelandii
J. Biol. Chem.
289
31382-31396
2014
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1
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1
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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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733738
Steigedal
The Azotobacter vinelandii Alg ...
Azotobacter vinelandii
Environ. Microbiol.
10
1760-1770
2008
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2
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734159
Rozeboom
Structural and mutational char ...
Azotobacter vinelandii
J. Biol. Chem.
283
23819-23828
2008
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19
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19
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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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1
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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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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
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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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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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734129
Hoidal
The recombinant Azotobacter vi ...
Azotobacter vinelandii
J. Biol. Chem.
274
12316-12322
1999
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1
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2
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734128
Ertesvag
The Azotobacter vinelandii man ...
Azotobacter vinelandii
J. Biol. Chem.
273
30927-30932
1998
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733742
Ramstad
-
Determination of mannuronan C- ...
Azotobacter vinelandii
Enzyme Microb. Technol.
20
308-316
1997
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1
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