BRENDA - Enzyme Database show
show all sequences of 1.1.1.132

Characterization of GDP-mannose dehydrogenase from the brown alga Ectocarpus siliculosus providing the precursor for the alginate polymer

Tenhaken, R.; Voglas, E.; Cock, J.M.; Neu, V.; Huber, C.G.; J. Biol. Chem. 286, 16707-16715 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli as a His-tagged fusion protein
Ectocarpus siliculosus
Inhibitors
Inhibitors
Commentary
Organism
Structure
NADPH
weak inhibitor of reaction
Ectocarpus siliculosus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.086
-
NAD+
pH and temperature not specified in the publication
Ectocarpus siliculosus
0.095
-
GDP-D-mannose
pH and temperature not specified in the publication
Ectocarpus siliculosus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
CoCl2
at 1 mM CoCl2 44% enzymatic activity
Ectocarpus siliculosus
CuSO4
at 1 mM CuSO4 no enzymatic activity
Ectocarpus siliculosus
FeCl3
at 1 mM FeCl3 49% enzymatic activity
Ectocarpus siliculosus
FeSO4
at 1 mM FeSO4 77% enzymatic activity
Ectocarpus siliculosus
K+
increases activity
Ectocarpus siliculosus
Na+
increases activity
Ectocarpus siliculosus
PCMB
0.025 mM, 0.8% activity
Ectocarpus siliculosus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
SDS-PAGE
Ectocarpus siliculosus
35000
-
2 * 35000, gel filtration
Ectocarpus siliculosus
70000
-
gel filtration
Ectocarpus siliculosus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Ectocarpus siliculosus
-
-
-
Purification (Commentary)
Commentary
Organism
using Ni-NTA chromatography
Ectocarpus siliculosus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
GDP-D-mannose + NAD+ + H2O
-
725424
Ectocarpus siliculosus
GDP-D-mannuronate + NADH
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 35000, gel filtration
Ectocarpus siliculosus
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
-
enzyme partly inactivated above 30C
Ectocarpus siliculosus
45
-
enzyme fully inactivated at 45C after 15 min
Ectocarpus siliculosus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.75
-
assay at
Ectocarpus siliculosus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
8.75
9
optimal pH range, enzyme inactive below pH 7
Ectocarpus siliculosus
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli as a His-tagged fusion protein
Ectocarpus siliculosus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
NADPH
weak inhibitor of reaction
Ectocarpus siliculosus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.086
-
NAD+
pH and temperature not specified in the publication
Ectocarpus siliculosus
0.095
-
GDP-D-mannose
pH and temperature not specified in the publication
Ectocarpus siliculosus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
CoCl2
at 1 mM CoCl2 44% enzymatic activity
Ectocarpus siliculosus
CuSO4
at 1 mM CuSO4 no enzymatic activity
Ectocarpus siliculosus
FeCl3
at 1 mM FeCl3 49% enzymatic activity
Ectocarpus siliculosus
FeSO4
at 1 mM FeSO4 77% enzymatic activity
Ectocarpus siliculosus
K+
increases activity
Ectocarpus siliculosus
Na+
increases activity
Ectocarpus siliculosus
PCMB
0.025 mM, 0.8% activity
Ectocarpus siliculosus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
SDS-PAGE
Ectocarpus siliculosus
35000
-
2 * 35000, gel filtration
Ectocarpus siliculosus
70000
-
gel filtration
Ectocarpus siliculosus
Purification (Commentary) (protein specific)
Commentary
Organism
using Ni-NTA chromatography
Ectocarpus siliculosus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
GDP-D-mannose + NAD+ + H2O
-
725424
Ectocarpus siliculosus
GDP-D-mannuronate + NADH
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 35000, gel filtration
Ectocarpus siliculosus
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
-
enzyme partly inactivated above 30C
Ectocarpus siliculosus
45
-
enzyme fully inactivated at 45C after 15 min
Ectocarpus siliculosus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.75
-
assay at
Ectocarpus siliculosus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
8.75
9
optimal pH range, enzyme inactive below pH 7
Ectocarpus siliculosus
Other publictions for EC 1.1.1.132
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)
725424
Tenhaken
Characterization of GDP-mannos ...
Ectocarpus siliculosus
J. Biol. Chem.
286
16707-16715
2011
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725757
Manzo
Post-transcriptional regulatio ...
Azotobacter vinelandii
J. Mol. Microbiol. Biotechnol.
21
147-159
2011
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1
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1
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691949
Li
Effects of ambroxol on alginat ...
Pseudomonas aeruginosa
Curr. Microbiol.
57
1-7
2008
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1
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4
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1
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701412
Shi
Detection of the key enzyme of ...
Vibrio sp. QY102
World J. Microbiol. Biotechnol.
24
1613-1615
2008
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1
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667316
Kimmel
Inactivation of GDP-mannose de ...
Pseudomonas aeruginosa
Arch. Biochem. Biophys.
441
132-140
2005
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1
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2
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1
6
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1
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1
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1
1
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1
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1
1
6
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1
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2
1
1
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1
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654702
Snook
Crystal structure of GDP-manno ...
Pseudomonas aeruginosa
Biochemistry
42
4658-4668
2003
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1
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1
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654666
Naught
Allosterism and cooperativity ...
Pseudomonas aeruginosa
Biochemistry
41
9637-9645
2002
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2
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1
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285841
Mitsuya
Influence of macrolides on gua ...
Pseudomonas aeruginosa
J. Infect. Chemother.
6
45-50
2000
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2
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7
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1
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285836
Tavares
Pattern of changes in the acti ...
Pseudomonas aeruginosa
Res. Microbiol.
150
105-116
1999
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1
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285838
Tatnell
Overexpression of the GDP-mann ...
Pseudomonas aeruginosa
Biochem. Soc. Trans.
24
405S
1996
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1
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16
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16
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1
1
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285842
Tatnell
GDP-mannose dehydrogenase is t ...
Pseudomonas aeruginosa
Microbiology
140
1745-1754
1994
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1
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1
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41
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41
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285839
Elloumi
-
Inhibitors of GDP-mannose dehy ...
Pseudomonas aeruginosa
Eur. J. Med. Chem.
27
149-154
1992
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11
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11
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285840
Roychoudhury
Characterization of guanosine ...
Pseudomonas aeruginosa
J. Biol. Chem.
267
990-996
1992
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1
1
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4
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1
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285837
Martins
Alginate biosynthesis in mucoi ...
Pseudomonas aeruginosa
Enzyme Microb. Technol.
13
385-389
1991
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285830
Roychoudhury
Purification and characterizat ...
Pseudomonas aeruginosa
J. Biol. Chem.
264
9380-9385
1989
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9
2
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1
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9
1
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4
2
1
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1
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1
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285833
Deretic
Gene algD coding for GDPmannos ...
Pseudomonas aeruginosa
J. Bacteriol.
169
351-358
1987
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285832
Pugashetti
GDPmannose dehydrogenase and b ...
Pseudomonas aeruginosa
J. Bacteriol.
153
1107-1110
1983
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285834
Horan
-
Studies on some enzymes of alg ...
Azotobacter vinelandii
J. Gen. Microbiol.
129
2985-2990
1983
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285835
Couperwhite
Polysaccharide production and ...
Azotobacter vinelandii
Antonie van Leeuwenhoek
41
25-32
1975
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1
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285829
Preiss
-
GDP-mannose dehydrogenase from ...
Arthrobacter sp., Arthrobacter sp. NRRL B1973
Methods Enzymol.
8
285-287
1966
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3
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4
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1
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1
4
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1
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1
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3
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1
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1
4
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1
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285831
Preiss
Sugar nucleotide reactions in ...
Arthrobacter sp.
J. Biol. Chem.
239
3127-3132
1964
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3
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1
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1
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2
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3
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1
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1
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2
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1
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