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show all sequences of 1.1.1.132

Inactivation of GDP-mannose dehydrogenase from Pseudomonas aeruginosa by penicillic acid identifies a critical active site loop

Kimmel, J.L.; Tipton, P.A.; Arch. Biochem. Biophys. 441, 132-140 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene algD, overexpression of wild-type and mutant enzymes in Escherichia coli
Pseudomonas aeruginosa
Engineering
Amino acid exchange
Commentary
Organism
C213A
site-directed mutagenesis, 1.8fold increased Vmax compared to the wild-type enzyme
Pseudomonas aeruginosa
C268A
site-directed mutagenesis, 250fold reduced Vmax, 5fold increased KM, and reduced sensitivity to penicillic acid inactivation compared to the wild-type enzyme
Pseudomonas aeruginosa
Inhibitors
Inhibitors
Commentary
Organism
Structure
penicillic acid
irreversible inactivation
Pseudomonas aeruginosa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.009
-
GDP-D-mannose
pH 8.0, 5°C, recombinant wild-type enzyme
Pseudomonas aeruginosa
0.023
-
GDP-D-mannose
pH 8.0, 5°C, recombinant mutant C213A
Pseudomonas aeruginosa
0.045
-
GDP-D-mannose
pH 8.0, 5°C, recombinant mutant C268A
Pseudomonas aeruginosa
0.19
-
NAD+
pH 8.0, 5°C, recombinant mutant C213A
Pseudomonas aeruginosa
0.21
-
NAD+
pH 8.0, 5°C, recombinant wild-type enzyme
Pseudomonas aeruginosa
0.51
-
NAD+
pH 8.0, 5°C, recombinant mutant C268A
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
GDP-D-mannose + NAD+ + H2O
Pseudomonas aeruginosa
the enzyme catalyzes the first committed step in alginate biosynthesis
GDP-D-mannunorate + NADH
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas aeruginosa
-
gene algD
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli by gel filtration of enzyme with tightly bound GDP-mannuronic acid and NAD+, dialysis and ion exchange chromatography
Pseudomonas aeruginosa
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
GDP-D-mannose + NAD+ + H2O
-
667316
Pseudomonas aeruginosa
GDP-D-mannunorate + NADH
-
-
-
?
GDP-D-mannose + NAD+ + H2O
the enzyme catalyzes the first committed step in alginate biosynthesis
667316
Pseudomonas aeruginosa
GDP-D-mannunorate + NADH
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
peptide mapping of recombinant wild-type and mutant enzymes with MALDI-TOF mass spectrometry
Pseudomonas aeruginosa
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Pseudomonas aeruginosa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Pseudomonas aeruginosa
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Pseudomonas aeruginosa
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
inactivation kinetics of recombinant wild-type and mutant enzymes with penicillic acid
Pseudomonas aeruginosa
Cloned(Commentary) (protein specific)
Commentary
Organism
gene algD, overexpression of wild-type and mutant enzymes in Escherichia coli
Pseudomonas aeruginosa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Pseudomonas aeruginosa
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C213A
site-directed mutagenesis, 1.8fold increased Vmax compared to the wild-type enzyme
Pseudomonas aeruginosa
C268A
site-directed mutagenesis, 250fold reduced Vmax, 5fold increased KM, and reduced sensitivity to penicillic acid inactivation compared to the wild-type enzyme
Pseudomonas aeruginosa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
penicillic acid
irreversible inactivation
Pseudomonas aeruginosa
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
inactivation kinetics of recombinant wild-type and mutant enzymes with penicillic acid
Pseudomonas aeruginosa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.009
-
GDP-D-mannose
pH 8.0, 5°C, recombinant wild-type enzyme
Pseudomonas aeruginosa
0.023
-
GDP-D-mannose
pH 8.0, 5°C, recombinant mutant C213A
Pseudomonas aeruginosa
0.045
-
GDP-D-mannose
pH 8.0, 5°C, recombinant mutant C268A
Pseudomonas aeruginosa
0.19
-
NAD+
pH 8.0, 5°C, recombinant mutant C213A
Pseudomonas aeruginosa
0.21
-
NAD+
pH 8.0, 5°C, recombinant wild-type enzyme
Pseudomonas aeruginosa
0.51
-
NAD+
pH 8.0, 5°C, recombinant mutant C268A
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
GDP-D-mannose + NAD+ + H2O
Pseudomonas aeruginosa
the enzyme catalyzes the first committed step in alginate biosynthesis
GDP-D-mannunorate + NADH
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli by gel filtration of enzyme with tightly bound GDP-mannuronic acid and NAD+, dialysis and ion exchange chromatography
Pseudomonas aeruginosa
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Pseudomonas aeruginosa
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
-
667316
Pseudomonas aeruginosa
GDP-D-mannunorate + NADH
-
-
-
?
GDP-D-mannose + NAD+ + H2O
the enzyme catalyzes the first committed step in alginate biosynthesis
667316
Pseudomonas aeruginosa
GDP-D-mannunorate + NADH
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
peptide mapping of recombinant wild-type and mutant enzymes with MALDI-TOF mass spectrometry
Pseudomonas aeruginosa
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Pseudomonas aeruginosa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Pseudomonas aeruginosa
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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7
3
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1
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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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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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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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6
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654702
Snook
Crystal structure of GDP-manno ...
Pseudomonas aeruginosa
Biochemistry
42
4658-4668
2003
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654666
Naught
Allosterism and cooperativity ...
Pseudomonas aeruginosa
Biochemistry
41
9637-9645
2002
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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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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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16
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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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285840
Roychoudhury
Characterization of guanosine ...
Pseudomonas aeruginosa
J. Biol. Chem.
267
990-996
1992
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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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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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285829
Preiss
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GDP-mannose dehydrogenase from ...
Arthrobacter sp., Arthrobacter sp. NRRL B1973
Methods Enzymol.
8
285-287
1966
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285831
Preiss
Sugar nucleotide reactions in ...
Arthrobacter sp.
J. Biol. Chem.
239
3127-3132
1964
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