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Literature summary for 1.1.1.132 extracted from

  • Kimmel, J.L.; Tipton, P.A.
    Inactivation of GDP-mannose dehydrogenase from Pseudomonas aeruginosa by penicillic acid identifies a critical active site loop (2005), Arch. Biochem. Biophys., 441, 132-140.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene algD, overexpression of wild-type and mutant enzymes in Escherichia coli Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment 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 Comment Organism Structure
penicillic acid irreversible inactivation Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GDP-D-mannose + NAD+ + H2O Pseudomonas aeruginosa the enzyme catalyzes the first committed step in alginate biosynthesis GDP-D-mannunorate + NADH
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
gene algD
-

Purification (Commentary)

Purification (Comment) 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] Comment Organism
additional information
-
-
Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDP-D-mannose + NAD+ + H2O
-
Pseudomonas aeruginosa GDP-D-mannunorate + NADH
-
?
GDP-D-mannose + NAD+ + H2O the enzyme catalyzes the first committed step in alginate biosynthesis Pseudomonas aeruginosa GDP-D-mannunorate + NADH
-
?

Subunits

Subunits Comment Organism
More peptide mapping of recombinant wild-type and mutant enzymes with MALDI-TOF mass spectrometry Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
GDP-mannose dehydrogenase
-
Pseudomonas aeruginosa
GMD
-
Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Pseudomonas aeruginosa

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inactivation kinetics of recombinant wild-type and mutant enzymes with penicillic acid Pseudomonas aeruginosa