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Literature summary for 1.1.1.132 extracted from

  • Naught, L.E.; Gilbert, S.; Imhoff, R.; Snook, C.; Beamer, L.; Tipton, P.
    Allosterism and cooperativity in Pseudomonas aeruginosa GDP-mannose dehydrogenase (2002), Biochemistry, 41, 9637-9645.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information in phosphate buffer, enzyme shows Michaelis-Menten kinetics, in Tris buffer, enzyme shows marked cooperativity with respect to NAD+ binding. Phosphate and GMP are allosteric effectors Pseudomonas aeruginosa
0.1
-
NAD+ pH 8.0, phosphate buffer Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Cofactor

Cofactor Comment Organism Structure
NAD+ cooperative behaviour with respect to NAD+ binding, sensitive to pH Pseudomonas aeruginosa