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Literature summary for 3.7.1.9 extracted from

  • Jun, S.Y.; Fushinobu, S.; Nojiri, H.; Omori, T.; Shoun, H.; Wakagi, T.
    Improving the catalytic efficiency of a meta-cleavage product hydrolase (CumD) from Pseudomonas fluorescens IP01 (2006), Biochim. Biophys. Acta, 1764, 1159-1166 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzyme A129V, vapor diffusion method Pseudomonas fluorescens

Protein Variants

Protein Variants Comment Organism
A129V the kcat/Km value of the single mutant is higher than that of the wild type enzyme. The mutant shows the highest kcat/Km value for 2-hydroxy-6-oxohepta-2,4-dienoate Pseudomonas fluorescens
I199V the kcat/Km value of the single mutant is higher than that of the wild type enzyme Pseudomonas fluorescens
V227I the kcat/Km value of the single mutant is higher than that of the wild type enzyme Pseudomonas fluorescens

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens P96965
-
-
Pseudomonas fluorescens IP01 P96965
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
-
Pseudomonas fluorescens ?
-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
-
Pseudomonas fluorescens IP01 ?
-
?

Synonyms

Synonyms Comment Organism
CumD
-
Pseudomonas fluorescens
meta-cleavage product hydrolase
-
Pseudomonas fluorescens