Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.8.1.2 extracted from

  • Asmara, W.; Murdiyatmo, U.; Baines, A.J.; Bull, A.T.; Hardman, D.J.
    Protein engineering of the 2-haloacid halidohydrolase IVa from Pseudomonas cepacia MBA4 (1993), Biochem. J., 292, 69-74.
No PubMed abstract available
Search for more literature for 3.8.1.2

Protein Variants

Protein Variants Comment Organism
additional information mutant library with reduced activity Burkholderia cepacia

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information comparison of KM of wild-type and mutant enzymes Burkholderia cepacia

Organism

Organism UniProt Comment Textmining
Burkholderia cepacia
-
 i.e. Pseudomonas cepacia MBA4
-
Burkholderia cepacia MBA4
-
 i.e. Pseudomonas cepacia MBA4
-

Purification (Commentary)

Purification (Comment) Organism
-
 Burkholderia cepacia

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-chloropropionate + H2O
-
 Burkholderia cepacia lactate + HCl
-
 ?
2-chloropropionate + H2O
-
 Burkholderia cepacia MBA4 lactate + HCl
-
 ?
monochloroacetate + H2O
-
 Burkholderia cepacia glycolate + HCl
-
 ?
monochloroacetate + H2O
-
 Burkholderia cepacia MBA4 glycolate + HCl
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information comparison of kcat of wild-type and mutant enzymes Burkholderia cepacia

pI Value

Organism Comment pI Value Maximum pI Value
Burkholderia cepacia the mutation from an acidic to a basic amino acid leads to an alteration in the enzyme pI valiue from 5.1 to 6.0
-
 5.1