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

BRENDA support

Literature summary for 1.11.1.6 extracted from

  • Andre, C.; Kim, S.W.; Yu, X.H.; Shanklin, J.
    Fusing catalase to an alkane-producing enzyme maintains enzymatic activity by converting the inhibitory byproduct H2O2 to the cosubstrate O2 (2013), Proc. Natl. Acad. Sci. USA, 110, 3191-3196.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene katE, expression as fusion enzyme with aldehyde deformylating oxygenase, ADO, from Prochlorococcus marinus Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information catalase fusion ezyme with aldehyde deformylating oxygenase, i.e. CAT-ADO, turns over 225times versus 3times for the native ADO, and its expression in Escherichia coli increases catalytic turnovers per active site by fivefold relative to the expression of native ADO. Catalase protects ADO from inhibition by its reaction product H2O2 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 H2O2 Escherichia coli
-
O2 + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
gene katE
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 H2O2
-
Escherichia coli O2 + 2 H2O
-
?

Synonyms

Synonyms Comment Organism
Kat E catalase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli