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Literature summary for 1.3.8.13 extracted from

  • Preusser, A.; Wagner, U.; Elssner, T.; Kleber, H.P.
    Crotonobetaine reductase from Escherichia coli consists of two proteins (1999), Biochim. Biophys. Acta, 1431, 166-178.
    View publication on PubMed
Search for more literature for 1.3.8.13

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41500
-
 4 * 41500, SDS-PAGE Escherichia coli
164400
-
 gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P60584
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
233
-
 pH 7.5, 22°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
crotonobetaine + reduced benzylviologen
-
 Escherichia coli gamma-butyrobetaine + oxidized benzylviologen
-
 ?
additional information presence of L-carnitine dehydratase is required for enzymatic activity Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 41500, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
caiA
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD contains non-covalently bound FAD in a molar ratio of 1:1 Escherichia coli

pI Value

Organism Comment pI Value Maximum pI Value
Escherichia coli
-
-
 5.6

General Information

General Information Comment Organism
physiological function presence of L-carnitine dehydratase is required for enzymatic activity. In the crotonobetaine reductase reaction one dimer of L-carnitine dehydratase associates with one tetramer of crotonobetaine reductase. A further low-molecular-mass effector described for the L-carnitine dehydratase is also necessary for crotonobetaine reductase activity Escherichia coli