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Literature summary for 1.14.13.59 extracted from

  • Thariath, A.M.; Fatum, K.L.; Valvano, M.A.; Viswanatha, T.
    Physico-chemical characterization of a recombinant cytoplasmic form of lysine:N6-hydroxylase (1993), Biochim. Biophys. Acta, 1203, 27-35.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Carbonylcyanide-m-chlorophenylhydrazone
-
Escherichia coli
Carbonylcyanide-p-fluoromethoxyphenylhydrazone
-
Escherichia coli
Cinnamylidene
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
NADPH recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Escherichia coli 5737
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.168
-
-
Escherichia coli

Storage Stability

Storage Stability Organism
4°C, medium of ionic strength 0.25 or higher, recombinant enzyme form IacD398, stable for 1 month Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-2-Aminoethyl-L-Cys + NADPH + O2
-
Escherichia coli ?
-
?
L-Lys + NADH + O2 with lower efficiency than NADPH, recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus Escherichia coli ?
-
?
L-Lys + NADPH + O2
-
Escherichia coli N6-Hydroxy-L-Lys + NADP+ + H2O
-
?

Cofactor

Cofactor Comment Organism Structure
FAD Km: 0.0051 mM Escherichia coli
FAD requires FAD Escherichia coli
NADH recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus Escherichia coli
NADPH required Escherichia coli