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Literature summary extracted from

  • Stehr, M.; Smau, L.; Singh, M.; Seth, O.; Macheroux, P.; Ghisla, S.; Diekmann, H.
    Studies with lysine N6-hydroxylase. Effect of a mutation in the assumed FAD binding site on coenzyme affinities and on lysine hydroxylating activity (1999), Biol. Chem., 380, 47-54.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.59 gene aerA, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and P14G mutant enzymes in strain M15-2, comparison of nucleotide sequences of enzyme-encoding genes iucD and aerA Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.59 P14G site-directed mutagenesis, requires different reaction conditions for full activity and shows altered cofactor specificity than the wild-type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.59 FAD inhibition of the wild-type and mutant P14G enzymes at very high concentrations Escherichia coli
1.14.13.59 L-lysine substrate inhibition of the wild-type and mutant P14G enzymes Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.59 additional information
-
 additional information kinetics Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.59 Escherichia coli
-
 gene aerA plasmid-encoded
-
1.14.13.59 Escherichia coli EN222
-
 gene aerA plasmid-encoded
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.59 recombinant His-tagged wild-type and P14G mutant enzymes from strain M15-2 to homogeneity by gel filtration, ion exchange and nickel affinity chromatography Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.13.59 0.00016
-
 recombinant mutant P14G, with 0.005 mM FAD, and NADPH Escherichia coli
1.14.13.59 0.0011
-
 recombinant mutant P14G, with 0.005 mM FAD, and iodine Escherichia coli
1.14.13.59 0.0039
-
 recombinant mutant P14G, with 0.3 mM FAD, and NADPH Escherichia coli
1.14.13.59 0.028
-
 recombinant mutant P14G, with 0.3 mM FAD, and iodine Escherichia coli
1.14.13.59 0.3
-
 recombinant wild-type enzyme, with 0.005 mM FAD, and iodine Escherichia coli
1.14.13.59 0.444
-
 recombinant wild-type enzyme, with 0.005 mM FAD, and NADPH Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.59 L-lysine + iodine + O2 iodine less effective than NADPH for the wild-type enzyme Escherichia coli N6-hydroxy-L-lysine + iodate + H2O
-
 ?
1.14.13.59 L-lysine + iodine + O2 iodine less effective than NADPH for the wild-type enzyme Escherichia coli EN222 N6-hydroxy-L-lysine + iodate + H2O
-
 ?
1.14.13.59 L-lysine + NADPH + O2 NADPH preferred compared to iodine for the wild-type enzyme Escherichia coli N6-hydroxy-L-lysine + NADP+ + H2O
-
 ?
1.14.13.59 L-lysine + NADPH + O2 NADPH preferred compared to iodine for the wild-type enzyme Escherichia coli EN222 N6-hydroxy-L-lysine + NADP+ + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.59 More comparison of amino acid sequences of enzyme-encoding genes iucD and aerA Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.14.13.59 LH
-
 Escherichia coli
1.14.13.59 Lysine N6-hydroxylase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.59 25
-
 assay at with NADPH as cofactor Escherichia coli
1.14.13.59 37
-
 assay at with iodine as cofactor Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.59 7
-
 P14G mutant Escherichia coli
1.14.13.59 8
-
 wild-type enzyme Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.14.13.59 additional information
-
 pH-profile of wild-type and mutant P14G enzymes Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.59 FAD binding site includes an unusual proline residue Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.14.13.59 additional information
-
 additional information inhibition kinetics Escherichia coli