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Literature summary for 1.14.13.196 extracted from

  • Bufkin, K.; Sobrado, P.
    Characterization of the ornithine hydroxylation step in albachelin biosynthesis (2017), Molecules, 22, E1652 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of N-terminally His8-MBP-tagged enzyme in Escherichia coli as soluble protein Amycolatopsis alba

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic analysis Amycolatopsis alba
0.107
-
L-ornithine recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication Amycolatopsis alba
0.305
-
L-ornithine recombinant holo-enzyme, pH 7.5, temperature not specified in the publication Amycolatopsis alba

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-ornithine + NADH + H+ + O2 Amycolatopsis alba
-
N5-hydroxy-L-ornithine + NAD+ + H2O
-
?
L-ornithine + NADPH + H+ + O2 Amycolatopsis alba
-
N5-hydroxy-L-ornithine + NADP+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Amycolatopsis alba
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by metal affinity chromatography, depending on the imidazole concentration used, the recombinant enzyme is isolated either in the apo (FAD-free) or holo (FAD-bound) form, cleavage of the tag by TEV protease Amycolatopsis alba

Source Tissue

Source Tissue Comment Organism Textmining
additional information Amycolatopsis alba cells grown under iron-limiting conditions Amycolatopsis alba
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-ornithine + NADH + H+ + O2
-
Amycolatopsis alba N5-hydroxy-L-ornithine + NAD+ + H2O
-
?
L-ornithine + NADPH + H+ + O2
-
Amycolatopsis alba N5-hydroxy-L-ornithine + NADP+ + H2O
-
?
additional information holo (FAD-bound) and apo (FAD-free) forms of the enzyme hydroxylate ornithine. No activity with L-lysine. The enzyme displays very low selectivity for the reduced nicotinamide coenzyme Amycolatopsis alba ?
-
?

Synonyms

Synonyms Comment Organism
abachelin monooxygenase
-
Amycolatopsis alba
AMO
-
Amycolatopsis alba

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.2
-
L-ornithine recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication Amycolatopsis alba
0.34
-
L-ornithine recombinant holo-enzyme, pH 7.5, temperature not specified in the publication Amycolatopsis alba

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Amycolatopsis alba

Cofactor

Cofactor Comment Organism Structure
FAD
-
Amycolatopsis alba
NADH the enzyme displays very low selectivity for the reduced nicotinamide coenzyme Amycolatopsis alba
NADPH the enzyme displays very low selectivity for the reduced nicotinamide coenzyme Amycolatopsis alba

General Information

General Information Comment Organism
evolution AMO is a member of the N-hydroxylating monooxygenase (NMO) family of enzymes Amycolatopsis alba
metabolism the enzyme is an N-hydroxylating monooxygenase (NMO) catalyzing the ornithine hydroxylation step in albachelin biosynthesis Amycolatopsis alba

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.12
-
L-ornithine recombinant holo-enzyme, pH 7.5, temperature not specified in the publication Amycolatopsis alba
1.7
-
L-ornithine recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication Amycolatopsis alba