1.14.13.196: L-ornithine N5-monooxygenase [NAD(P)H]

This is an abbreviated version!
For detailed information about L-ornithine N5-monooxygenase [NAD(P)H], go to the full flat file.

Reaction

Synonyms

abachelin monooxygenase, AfSidA, AMO, SidA, siderophore A

ECTree

1 Oxidoreductases

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

1.14.13.196 L-ornithine N5-monooxygenase [NAD(P)H]

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Results	in table
2054	AA Sequence
1	Application
3	Cloned(Commentary)
10	Cofactor
1	Crystallization (Commentary)
6	General Information
2	General Stability
3	Inhibitors
16	kcat/KM [mM/s]
2	Ki Value [mM]
17	KM Value [mM]
3	Molecular Weight [Da]
10	Natural Substrates/ Products (Substrates)
9	Organism
1	Pathway
29	PDB ID
3	pH Optimum
1	pI Value
2	Posttranslational Modification
1	Protein Variants
3	Purification (Commentary)
2	Reaction
9	Reference
1	Source Tissue
17	Substrates and Products (Substrate)
3	Subunits
13	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
18	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 1.14.13.196 - L-ornithine N5-monooxygenase [NAD(P)H]

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L-ornithine,NAD(P)H:oxygen oxidoreductase (N5-hydroxylating)

A flavoprotein (FAD). The enzyme from the pathogenic fungus Aspergillus fumigatus catalyses a step in the biosynthesis of the siderophores triacetylfusarinine and desferriferricrocin, while the enzyme from the bacterium Kutzneria sp. 744 is involved in the biosynthesis of piperazate, a building block of the kutzneride family of antifungal antibiotics. Activity of the fungal enzyme is higher with NADPH, due to the fact that following the reduction of the flavin, NADP+ (but not NAD+) stabilizes the C4a-hydroperoxyflavin intermediate that oxidizes the substrate [3]. cf. EC 1.14.13.195, L-ornithine N5-monooxygenase (NADPH).