1.14.13.195: L-ornithine N5-monooxygenase (NADPH)
This is an abbreviated version!
For detailed information about L-ornithine N5-monooxygenase (NADPH), go to the full flat file.
Word Map on EC 1.14.13.195
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1.14.13.195
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flavin
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fumigatus
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aspergillus
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flavin-dependent
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pyoverdine
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nadp+
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c4a-hydroperoxyflavin
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hydroxamate
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hydroxamate-containing
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flavin-containing
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non-ribosomal
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half-reaction
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n-hydroxylating
- 1.14.13.195
- flavin
- fumigatus
- aspergillus
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flavin-dependent
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pyoverdine
- nadp+
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c4a-hydroperoxyflavin
- hydroxamate
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hydroxamate-containing
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flavin-containing
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non-ribosomal
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half-reaction
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n-hydroxylating
Reaction
Synonyms
Af-OMO, CchB, flavin-dependent monooxygenase, L-Orn N5-oxygenase, L-ornithine N5-hydroxylase, L-ornithine-Ndelta-oxygenase, monooxygenase EtcB, omega-amino acid monooxygenase, ornithine hydroxylase, ornithine N5-monooxygenase, PsbA, PvdA, SidA, siderophore A
ECTree
1.14.13.195 L-ornithine N5-monooxygenase (NADPH)Advanced search results
results (
results (Engineering
Engineering on EC 1.14.13.195 - L-ornithine N5-monooxygenase (NADPH)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
N293A
site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type
N323A
site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type, and to increased rate constant for flavin reduction by NADPH by 18fold
S257A
Q5SE95
the interaction between residue Ser257 and NADP(H) is essential for stabilization of the C4a-hydroperoxyflavin intermediate. Ser257 may function as a pivot point, allowing the nicotinamide of NADP+ to slide into position for stabilization of the C4a-hydroperoxyflavin
S469A
site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type
additional information
additional information
construction of diverse inactive truncation mutants, overview
additional information
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construction of diverse inactive truncation mutants, overview
additional information
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construction of PvdA-PhoA fusion protein mutantsa nd of a pvdA deletion mutant strain
additional information
a PsbA-defective mutant B10CA1 is fully complemented by addition of L-ornithine N5-oxide, the mutant strain shows impaired synthesis of fluorescent pigment and hydroxamate nitrogen in iron-poor medium, as well as defective biosynthesis of both forms of pseudobactin and salicylate-based siderophores, Fe3+ transfer is impaired, phenotype, overview
additional information
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a PsbA-defective mutant B10CA1 is fully complemented by addition of L-ornithine N5-oxide, the mutant strain shows impaired synthesis of fluorescent pigment and hydroxamate nitrogen in iron-poor medium, as well as defective biosynthesis of both forms of pseudobactin and salicylate-based siderophores, Fe3+ transfer is impaired, phenotype, overview
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