Enzyme

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     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
ID:1.14.13.196
Description:L-ornithine N(5)-monooxygenase (NAD(P)H).
Cath: 3.50.50.60;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.13.196
BRENDA Enzyme Link: BRENDA 1.14.13.196
KEGG Enzyme Link: KEGG1.14.13.196
BioCyc Enzyme Link: BioCyc 1.14.13.196
ExPASy Enzyme Link: ExPASy1.14.13.196
EC2PDB Enzyme Link: EC2PDB 1.14.13.196
ExplorEnz Enzyme Link: ExplorEnz 1.14.13.196
PRIAM enzyme-specific profiles Link: PRIAM 1.14.13.196
IntEnz Enzyme Link: IntEnz 1.14.13.196
MEDLINE Enzyme Link: MEDLINE 1.14.13.196
MSA:

1.14.13.196;

Phylogenetic Tree:

1.14.13.196;

Uniprot:
M-CSA:
RHEA:41512 L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+)
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]-[NH2;+0:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:9]-[NH;+0:10]-[OH;+0:11].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[OH2;+0:12]
Reaction
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References

TitleAuthorsDatePubMed ID
sid1, a gene initiating siderophore biosynthesis in Ustilago maydis: molecular characterization, regulation by iron, and role in phytopathogenicity.Mei B, Budde AD, Leong SA1993 Feb 18430103
Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases.Franceschini S, Fedkenheuer M, Vogelaar NJ, Robinson HH, Sobrado P, Mattevi A2012 Sep 1122928747
Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase.Mayfield JA, Frederick RE, Streit BR, Wencewicz TA, Ballou DP, DuBois JL2010 Oct 120650894
Aspergillus fumigatus SidA is a highly specific ornithine hydroxylase with bound flavin cofactor.Chocklett SW, Sobrado P2010 Aug 1020614882
dffA gene from Aspergillus oryzae encodes L-ornithine N5-oxygenase and is indispensable for deferriferrichrysin biosynthesis.Yamada O, Na Nan S, Akao T, Tominaga M, Watanabe H, Satoh T, Enei H, Akita O200316233371

RHEA:41508 L-ornithine + NADPH + O2 = H2O + N(5)-hydroxy-L-ornithine + NADP(+)
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]-[NH2;+0:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:9]-[NH;+0:10]-[OH;+0:11].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[OH2;+0:12]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
sid1, a gene initiating siderophore biosynthesis in Ustilago maydis: molecular characterization, regulation by iron, and role in phytopathogenicity.Mei B, Budde AD, Leong SA1993 Feb 18430103
Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in Pseudomonas aeruginosa.Visca P, Ciervo A, Orsi N1994 Feb8106324
Consecutive enzymatic modification of ornithine generates the hydroxamate moieties of the siderophore erythrochelin.Robbel L, Helmetag V, Knappe TA, Marahiel MA2011 Jul 1221650455
Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase.Mayfield JA, Frederick RE, Streit BR, Wencewicz TA, Ballou DP, DuBois JL2010 Oct 120650894
Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction.Meneely KM, Barr EW, Bollinger JM Jr, Lamb AL2009 May 2619368334
Delta-amino group hydroxylation of L-ornithine during coelichelin biosynthesis.Pohlmann V, Marahiel MA2008 May 2118452021
Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism.Meneely KM, Lamb AL2007 Oct 2317900176
Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa.Ge L, Seah SY2006 Oct17015659
dffA gene from Aspergillus oryzae encodes L-ornithine N5-oxygenase and is indispensable for deferriferrichrysin biosynthesis.Yamada O, Na Nan S, Akao T, Tominaga M, Watanabe H, Satoh T, Enei H, Akita O200316233371