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IUBMB Comments The enzyme, found in some Actinobacteria, is involved in a pathway that forms nitrite, which is subsequently used to generate a diazo group in some secondary metabolites. Requires an FAD cofactor.
Synonyms
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BN159_4422
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creE
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(2S)-2-nitrosobutanedioate + NADPH + H+ + O2 = (2S)-2-nitrobutanedioate + NADP+ + H2O
1d
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-
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L-aspartate + 3 NADPH + 3 H+ + 3 O2 = (2S)-2-nitrobutanedioate + 3 NADP+ + 4 H2O
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L-aspartate + NADPH + H+ + O2 = N-hydroxy-L-aspartate + NADP+ + H2O
1a
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N,N-dihydroxy-L-aspartate = (2S)-2-nitrosobutanedioate + H2O
1c, spontaneous
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N-hydroxy-L-aspartate + NADPH + H+ + O2 = N,N-dihydroxy-L-aspartate + NADP+ + H2O
1b
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MetaCyc
nitrite biosynthesis
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L-aspartate,NADPH:oxygen oxidoreductase [(2S)-2-nitrobutanedioate-forming]
The enzyme, found in some Actinobacteria, is involved in a pathway that forms nitrite, which is subsequently used to generate a diazo group in some secondary metabolites. Requires an FAD cofactor.
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(2S)-2-nitrosobutanedioate + NADPH + H+ + O2
(2S)-2-nitrobutanedioate + NADP+ + H2O
Substrates: -
?
L-aspartate + 3 NADPH + 3 H+ + 3 O2
(2S)-2-nitrobutanedioate + 3 NADP+ + 4 H2O
L-aspartate + NADPH + H+ + O2
N-hydroxy-L-aspartate + NADP+ + H2O
Substrates: -
?
N-hydroxy-L-aspartate + NADPH + H+ + O2
N,N-dihydroxy-L-aspartate + NADP+ + H2O
Substrates: -
?
L-aspartate + 3 NADPH + 3 H+ + 3 O2
(2S)-2-nitrobutanedioate + 3 NADP+ + 4 H2O
Substrates: -
?
L-aspartate + 3 NADPH + 3 H+ + 3 O2
(2S)-2-nitrobutanedioate + 3 NADP+ + 4 H2O
Substrates: -
?
L-aspartate + 3 NADPH + 3 H+ + 3 O2
(2S)-2-nitrobutanedioate + 3 NADP+ + 4 H2O
Substrates: -
?
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(2S)-2-nitrosobutanedioate + NADPH + H+ + O2
(2S)-2-nitrobutanedioate + NADP+ + H2O
Substrates: -
?
L-aspartate + 3 NADPH + 3 H+ + 3 O2
(2S)-2-nitrobutanedioate + 3 NADP+ + 4 H2O
L-aspartate + NADPH + H+ + O2
N-hydroxy-L-aspartate + NADP+ + H2O
Substrates: -
?
N-hydroxy-L-aspartate + NADPH + H+ + O2
N,N-dihydroxy-L-aspartate + NADP+ + H2O
Substrates: -
?
L-aspartate + 3 NADPH + 3 H+ + 3 O2
(2S)-2-nitrobutanedioate + 3 NADP+ + 4 H2O
Substrates: -
?
L-aspartate + 3 NADPH + 3 H+ + 3 O2
(2S)-2-nitrobutanedioate + 3 NADP+ + 4 H2O
Substrates: -
?
L-aspartate + 3 NADPH + 3 H+ + 3 O2
(2S)-2-nitrobutanedioate + 3 NADP+ + 4 H2O
Substrates: -
?
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0.125
L-aspartate
30°C, pH not specified in the publication
0.055
NADPH
30°C, pH not specified in the publication
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1.14
L-aspartate
30°C, pH not specified in the publication
1.19
NADPH
30°C, pH not specified in the publication
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UniProt
brenda
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UniProt
brenda
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UniProt
brenda
Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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metabolism
CreE catalyzes iterative oxidation of L-aspartic acid to nitrosuccinic acid via N-hydroxyaspartic acid and nitrososuccinic acid. When CreE and CreD are incubated with L-aspartic acid, nitrous acid is the product. CreD accepts nitrosuccinic acid as a substrate only when it is directly delivered by CreE immediately after its synthesis. Both are involved in cremeomycin biosynthesis
physiological function
gene products of BN159_4422 and BN159_4421 synthesizes nitrous acid from L-aspartic acid. Both are involved in the synthesis of desferrioxamine derivatives
physiological function
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gene products of BN159_4422 and BN159_4421 synthesizes nitrous acid from L-aspartic acid. Both are involved in the synthesis of desferrioxamine derivatives
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CREE_STRCM
666
0
71483
Swiss-Prot
Secretory Pathway (Reliability: 1 )
CREEH_STRDJ
Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768)
650
0
71092
Swiss-Prot
-
NPAA_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
649
0
71149
Swiss-Prot
-
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recombinant protein, purified by Ni2+ affinity chromatography
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expression in Escherichia coli
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Hagihara, R.; Katsuyama, Y.; Sugai, Y.; Onaka, H.; Ohnishi, Y.
Novel desferrioxamine derivatives synthesized using the secondary metabolism-specific nitrous acid biosynthetic pathway in Streptomyces davawensis
J. Antibiot.
71
911-919
2018
Streptomyces davaonensis (K4QXN8), Streptomyces davaonensis, Streptomyces davaonensis DSM 101723 (K4QXN8)
brenda
Sugai, Y.; Katsuyama, Y.; Ohnishi, Y.
A nitrous acid biosynthetic pathway for diazo group formation in bacteria
Nat. Chem. Biol.
12
73-75
2016
Streptomyces cremeus (A0A0K2JL70)
brenda
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