KEGG   ENZYME: 1.7.3.1
Entry
EC 1.7.3.1                  Enzyme                                 
Name
nitroalkane oxidase;
nitroethane oxidase;
NAO;
nitroethane:oxygen oxidoreductase
Class
Oxidoreductases;
Acting on other nitrogenous compounds as donors;
With oxygen as acceptor
Sysname
nitroalkane:oxygen oxidoreductase
Reaction(IUBMB)
a nitroalkane + H2O + O2 = an aldehyde or ketone + nitrite + H2O2 [RN:R10388 R10389]
Reaction(KEGG)
R10388 > R00799;
R10389
Substrate
nitroalkane [CPD:C06058];
H2O [CPD:C00001];
O2 [CPD:C00007]
Product
aldehyde [CPD:C00071];
ketone [CPD:C01450];
nitrite [CPD:C00088];
H2O2 [CPD:C00027]
Comment
Has an absolute requirement for FAD [4]. While nitroethane may be the physiological substrate [2], the enzyme also acts on several other nitroalkanes, including 1-nitropropane, 2-nitropropane, 1-nitrobutane, 1-nitropentane, 1-nitrohexane, nitrocyclohexane and some nitroalkanols [4]. Differs from EC 1.13.12.16, nitronate monooxygenase, in that the preferred substrates are neutral nitroalkanes rather than anionic nitronates [4].
History
EC 1.7.3.1 created 1961, modified 2006, modified 2009
Pathway
ec00910  Nitrogen metabolism
ec01100  Metabolic pathways
Orthology
K19823  nitroalkane oxidase
Genes
PANPODANSg2158 PODANSg4289
PBELQC761_506340
PPSDQC762_506340
TMNUCRPA7_3412
FGRFGSG_02379
FPUFPSE_06845
FVNFVRRES_02782
FVRFVEG_05969
FOXFOXG_08703
NHENECHADRAFT_81017
FFCNCS54_00761100
FKRNCS57_00801500
FMUJ7337_004795
CFJCFIO01_03827
CHIGCH63R_08266
ELAUCREL1_3529
PFYPFICI_01984
SSLSS1G_09730
BFUBCIN_07g06070
PSCOLY89DRAFT_617478 LY89DRAFT_709519
GLZGLAREA_03183
ANIANIA_09162
NFINFIA_030710
AFVAFLA_013415
TMFEYB26_001336
TRGTRUGW13939_02491
PNOSNOG_15929(SNOG_15928)
BZECOCCADRAFT_81440
BSCCOCSADRAFT_112376
BORCOCMIDRAFT_92255
FFUCLAFUR5_09879
CBETCB0940_06016 CB0940_08512
BCOMBAUCODRAFT_39353
NPAUCRNP2_4550
ADLAURDEDRAFT_71413
PLALFXN65_13835
VBOCKY39_23140
MPTMpe_A2676
METPC1M51_14750
HSEHsero_0937
HSZACP92_04690
HRBHrubri_0798
AVVRvVAT039_pl02080
AVIAvi_7637
BBTBBta_3103
BRSS23_32530
BRKCWS35_13395
BSYMCIT39_16315
BSEPHAP48_0007595
BQBJ4P68_0028370
BBANJ4G43_048315
BCOUIC761_06750 IC761_06755 IC761_34095
PSINCAK95_27115
NPNJI59_19965
RHARHA1_ro05247
RHBNY08_1957
RKOJWS14_36595
PDEFP9209_06210
SPINKV203_00865
SQZFQU76_30855
STSUB7R87_30865
LSEF1C12_09540
ARLAFL94_04845
GPRJQN66_05285
GNCQQS42_08525
PSIMKR76_25720
PDXPsed_2734 Psed_2948
PSEAWY02_17450
PBROHOP40_05335 HOP40_07760
PPELH6H00_00610 H6H00_09505
ACTYOG774_11345
BALADSM104299_04129(acdA_3)
 » show all
Reference
1  [PMID:14907722]
  Authors
LITTLE HN.
  Title
Oxidation of nitroethane by extracts from Neurospora.
  Journal
J Biol Chem 193:347-58 (1951)
Reference
2  [PMID:22538]
  Authors
Kido T, Hashizume K, Soda K.
  Title
Purification and properties of nitroalkane oxidase from Fusarium oxysporum.
  Journal
J Bacteriol 133:53-8 (1978)
DOI:10.1128/JB.133.1.53-58.1978
Reference
3  [PMID:11867731]
  Authors
Daubner SC, Gadda G, Valley MP, Fitzpatrick PF
  Title
Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl-CoA dehydrogenase superfamily.
  Journal
Proc Natl Acad Sci U S A 99:2702-7 (2002)
DOI:10.1073/pnas.052527799
  Sequence
Reference
4  [PMID:15581574]
  Authors
Fitzpatrick PF, Orville AM, Nagpal A, Valley MP.
  Title
Nitroalkane oxidase, a carbanion-forming flavoprotein homologous to acyl-CoA dehydrogenase.
  Journal
Arch Biochem Biophys 433:157-65 (2005)
DOI:10.1016/j.abb.2004.08.021
Reference
5  [PMID:15713081]
  Authors
Valley MP, Tichy SE, Fitzpatrick PF.
  Title
Establishing the kinetic competency of the cationic imine intermediate in nitroalkane oxidase.
  Journal
J Am Chem Soc 127:2062-6 (2005)
DOI:10.1021/ja043542f
Other DBs
ExplorEnz - The Enzyme Database: 1.7.3.1
IUBMB Enzyme Nomenclature: 1.7.3.1
ExPASy - ENZYME nomenclature database: 1.7.3.1
UM-BBD (Biocatalysis/Biodegradation Database): 1.7.3.1
BRENDA, the Enzyme Database: 1.7.3.1
CAS: 9029-36-1 65802-82-6

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