Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.7.3.1 - nitroalkane oxidase and Organism(s) Podospora anserina and UniProt Accession B2AM55

for references in articles please use BRENDA:EC1.7.3.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Has an absolute requirement for FAD . While nitroethane may be the physiological substrate , the enzyme also acts on several other nitroalkanes, including 1-nitropropane, 2-nitropropane, 1-nitrobutane, 1-nitropentane, 1-nitrohexane, nitrocyclohexane and some nitroalkanols . Differs from EC 1.13.11.16, nitronate monooxygenase, in that the preferred substrates are neutral nitroalkanes rather than anionic nitronates .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Podospora anserina
UNIPROT: B2AM55
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
  • 1.7.3.1
  • atlantic
  • oscillation
  • climate
  • winter
  • atmospheric
  • orange
  • robot
  • weather
  • acridine
  • ocean
  • interannual
  • summer
  • arctic
  • nai
  • phenology
  • cardiolipin
  • humanoid
  • forecast
  • warmer
  • nonyl
  • rainfall
  • meteorological
  • hydrological
  • seabird
  • snow
  • latitudinal
The taxonomic range for the selected organisms is: Podospora anserina
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
nao, nitroalkane oxidase, pa4202, nitroalkane-oxidizing enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nitroethane oxidase
-
-
-
-
nitroethane:oxygen oxidoreductase
-
-
-
-
oxidase, nitroethane
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
nitroalkane:oxygen oxidoreductase
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 1.13.11.16, nitronate monooxygenase, in that the preferred substrates are neutral nitroalkanes rather than anionic nitronates [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9029-36-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nitroethane + O2 + H2O
ethanal + nitrite + H2O2 + H+
show the reaction diagram
-
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
0.5 mM FAD is used in assay conditions
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10 - 25
nitroethane
0.39
O2
wild type enzyme, in 50 mM HEPES, pH 8.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037 - 15
nitroethane
15
O2
wild type enzyme, in 50 mM HEPES, pH 8.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 0.74
nitroethane
38
O2
wild type enzyme, in 50 mM HEPES, pH 8.0, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method, using 2.5 M magnesium sulfate, 0.1 M 2-(N-morpholino) ethanesulfonic acid buffer, pH 6.0, and 18% (v/v) glycerol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D399N
the mutation decreases the kcat/KM value for nitroethane over 2 orders of magnitude
R406K
the mutation decreases the kcat/KM value for nitroethane about 64fold
S373A
the mutation decreases the kcat/KM value for nitroethane about 3fold
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tormos, J.R.; Taylor, A.B.; Daubner, S.C.; Hart, P.J.; Fitzpatrick, P.F.
Identification of a hypothetical protein from Podospora anserina as a nitroalkane oxidase
Biochemistry
49
5035-5041
2010
Podospora anserina (B2AM55), Podospora anserina
Manually annotated by BRENDA team