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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.7.2.3 - trimethylamine-N-oxide reductase and Organism(s) Shewanella massilia and UniProt Accession O87948

for references in articles please use BRENDA:EC1.7.2.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Contains bis(molybdopterin guanine dinucleotide)molybdenum cofactor. The reductant is a membrane-bound multiheme cytochrome c. Also reduces dimethyl sulfoxide to dimethyl sulfide.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Shewanella massilia
UNIPROT: O87948
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Shewanella massilia
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
tmao reductase, trimethylamine n-oxide reductase, trimethylamine-n-oxide reductase, torecad, trimethylamine oxide reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
reductase, trimethylamine N-oxide
-
-
-
-
TMAO reductase
-
-
-
-
TOR
-
-
-
-
TorA
-
-
-
-
TorZ
-
-
-
-
trimethylamine oxide reductase
-
-
-
-
additional information
-
enzyme belongs to the TorD-family chaperones
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
trimethylamine:cytochrome c oxidoreductase
Contains bis(molybdopterin guanine dinucleotide)molybdenum cofactor. The reductant is a membrane-bound multiheme cytochrome c. Also reduces dimethyl sulfoxide to dimethyl sulfide.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-34-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylmorpholine N-oxide + electron donor
4-methylmorpholine + oxidized electron donor + H2O
show the reaction diagram
-
-
?
alpha-picoline N-oxide + electron donor
alpha-picoline + H2O + oxidized electron donor
show the reaction diagram
alpha-picoline N-oxide is not an efficient substrate for the enzyme
-
?
dimethylsulfoxide + electron donor
? + oxidized electron donor + H2O
show the reaction diagram
-
-
?
diphenylsulfoxide + electron donor
diphenylsulfide + oxidized electron donor + H2O
show the reaction diagram
-
-
-
?
L-methionine sulfoxide + electron donor
L-methionine + oxidized electron donor + H2O
show the reaction diagram
-
-
?
N,N-dimethyldodecylamine N-oxide + electron donor
N,N-dimethyldodecylamine + H2O + oxidized electron donor
show the reaction diagram
N,N-dimethyldodecylamine N-oxide is not an efficient substrate for the enzyme
-
?
nitrite + dibutylsulfoxide
?
show the reaction diagram
-
-
-
?
nitrite + DL-methionine sulfoxide
?
show the reaction diagram
-
-
-
?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
show the reaction diagram
-
-
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
show the reaction diagram
-
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
show the reaction diagram
-
-
?
additional information
?
-
-
enzyme is probably required for acquisition of molybdenum cofactor and translocation of the trimethylamine reductase TorA, EC 1.6.6.9, monomeric and dimeric enzyme forms bind to Tor A, the dimeric form binds more efficiently
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
show the reaction diagram
-
-
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
show the reaction diagram
-
-
?
additional information
?
-
-
enzyme is probably required for acquisition of molybdenum cofactor and translocation of the trimethylamine reductase TorA, EC 1.6.6.9, monomeric and dimeric enzyme forms bind to Tor A, the dimeric form binds more efficiently
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
-
pentahemic
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022
4-methylmorpholine N-oxide
-
0.61
alpha-picoline N-oxide
-
1
N,N-dimethyldodecylamine N-oxide
-
0.017
Trimethylamine N-oxide
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
109
4-methylmorpholine N-oxide
-
78
alpha-picoline N-oxide
-
4
dibutylsulfoxide
value below
4
Dimethylsulfoxide
value below
4
diphenylsulfoxide
value below
4
DL-methionine sulfoxide
value below
151
N,N-dimethyldodecylamine N-oxide
-
120
Trimethylamine N-oxide
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TORA_SHEMA
829
0
92362
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90000
1 * 90000, SDS-PAGE
19500
-
1 * 24100, monomeric form, small-angle X-ray scattering, 1 * 19500, monomeric form, Guinier analysis, 1 * 25000, monomeric form, non-denaturing PAGE, 1 * 24354-24356, mass spectrometry and sedimentation equilibrium analysis
24100
-
monomeric form, small-angle X-ray scattering
24350 - 24360
-
monomeric form, mass spectrometry and sedimentation equilibrium analysis
24356
-
2 * 24356, sedimentation equilibrium analysis, 2 * 27900, dimeric form, Guinier analysis
25000
-
1 * 24100, monomeric form, small-angle X-ray scattering, 1 * 19500, monomeric form, Guinier analysis, 1 * 25000, monomeric form, non-denaturing PAGE, 1 * 24354-24356, mass spectrometry and sedimentation equilibrium analysis
27900
-
2 * 24356, sedimentation equilibrium analysis, 2 * 27900, dimeric form, Guinier analysis
47800
-
dimeric form, small-angle X-ray scattering
48710
-
dimeric form, mass spectrometry and sedimentation equilibrium analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 90000, SDS-PAGE
dimer
-
2 * 24356, sedimentation equilibrium analysis, 2 * 27900, dimeric form, Guinier analysis
monomer
-
1 * 24100, monomeric form, small-angle X-ray scattering, 1 * 19500, monomeric form, Guinier analysis, 1 * 25000, monomeric form, non-denaturing PAGE, 1 * 24354-24356, mass spectrometry and sedimentation equilibrium analysis
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
recombinant monomeric, dimeric, and trimeric forms, hanging drop vapour diffusion method, 4°C, 0.001 ml of 1.2 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 220 mM NaCl, 10 mM DTT, mixed with equal volume of reservoir solution containing 1.6 M ammonium sulfate, 100 mM MES, pH 6.4, 4-6 days, cryoprotection by addition of 15% w/v ethylene glycerol to the reservoir solution, X-ray diffraction structure determination and analysis at 2.42 A resolution
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using ion exchange chromatography on DE52 column, chromatography on a Mono Q HR 16/10 column and preparative electrophoresis
recombinant His-tagged monomeric, dimeric, and trimeric forms from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity chromatography, and gel filtration for the the monomeric form
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplification of the structural torA gene encoding the enzyme and iits flanking regions using PCR techniques, the torA gene is the third gene of a TMAO-inducible operon, torECAD, encoding the TMAO respiratory components, the torC gene encodes a pentahemic c-type cytochrome, likely to be involved in electron transfer to the TorA terminal reductase, the role of the torE gene is unknown, torD gene encodes the TorD protein, a cytoplasmic protein involved in the folding process of the TorA precursor protein
gene torD, DNA sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3) as His-tagged protein
-
overexpression
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Czjzek, M.; Dos Santos, J.P.; Pommier, J.; Giordano, G.; Mejean, V.; Haser, R.
Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution
J. Mol. Biol.
284
435-447
1998
Shewanella massilia (O87948), Shewanella massilia, Shewanella massilia MR1 (O87948)
Manually annotated by BRENDA team
Dos Santos, J.; Iobbi-Nivol, C.; Couillault, C; Giordano, G.; Mejean, V.
Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species
J. Mol. Biol.
284
421-433
1998
Shewanella massilia (O87948), Shewanella massilia
Manually annotated by BRENDA team
Hatzixanthis, K.; Richardson, D.J.; Sargent, F.
Chaperones involved in assembly and export of N-oxide reductases
Biochem. Soc. Trans.
33
124-126
2005
Escherichia coli, Shewanella massilia
Manually annotated by BRENDA team
Tranier, S.; Mortier-Barriere, I.; Ilbert, M.; Birck, C.; Iobbi-Nivol, C.; Mejean, V.; Samama, J.P.
Characterization and multiple molecular forms of TorD from Shewanella massilia, the putative chaperone of the molybdoenzyme TorA
Protein Sci.
11
2148-2157
2002
Shewanella massilia
Manually annotated by BRENDA team