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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.8.2.1 - sulfite dehydrogenase (cytochrome) and Organism(s) Gallus gallus and UniProt Accession P07850

for references in articles please use BRENDA:EC1.8.2.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Associated with cytochrome c-551. The enzyme from the bacterium Starkeya novella contains a molybdopyranopterin cofactor and a smaller monoheme cytochrome c subunit. cf. EC 1.8.5.6, sulfite dehydrogenase (quinone).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Gallus gallus
UNIPROT: P07850
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Gallus gallus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
sulfite dehydrogenase, sorab, sir-fp18, sulfite cytochrome c reductase, sulfite oxidoreductase, sulfate oxidase, sulphite:cytochrome c oxidoreductase, sulfite ferricytochrome-c oxidoreductase, multiheme cytochrome c sulfite reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfate oxidase
-
sulfite oxidase
-
dehydrogenase, sulfite
-
-
-
-
sulfite cytochrome c reductase
-
-
-
-
sulfite oxidase
-
-
-
-
sulfite-cytochrome c oxidoreductase
-
-
-
-
sulphite:cytochrome c oxidoreductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
sulfite:ferricytochrome-c oxidoreductase
Associated with cytochrome c-551. The enzyme from the bacterium Starkeya novella contains a molybdopyranopterin cofactor and a smaller monoheme cytochrome c subunit. cf. EC 1.8.5.6, sulfite dehydrogenase (quinone).
CAS REGISTRY NUMBER
COMMENTARY hide
37256-47-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
show the reaction diagram
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
show the reaction diagram
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
show the reaction diagram
ferricytochrome c is the physiological electron acceptor
-
-
?
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
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
show the reaction diagram
ferricytochrome c is the physiological electron acceptor
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdopterin
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
the enzyme contains a molybdenum center
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SUOX_CHICK
459
0
50205
Swiss-Prot
other Location (Reliability: 3)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the C185S variant is crystallized by the hanging drop vapor diffusion method using 15% (v/v) 2-methyl-2,4-pentanediol, 2% PEG 4000 (w/v), and 100 mM sodium acetate (pH 5.0) and in the presence of sulfite using 2% PEG 4000 (w/v), 10% MPD (v/v), 100 mM sodium acetate (pH 5.0) and 0.5 mM sodium sulfite. The C185A variant is crystallized by the sitting drop vapor diffusion method, using 15% (w/v) PEG 4000, 150 mM (NH4)2SO4, and 100 mM MES (pH 6.0)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C185A
the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor
C185S
the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
phenyl-Sepharose column chromatography and Superdex-200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli TP1000 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Qiu, J.A.; Wilson, H.L.; Pushie, M.J.; Kisker, C.; George, G.N.; Rajagopalan, K.V.
The structures of the C185S and C185A mutants of sulfite oxidase reveal rearrangement of the active site
Biochemistry
49
3989-4000
2010
Gallus gallus (P07850)
Manually annotated by BRENDA team
Hernandez-Marin, E.; Ziegler, T.
Theoretical study of the oxidation reaction and electron spin resonance parameters involving sulfite oxidase
Inorg. Chem.
48
1323-1333
2009
Gallus gallus (P07850)
Manually annotated by BRENDA team