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Information on EC 1.13.11.20 - cysteine dioxygenase and Organism(s) Bacillus subtilis and UniProt Accession O32085

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IUBMB Comments
Requires Fe2+ and NAD(P)H.
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This record set is specific for:
Bacillus subtilis
UNIPROT: O32085
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
cysteine dioxygenase, cysteine oxidase, cysteine dioxygenase type 1, bscdo, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cysteine oxidase
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-
-
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oxygenase, cysteine di-
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-cysteine + O2 = 3-sulfinoalanine
show the reaction diagram
reaction mechanism and structure-function analysis
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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-
SYSTEMATIC NAME
IUBMB Comments
L-cysteine:oxygen oxidoreductase
Requires Fe2+ and NAD(P)H.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-59-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-cysteine + O2
3-sulfino-L-alanine
show the reaction diagram
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
show the reaction diagram
-
-
-
?
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
L-cysteine + O2
3-sulfinoalanine
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-amino-ethanethiol
YubC: 1 x the Km for cysteine = 12% inhibition, 10 x the Km for cysteine = 19% inhibition
2-sulfanyl-ethanol
YubC: 1 x the Km for cysteine = -0.7% inhibition, 10 x the Km for cysteine = 6.6% inhibition
3-sulfanyl-propionic acid
YubC: 1 x the Km for cysteine = 4.7% inhibition, 10 x the Km for cysteine = 11% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
cysteine
YubC, measurement of cysteine sulfinic acid production is done by high-performance liquid chromatography
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.39
L-cysteine
YubC
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
YubC, pH optimum is determined by using 2-morpholinoethanesulfonic acid or Tris buffers at a final concentration of 62.5 mM
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
analysis of examples for two structural genomics groups of CDOs: a Bacillus subtilis Arg-type enzyme that has cysteine dioxygenase activity (BsCDO), and a Ralstonia eutropha Gln-type CDO homologue of uncharacterized activity (ReCDOhom), overview. The BsCDO active site is well conserved with mammalian CDO, and a cysteine complex captured in the active site confirms that the cysteine binding mode is also similar. The Arg position is not compatible with the mode of Cys binding seen in both Rattus norvegicus CDO and Bacillus subtilis CDO. Gln-type CDO homologues are not authentic CDOs but have substrate specificity more similar to 3-mercaptopropionate dioxygenases
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme free or with bound substrate L-Cys, hanging drop vapour diffusion method, mixing of 0.004 ml of 10 mg/ml protein solution with 0.004 ml of reservoir solution containing 18% w/v PEG 4000, 0.1 M potassium acetate, 0.05 M 2-(N-morpholino)ethanesulfonic acid, pH 6.0, 25°C, 2-7 days, X-ray diffraction structure determination and analysis at 2.38-2.82 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap HP column, immobilized metal affinity chromatography, during purification two peaks of highly purified recombinant protein are found to elute: one at 10% (peak1) and the second at 20%(peak 2), kinetic datat show that peak 1 has lower Km and higher Vmax values for cysteine thant peak 2.
recombinant enzyme from Escherichia coli strain BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cdoA, recombinant enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia cli strain DH5alpha
the open reading frame of putative cysteine dioxygenase NP_390992(yubC, Bacillus subtilis) is cloned and overexpressed in Escherichia coli.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dominy, J.E.; Simmons, C.R.; Karplus, P.A.; Gehring, A.M.; Stipanuk, M.H.
Identification and characterization of bacterial cysteine dioxygenases: a new route of cysteine degradation for eubacteria
J. Bacteriol.
188
5561-5569
2006
Bacillus cereus (Q81CX4), Bacillus cereus, Bacillus cereus DSM 31 (Q81CX4), Bacillus subtilis (O32085), Bacillus subtilis, no activity in Nostoc sp., Rattus norvegicus (P21816), Streptomyces coelicolor (O50490), Streptomyces coelicolor (Q9KZL0), Streptomyces coelicolor A3(2) SCO3035 (Q9KZL0), Streptomyces coelicolor A3(2) SCO5772 (O50490)
Manually annotated by BRENDA team
Driggers, C.M.; Hartman, S.J.; Karplus, P.A.
Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs
Protein Sci.
24
154-161
2015
Bacillus subtilis (O32085), Bacillus subtilis, Bacillus subtilis 168 (O32085)
Manually annotated by BRENDA team