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

BRENDA support

Literature summary for 1.13.11.20 extracted from

  • Tchesnokov, E.P.; Faponle, A.S.; Davies, C.G.; Quesne, M.G.; Turner, R.; Fellner, M.; Souness, R.J.; Wilbanks, S.M.; de Visser, S.P.; Jameson, G.N.
    An iron-oxygen intermediate formed during the catalytic cycle of cysteine dioxygenase (2016), Chem. Commun. (Camb.), 52, 8814-8817 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.11.20

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of Strep-tagged enzyme Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
C93G site-directed mutagenesis Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information stopped-flow kinetics of wild-type and mutant enzymes Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required for activity, an iron-oxygen intermediate is formed during the catalytic cycle of cysteine dioxygenase, Moessbauer spectroscopy analysis resuting in three different species: CDO:FeII, CDO:FeII:cysteine site I, and CDO:FeII:cysteine site II, dissociation constants, absorptions spectra, and structure analysis, detailed overview Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-cysteine + O2 Rattus norvegicus
-
 3-sulfinoalanine
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P21816
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information residues C93-Y157 crosslink as a result of a posttranslational modification Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
recombinant Strep-tagged enzyme Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
L-cysteine + O2 = 3-sulfinoalanine proposed catalytic cycle of CDO enzymes: the pentacoordinated resting state structure can convert to a hexacoordinated structure by binding of water. Upon binding of molecular oxygen the water molecule is displaced and an iron(III)-superoxo structure is formed. The terminal oxygen atom of the iron(III)-superoxo group attacks the sulfur of the cysteinate group to form a ring-structure, which can homogeneously split into a sulfoxide and iron(IV)-oxo species. The sulfoxide-bound complex rotates from sulfur-bound to oxygen-bound to the iron center. The latter transfers the oxygen atom from the iron(IV)-oxo group to substrate in a final step to form cysteine sulfinic acid product complex Rattus norvegicus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + O2
-
 Rattus norvegicus 3-sulfinoalanine
-
 ?
L-cysteine + O2 anaerobic CDO reaction conditions Rattus norvegicus 3-sulfinoalanine
-
 ?
additional information formation of an active CDO:cysteine substrate complex Rattus norvegicus ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Rattus norvegicus