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Literature summary extracted from

  • Driggers, C.M.; Kean, K.M.; Hirschberger, L.L.; Cooley, R.B.; Stipanuk, M.H.; Karplus, P.A.
    Structure-based insights into the role of the Cys-Tyr crosslink and inhibitor recognition by mammalian cysteine dioxygenase (2016), J. Mol. Biol., 428, 3999-4012 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.13.11.20 additional information the enzyme activity is in part modulated by the formation of a Cys93-Tyr157 crosslink that increases its catalytic efficiency over 10fold, mechanism, overview. The crosslink enhances activity by positioning the Tyr157 hydroxyl to enable proper Cys binding, proper oxygen binding, and optimal chemistry Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.20 generation of 21 CDO crystal structures at resolutions between 1.25 and 1.65 A. Of these, 16 are of C93A or Y157F CDO mutants either alone or bound to L-Cys, D-Cys, or the inhibitor homocysteine, the other five are of wild-type CDO bound to homocysteine, azide, or thiosulfate. Cys-soaked wild-type CDO crystals are analysed at pH 6.2 and pH 8.0, detailed overview Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.20 C93A site-directed mutagenesis, mutation of the active site residue, no crosslink formation resulting in reduced activity compared to the wild-type enzyme. The mutant variant structure has a new chloride ion coordinating the active site iron. Cys binding is also different from wild-type CDO, and no Cys-persulfenate forms in the C93A active site at pH 6.2 or pH 8.0 Rattus norvegicus
1.13.11.20 additional information C93A and Y157F unliganded active site structures comparison Rattus norvegicus
1.13.11.20 Y157F site-directed mutagenesis, mutation of the active site residue, no crosslink formation resulting in reduced activity compared to the wild-type enzyme. The mutant variant structure has a new chloride ion coordinating the active site iron. Cys binding is also different from wild-type CDO, and no Cys-persulfenate forms in the Y157F active site at pH 6.2 or pH 8.0 Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.20 azide competitive inhibitor, binding structure, overview. Azide does not bind in the enzyme crystal as a superoxide mimic Rattus norvegicus
1.13.11.20 D-Cys competitive inhibitor, binding structure, overview Rattus norvegicus
1.13.11.20 homocysteine competitive inhibitor, binding structure, overview Rattus norvegicus
1.13.11.20 thiosulfate competitive inhibitor, binding structure, overview Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.20 Fe2+ a non-heme iron enzyme Rattus norvegicus

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.20 Rattus norvegicus P21816
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.13.11.20 additional information the enzyme activity is in part modulated by the formation of a Cys93-Tyr157 crosslink that increases its catalytic efficiency over 10fold, mechanism, overview. The crosslink enhances activity by positioning the Tyr157 hydroxyl to enable proper Cys binding, proper oxygen binding, and optimal chemistry Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.20 L-cysteine + O2 = 3-sulfinoalanine reaction mechanism Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.20 L-cysteine + O2
-
Rattus norvegicus 3-sulfinoalanine
-
?
1.13.11.20 additional information homocysteine and D-Cys are no substrates Rattus norvegicus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.20 CDO
-
Rattus norvegicus
1.13.11.20 CDO1
-
Rattus norvegicus

General Information

EC Number General Information Comment Organism
1.13.11.20 additional information wild-type and mutant active site structures, overview Rattus norvegicus
1.13.11.20 physiological function cysteine dioxygenase (CDO) helps regulate Cys levels through converting Cys to Cys sulfinic acid. The enzyme activity is in part modulated by the formation of a Cys93-Tyr157 crosslink that increases its catalytic efficiency over 10fold, mechanism, overview. The crosslink enhances activity by positioning the Tyr157 hydroxyl to enable proper Cys binding, proper oxygen binding, and optimal chemistry Rattus norvegicus