Literature summary for 1.13.11.20 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 .

Search for more literature for 1.13.11.20

Activating Compound

Activating Compound	Comment	Organism	Structure
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)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
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
additional information	C93A and Y157F unliganded active site structures comparison	Rattus norvegicus
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

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	a non-heme iron enzyme	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	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

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
CDO	-	Rattus norvegicus
CDO1	-	Rattus norvegicus

General Information

General Information	Comment	Organism
additional information	wild-type and mutant active site structures, overview	Rattus norvegicus
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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)