Literature summary for 4.4.1.13 extracted from

Kaiser, J.T.; Bruno, S.; Clausen, T.; Huber, R.; Schiaretti, F.; Mozzarelli, A.; Kessler, D.
Snapshots of the cystine lyase C-DES during catalysis. Studies in solution and in the crystalline state (2003), J. Biol. Chem., 278, 357-365.

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Protein Variants

Protein Variants	Comment	Organism
K223A	inactive mutant enzyme	Synechocystis sp.

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp.	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
cocrystallization of wild-type enzyme and mutant enzyme K223A with cystine and cysteine	Synechocystis sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the catalytic mechanism is proposed involving interactions between cystine and active site residues Arg360, Arg369, and Trp251. These residues reorient during beta-elimination reaction, leading to the formation of a hydrophobic pocket that stabilizes the enolimine tautomer of the aminoacrylate and the cysteine persulfide product	Synechocystis sp.	?	-	?

Synonyms

Synonyms	Comment	Organism
C-DES	-	Synechocystis sp.
cystine lyase	-	Synechocystis sp.

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	enzyme is dependent on	Synechocystis sp.

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Release 2023.1 (January 2023)