Literature summary for 2.8.1.2 extracted from

Spallarossa, A.; Forlani, F.; Carpen, A.; Armirotti, A.; Pagani, S.; Bolognesi, M.; Bordo, D.
The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: Crystal structure of SseA from Escherichia coli (2004), J. Mol. Biol., 335, 583-593.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
3-mercaptopyruvate + cyanide	Escherichia coli	-	pyruvate + thiocyanate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P31142	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin	mechanism	Escherichia coli	a
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin	sulfur transfer mechanism involving C237 as the nucleophilic species and H66, R102 and D262 as residues assisting catalysis	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3-mercaptopyruvate + cyanide	-	Escherichia coli	pyruvate + thiocyanate	-	?

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Release 2023.1 (January 2023)