Literature summary extracted from

Mohammad, A.; Bon Ramos, A.; Lee, B.W.; Cohen, S.W.; Kiani, M.K.; Iwata-Reuyl, D.; Stec, B.; Swairjo, M.A.
Protection of the queuosine biosynthesis enzyme QueF from irreversible oxidation by a conserved intramolecular disulfide (2017), Biomolecules, 7, E30 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.7.1.13	-	Bacillus subtilis

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.7.1.13	structure of mutant E97Q, displays an intramolecular disulfide formed between the catalytic Cys55 and a conserved Cys99 located near the active site. This structure exhibits major rearrangement of the loops responsible for substrate binding	Bacillus subtilis

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.7.1.13	C99A	mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible	Bacillus subtilis
1.7.1.13	C99S	mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible	Bacillus subtilis

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.7.1.13	peroxide	peroxide-induced inactivation of the wild-type enzyme is reversible with thioredoxin	Bacillus subtilis

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.7.1.13	Bacillus subtilis	O31678	-	-
1.7.1.13	Bacillus subtilis 168	O31678	-	-

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Release 2023.1 (January 2023)