Literature summary for 1.7.1.13 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 .

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Inhibitors

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

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O31678	-	-
Bacillus subtilis 168	O31678	-	-

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Release 2023.1 (January 2023)