Literature summary for 1.1.1.320 extracted from

Rabuffetti, M.; Cannazza, P.; Contente, M.; Pinto, A.; Romano, D.; Hoyos, P.; Alcantara, A.; Eberini, I.; Laurenzi, T.; Gourlay, L.; Di Pisa, F.; Molinari, F.
Structural insights into the desymmetrization of bulky 1,2-dicarbonyls through enzymatic monoreduction (2021), Bioorg. Chem., 108, 104644 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme KRED1-Pglu, X-ray diffraction structure determination and analysis at 1.77 A resolution	Ogataea glucozyma

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
benzil + NADPH + H+	Ogataea glucozyma	-	(S)-benzoin + NADP+	-	r

Organism

Organism	UniProt	Comment	Textmining
Ogataea glucozyma	A0A0H4SN47	Pichia glucozyma	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
benzil + NADPH + H+	-	Ogataea glucozyma	(S)-benzoin + NADP+	-	r
additional information	the enzyme is preferentiallly active on aromatic 1,2-diketones. It catalyzes the stereoselective monoreduction and desymmerization of bulky dicarbonyls. Mechanism and in silico prediction of substrates reactivity, overview	Ogataea glucozyma	?	-	-

Synonyms

Synonyms	Comment	Organism
benzil reductase	-	Ogataea glucozyma
KRED1-Pglu	-	Ogataea glucozyma

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	-	Ogataea glucozyma
NADPH	-	Ogataea glucozyma

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Release 2023.1 (January 2023)