Literature summary for 1.1.1.1 extracted from

Campbell, E.; Chuang, S.; Banta, S.
Modular exchange of substrate-binding loops alters both substrate and cofactor specificity in a member of the aldo-keto reductase superfamily (2013), Protein Eng. Des. Sel., 26, 181-186.

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Protein Variants

Protein Variants	Comment	Organism
additional information	replacement of three mobile loops positioned at the top of the canonical (alpha/beta)8-barrel structure by those from human aldose reductase. Replacement of Loops A and B is sufficient to impart from human aldose reductase activity into AdhD, and the resulting chimera retains the thermostability of the parent enzyme. No active chimeras are observed when the from human aldose reductase loops are grafted into a previously engineered cofactor specificity mutant of AdhD, which displays similar kinetics to from human aldose reductase with the model substrate DL-glyceraldehyde	Pyrococcus furiosus

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	Q8TZM9	-	-

Synonyms

Synonyms	Comment	Organism
AdhD	-	Pyrococcus furiosus

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Release 2023.1 (January 2023)