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Literature summary for 1.1.1.431 extracted from

  • Khoury, G.A.; Fazelinia, H.; Chin, J.W.; Pantazes, R.J.; Cirino, P.C.; Maranas, C.D.
    Computational design of Candida boidinii xylose reductase for altered cofactor specificity (2009), Protein Sci., 18, 2125-2138 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.431

Organism

Organism UniProt Comment Textmining
[Candida] boidinii
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylose + NADH + H+ using a modified iterative protein redesign and optimization workflow, a sets of mutations is identified that change the nicotinamide cofactor specificity of xylose reductase (CbXR) from its physiological preference for NADPH, to the alternate cofactor NADH [Candida] boidinii xylitol + NAD+
-
 ?
D-xylose + NADPH + H+ using a modified iterative protein redesign and optimization workflow, a sets of mutations is identified that change the nicotinamide cofactor specificity of xylose reductase (CbXR) from its physiological preference for NADPH, to the alternate cofactor NADH [Candida] boidinii xylitol + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
CbXR
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 [Candida] boidinii
xylose reductase
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 [Candida] boidinii

Cofactor

Cofactor Comment Organism Structure
NADH using a modified iterative protein redesign and optimization workflow, a sets of mutations is identified that change the nicotinamide cofactor specificity of xylose reductase (CbXR) from its physiological preference for NADPH, to the alternate cofactor NADH [Candida] boidinii
NADPH using a modified iterative protein redesign and optimization workflow, a sets of mutations is identified that change the nicotinamide cofactor specificity of xylose reductase (CbXR) from its physiological preference for NADPH, to the alternate cofactor NADH [Candida] boidinii