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Literature summary extracted from

  • Alizade, M.A.; Brendel, K.; Gaede, K.
    Chirality of xylitol-oxidizing enzymes from mammalian liver (1976), FEBS Lett., 67, 41-44.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.9 cytoplasm
-
 Cavia porcellus 5737
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.9 Cavia porcellus
-
-
-
1.1.1.10 Cavia porcellus
-
 guinea pig
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.9 liver
-
 Cavia porcellus
-
1.1.1.10 liver
-
 Cavia porcellus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.9 D-ribitol + NAD+
-
 Cavia porcellus D-ribulose + NADH
-
 ?
1.1.1.9 D-sorbitol + NAD+
-
 Cavia porcellus D-fructose + NADH + H+
-
 ?
1.1.1.9 xylitol + NAD+
-
 Cavia porcellus D-xylulose + NADH + H+
-
 ?
1.1.1.10 xylitol + NADP+
-
 Cavia porcellus L-xylulose + NADPH + H+
-
 r

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.9 NAD+ stereochemistry of hydrogen transfer from xylitol, ribitol or sorbitol to NAD+ is of the (R)- or A-type Cavia porcellus
1.1.1.9 NADH
-
 Cavia porcellus
1.1.1.10 NAD+ preference for, coenzyme-binding domain is a beta-alpha-beta-fold typical for NAD+ dehydrogenases Cavia porcellus
1.1.1.10 NADP+ B-specific hydrogen transfer from xylitol to NADP+ Cavia porcellus