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Literature summary for 1.1.99.28 extracted from

  • Kingston, R.L.; Scopes, R.K.; Baker, E.N.
    The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP (1996), Structure, 4, 1413-1428.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
structure at 2.7 A Zymomonas mobilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-Glucose + D-fructose Zymomonas mobilis the enzyme produces the solute sorbitol by reduction of fructose, coupled with the oxidation of glucose to gluconolactone and thereby protects the bacterium against osmotic shock in sugar-rich environment ?
-
 ?

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + D-fructose
-
 Zymomonas mobilis D-glucono-1,5-lactone + D-sorbitol
-
 ?
D-Glucose + D-fructose the enzyme produces the solute sorbitol by reduction of fructose, coupled with the oxidation of glucose to gluconolactone and thereby protects the bacterium against osmotic shock in sugar-rich environment Zymomonas mobilis ?
-
 ?

Subunits

Subunits Comment Organism
tetramer each subunit of the tetramer comprises two domains, a classical dinucleotide-binding domain, and a C-terminal domain based on a predominantly antiparallel nine-stranded beta sheet Zymomonas mobilis

Cofactor

Cofactor Comment Organism Structure
NADP+ tightly bound as hydrogen carrier Zymomonas mobilis
NADPH tightly bound as hydrogen carrier Zymomonas mobilis