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Literature summary 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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.99.28 structure at 2.7 A Zymomonas mobilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.99.28 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 ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.28 Zymomonas mobilis
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-
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.99.28 D-glucose + D-fructose
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 Zymomonas mobilis D-glucono-1,5-lactone + D-sorbitol
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 ?
1.1.99.28 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

EC Number Subunits Comment Organism
1.1.99.28 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

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