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Literature summary for 1.1.99.28 extracted from

  • Halbig, D.; Wiegert, T.; Blaudeck, N.; Freudl, R.; Sprenger, G.A.
    The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding (1999), Eur. J. Biochem., 263, 543-551.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
K121A mutant enzyme is not processed within 60 min Zymomonas mobilis
K123A mutant enzyme shows processing behavior comparable to wild-type enzyme Zymomonas mobilis
S116D significantly retarded processing kinetics with residual unprocessed form being detectable even after 60 min Zymomonas mobilis
S116D/K121A/K123Q/I124K significantly retarded processing kinetics with residual unprocessed form being detectable even after 60 min Zymomonas mobilis

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm the efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding Zymomonas mobilis
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Organism

Organism UniProt Comment Textmining
Zymomonas mobilis
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification K123A mutant enzyme shows processing behavior comparable to wild-type enzyme, S116D mutant enzyme and S116D/K121A/K123Q/I124K mutant enzyme shows significantly retarded processing kinetics with residual unprocessed form being detectable even after 60 min, K121A mutant enzyme is not processed within 60 min Zymomonas mobilis

Cofactor

Cofactor Comment Organism Structure
NADP+ tightly bound Zymomonas mobilis