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Literature summary for 1.1.99.28 extracted from

  • Lott, J.S.; Halbig, D.; Baker, H.M.; Hardman, M.J.; Sprenger, G.A.; Baker, E.N.
    Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation (2000), J. Mol. Biol., 304, 575-584.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
vapour diffusion in hanging drops, crystal structure of the NAD+ complex of a truncated form of the enzyme, GFORDELTA1-22/S64D, in which the first 22 residues of the N-terminal arm of the mature protein have been deleted, structure refined at 2.7 A resolution shows that the truncated form of the enzyme forms a dimer and implies that the N-terminal arm is essential for tetramer formation by wild-type GFOR Zymomonas mobilis

Protein Variants

Protein Variants Comment Organism
DELTA1-22/S64D S64D mutation converts the strict NADP+ spoecificity of wild-type GFOR to a dual NADP+/NAD+ specificity Zymomonas mobilis

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Zymomonas mobilis
-
-

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis Q07982
-
-

Subunits

Subunits Comment Organism
tetramer the N-terminal arm is essential for tetramer formation by wild-type GFOR Zymomonas mobilis

Synonyms

Synonyms Comment Organism
GFOR
-
Zymomonas mobilis
glucose-fructose oxidoreductase
-
Zymomonas mobilis

Cofactor

Cofactor Comment Organism Structure
NAD+ S64D mutation converts the strict NADP+ specificity of wild-type GFOR to a dual NADP+/NAD+ specificity Zymomonas mobilis
NADP+ S64D mutation converts the strict NADP+ specificity of wild-type GFOR to a dual NADP+/NAD+ specificity Zymomonas mobilis