Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

EC Number Crystallization (Comment) Organism
1.1.99.28 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

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.99.28 periplasm
-
 Zymomonas mobilis
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.28 Zymomonas mobilis Q07982
-
-

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.1.99.28 GFOR
-
 Zymomonas mobilis
1.1.99.28 glucose-fructose oxidoreductase
-
 Zymomonas mobilis

Cofactor

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