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Crystallization and preliminary x‐ray analysis of glucose‐fructose oxidoreductase from zymomonas mobilis
Author(s) -
Loos Heidi,
Ermler Ulrich,
Sprenger Georg A.,
Sahm Hermann
Publication year - 1994
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560031228
Subject(s) - zymomonas mobilis , oxidoreductase , chemistry , cofactor , periplasmic space , fructose , dehydrogenase , crystallography , nad+ kinase , methanol dehydrogenase , enzyme , biochemistry , escherichia coli , ethanol , ethanol fuel , gene
Abstract Glucose‐fructose oxidoreductase (E.C. 1.1.99.‐) from the ethanol‐producing Gram‐negative bacterium Zymomonas mobilis is a periplasmic, soluble enzyme that forms a homotet‐ramer of 160 kDa with one NADP(H) cofactor per subunit that is tightly, but noncovalently, bound. The enzyme was crystallized by the hanging drop vapor diffusion method using sodium citrate as precipitant. The obtained crystals belong to the space group P2 1 2 1 2, with unit cell constants of 84.6 Å, 94.1 Å, and 117.0 Å, consistent with two monomers in the asymmetric unit. They diffract to a resolution of about 2 Å and are suitable for X‐ray structure determination.