Crystallization and preliminary X-ray analysis of a bifunctional catalase-phenol oxidase from Scytalidium thermophilum.
Catalase-phenol oxidase from Scytalidium thermophilum is a bifunctional enzyme: its major activity is the catalase-mediated decomposition of hydrogen peroxide, but it also catalyzes phenol oxidation. To understand the structural basis of this dual functionality, the enzyme, which has been shown to be a tetramer in solution, has been purified by anion-exchange and gel-filtration chromatography and has been crystallized using the hanging-drop vapour-diffusion technique. Streak-seeding was used to obtain larger crystals suitable for X-ray analysis. Diffraction data were collected to 2.8 A resolution at the Daresbury Synchrotron Radiation Source. The crystals belonged to space group P2(1) and contained one tetramer per asymmetric unit.
Sutay Kocabas
Didem
D
Chemical Engineering Department, Middle East Technical University, Ankara, Turkey. didemsutay@gmail.com
Pearson
Arwen R
AR
Phillips
Simon E V
SE
Bakir
Ufuk
U
Ogel
Zumrut B
ZB
McPherson
Michael J
MJ
Trinh
Chi H
CH
D001203:Ascomycota / Q000201:enzymology* / Q000235:genetics; D002374:Catalase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D014442:Monophenol Monooxygenase / Q000032:analysis* / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D002374:Catalase; D014442:Monophenol Monooxygenase