Crystallization and preliminary X-ray analysis of pyridoxal 4-dehydrogenase, the second enzyme in degradation pathway I of pyridoxine.
Pyridoxal 4-dehydrogenase (PLDH; EC 1.1.107) is the second enzyme in the bacterial degradation pathway I of vitamin B(6), which catalyzes the oxidation of pyridoxal to 4-pyridoxolactone using NAD(+). PLDH from Microbacterium luteolum, a dimeric protein with a subunit molecular weight of 38 kDa, was crystallized at 277 K in a drop solution comprising 15%(w/v) polyethylene glycol 4000, 0.15 M sodium acetate, 7.5 mM n-octyl-beta-D-glucoside and 0.075 M Tris-HCl pH 7.5 by the sitting-drop vapour-diffusion method. The crystals were monoclinic and belonged to space group C2, with unit-cell parameters a = 107.0, b = 56.7, c = 130.2 A, beta = 103.6 degrees . Diffraction data were collected from a single crystal to 2.0 A.
Yokochi
Nana
N
Department of Bioresources Science, Faculty of Agriculture, Kochi University, Nankoku, Kochi 783-8502, Japan.
Yoshikane
Yu
Y
Yagi
Toshiharu
T
Yamasaki
Masayuki
M
Mikami
Bunzo
B
D000192:Actinomycetales / Q000201:enzymology*; D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015394:Molecular Structure; D011736:Pyridoxine / Q000378:metabolism*
D000429:Alcohol Oxidoreductases; C042642:pyridoxal dehydrogenase; D011736:Pyridoxine