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Crystallization and preliminary X-ray analysis of pyridoxal 4-dehydrogenase, the second enzyme in degradation pathway I of pyridoxine.
- Source :
- Acta Crystallographica: Section D (Wiley-Blackwell); Nov2004, Vol. 60 Issue 11, p2061-2062, 2p
- Publication Year :
- 2004
-
Abstract
- Pyridoxal 4-dehydrogenase (PLDH; EC L1.107) is the second enzyme in the bacterial degradation pathway I of vitamin B<subscript>6</subscript>, which catalyzes the oxidation of pyridoxal to 4-pyridoxolactone using NAD<superscript>+</superscript>. 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-β-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, h = 56.7, c = 130.2 Å, β = 103.6°. Diffraction data were collected from a single crystal to 2.0 Å. [ABSTRACT FROM AUTHOR]
- Subjects :
- VITAMIN B6
DEHYDROGENASES
CRYSTALLOGRAPHY
PHYSICAL sciences
CRYSTALS
CRYSTALLIZATION
Subjects
Details
- Language :
- English
- ISSN :
- 09074449
- Volume :
- 60
- Issue :
- 11
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section D (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 14797092
- Full Text :
- https://doi.org/10.1107/S0907444904021754