Crystallization and preliminary X-ray crystallographic studies of α-galactosidase I fromMortierella vinacea

Abstract

alpha-Galactosidases catalyze the hydrolysis of a galactosyl residue from galactooligosaccharides and galactopolysaccharides. alpha-Galactosidase I from Mortierella vinacea was crystallized in two crystal forms using the hanging-drop vapour-diffusion method. Type 1 crystals belonged to space group I422, with unit-cell parameters a = b = 142.4, c = 131.5 A, and diffracted to beyond 2.1 A resolution, while type 2 crystals belonged to space group P4, with unit-cell parameters a = b = 100.9, c = 102.7 A, and diffracted to beyond 1.6 A resolution. This enzyme crystallized as a glycoprotein tetramer and the tetrameric structure was located around the crystallographic fourfold axis.

The Tetramer Structure of the Glycoside Hydrolase Family 27 α-Galactosidase I fromUmbelopsis vinacea

“…UvGalI was purified and crystallized as previously reported. 16) Crystallization trials of UvGalI yielded two different crystal forms, type 1 and type 2, and structure analyses succeeded for both crystal forms. Their overall structures were similar, and hence we describe the structure analysis here for the type-1 crystal.…”

Production of soya milk containing low flatulence‐causing oligosaccharides in a packed bed reactor using immobilised α‐galactosidase

“…Most studies on purification and characterisation of a-galactosidases indicate that the enzyme functions as a tetramer (Brumer et al, 1999;Fridjonsson et al, 1999;Baik et al, 2000;Fujimoto et al, 2003). However, Ishiguro et al (2001) purified a recombinant a-galactosidase and is shown to be a hexamer.…”

Crystallization and preliminary X-ray diffraction studies of two thermostable α-galactosidases from glycoside hydrolase family 36

“…-Galactosidases are found in families 4, 27, 36 and 57. Family 27 has been extensively studied and four crystallographic structures have been determined: chicken N-acetylgalactosaminidase (PDB code 1ktb; Garman et al, 2002), rice -galactosidase (PDB code 1uas; Fujimoto et al, 2003), the fungus Trichoderma reesei -galactosidase (PDB code 1szn; Golubev et al, 2004) and human -galactosidase (PDB code 1r46; Garman & Garboczi, 2004). All these structures display the same (/) 8 -barrel topology and similar active sites.…”