Purification and characterization of recombinant Mortierella vinacea alpha-galactosidases I and II expressed in Saccharomyces cerevisiae.
The cDNAs coding for Mortierella vinacea alpha-galactosidases I and II were expressed in Saccharomyces cerevisiae under the control of the yeast GAL10 promoter. The recombinant enzymes purified to homogeneity from the culture filtrate were glycosylated, and had properties identical to those of the native enzymes except for improving the heat stability of alpha-galactosidase II and decreasing the specific activities of both enzymes.
Shibuya
H
H
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Kobayashi
H
H
Yoshida
S
S
Kaneko
S
S
Park
G G
GG
Kusakabe
I
I
D001426:Bacterial Proteins; D018076:DNA, Complementary / Q000096:biosynthesis / Q000235:genetics; D006031:Glycosylation; D007527:Isoenzymes / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification; D020094:Mortierella / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D013696:Temperature; D000519:alpha-Galactosidase / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification
D001426:Bacterial Proteins; D018076:DNA, Complementary; D007527:Isoenzymes; D011994:Recombinant Proteins; C115462:alpha-galactosidase I; C121320:alpha-galactosidase II; D000519:alpha-Galactosidase