Nucleotide Sequence of<i>α</i>-Galactosidase cDNA from<i>Mortierella vinacea</i>

Shibuya, Haruo; Kobayashi, Hideyuki; Kasamo, Kunihiro; Kusakabe, Isao

doi:10.1271/bbb.59.1345

Cited by 22 publications

(10 citation statements)

References 4 publications

(4 reference statements)

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“…Although the optimum pH and temperature of P. purpurogenum enzyme were similar to those of M. vinacea enzyme, the pH stability of each enzyme was quite different. P. purpurogenum enzyme was stable at acidic pHs, while M. vinacea enzyme was stable at neutral and 3 -a-D-galactosylmannotetraose) were prepared from the hydrolyzate of copra galactomannan as described previously.2) Figure 3 shows the courses of hydrolysis of GaPMan 3 and GaPMan 4 by a-galactosidases of M. vinacea and P. purpurogenum. a-Galactosidase of M. vinacea could hydrolyze GaPMan 3 but not GaPMan 4 , while that of P. purpurogenum acted on Gal 3 Man 4 but not on GaPMan 3 .…”

Section: -mentioning

confidence: 98%

Purification and Some Properties ofα-Galactosidase fromPenicillium purpurogenum

Shibuya

Kobayashi

Park

et al. 1995

Bioscience, Biotechnology, and Biochemistry

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Section: -mentioning

confidence: 98%

Purification and Some Properties ofα-Galactosidase fromPenicillium purpurogenum

Shibuya

Kobayashi

Park

et al. 1995

Bioscience, Biotechnology, and Biochemistry

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“…S79440), 25) but in the course of refinement, there was some inconsistency between the electron density of the model and the amino acid sequence. Amino acids for the model were assumed according to the electron density, and 60 amino acids were finally modeled to be different from the deduced amino acid sequence.…”

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confidence: 99%

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

Fujimoto

Kaneko

Kim

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…The M. vinacea ␣-Gal II (28) acts on both substrates to almost equal extents. These facts indicate that eukaryotic ␣-Gals were classified into three groups based on the substrate specificity of these galactomanno-oligosaccharides.Genes encoding ␣-Gals have been cloned from various sources, including humans (3), plants (20, 33), yeasts (12), filamentous fungi (4,19,26,28), and bacteria (1, 2, 13, 17, 18). ␣-Gals from eukaryotes show a significant degree of similarity and are grouped into family 27.…”

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confidence: 99%

Purification and Characterization of the RecombinantThermussp. Strain T2 α-Galactosidase Expressed inEscherichia coli

Ishiguro

Kaneko

Kuno

et al. 2001

Appl Environ Microbiol

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The nucleotide sequence of the Thermus sp. strain T2 DNA coding for a thermostable ␣-galactosidase was determined. The deduced amino acid sequence of the enzyme predicts a polypeptide of 474 amino acids (M r , 53,514). The observed homology between the deduced amino acid sequences of the enzyme and ␣-galactosidase from Thermus brockianus was over 70%. Thermus sp. strain T2 ␣-galactosidase was expressed in its active form in Escherichia coli and purified. Native polyacrylamide gel electrophoresis and gel filtration chromatography data suggest that the enzyme is octameric. The enzyme was most active at 75°C for p-nitrophenyl-␣-Dgalactopyranoside hydrolysis, and it retained 50% of its initial activity after 1 h of incubation at 70°C. The enzyme was extremely stable over a broad range of pH (pH 6 to 13) after treatment at 40°C for 1 h. The enzyme acted on the terminal ␣-galactosyl residue, not on the side chain residue, of the galactomanno-oligosaccharides as well as those of yeasts and Mortierella vinacea ␣-galactosidase I. The enzyme has only one Cys residue in the molecule. para-Chloromercuribenzoic acid completely inhibited the enzyme but did not affect the mutant enzyme which contained Ala instead of Cys, indicating that this Cys residue is not responsible for its catalytic function.␣-Galactosidases (␣-Gals) are known to occur widely in microorganisms, plants, and animals, and some of them have been purified and characterized (5). ␣-Gals catalyze the hydrolysis of 1,6-linked ␣-galactose residues from oligosaccharides and polymeric galactomannans (19,27,28). In the sugar beet industry, ␣-Gals have been used to increase the sucrose yield by eliminating raffinose, which prevents the crystallization of beet sugar (31). Raffinose and stachyose in beans are known to cause flatulence. ␣-Gal has the potential to alleviate these symptoms, for instance, in the treatment of soybean milk (6).We have studied the substrate specificity of ␣-Gals from eukaryotes by using galactomanno-oligosaccharides, such as 6 3 -mono-␣-D-galactopyranosyl-␤-1,4-mannotriose (Gal 3 Man 3 ) and 63 -mono-␣-D-galactopyranosyl-␤-1,4-mannotetraose (Gal 3 Man 4 ). The structures of these galactomanno-oligosaccharides are shown in Fig. 1. Mortierella vinacea ␣-Gal I (11) and yeast ␣-Gals (32) are specific for Gal 3 Man 3, having an ␣-galactosyl residue (designated the terminal ␣-galactosyl residue) attached to the O-to-6 position of the nonreducing end mannose of ␤-1,4-mannotriose. On the other hand, Aspergillus niger 5-16 ␣-Gal (12) and Penicillium purpurogenum ␣-Gal (27) show a preference for Gal 3 Man 4 , having an ␣-galactosyl residue (designated as the side chain ␣-galactosyl residue) attached to the O-to-6 position of the third mannose from the reducing end of ␤-1,4-mannotetraose. The M. vinacea ␣-Gal II (28) acts on both substrates to almost equal extents. These facts indicate that eukaryotic ␣-Gals were classified into three groups based on the substrate specificity of these galactomanno-oligosaccharides.Genes encoding ␣-Gals have been cloned ...

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Nucleotide Sequence ofα-Galactosidase cDNA fromMortierella vinacea

Cited by 22 publications

References 4 publications

Purification and Some Properties ofα-Galactosidase fromPenicillium purpurogenum

Purification and Some Properties ofα-Galactosidase fromPenicillium purpurogenum

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

Purification and Characterization of the RecombinantThermussp. Strain T2 α-Galactosidase Expressed inEscherichia coli

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