Cloning, sequencing, and expression of cDNA for human β-galactosidase

Oshima, Akihiro; Tsuji, Akihiko; Nagao, Yoshiro; Sakuraba, Hitoshi; Suzuki, Yoshiyuki

doi:10.1016/s0006-291x(88)80038-x

Cited by 117 publications

(50 citation statements)

References 24 publications

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“…Conserved glutamate residues that probably act as the proton donor and the nucleophile are indicated by asterisks. Accession numbers for these sequences are as follows: "P. abyssi," CAB50440; P. horikoshii, BAA29599; P. furiosus, AAL80487; family 35 ␤-galactosidases from human (NP_000395 [27]), mouse (AAA37292 [21]), tomato (P48980 [1]), apple (T17002 [29]), Aspergillus niger (P29853 [19]), Bacillus circulans (JC5618 [13]), Xanthomonas manihotis (P48982 [34]), and Arthrobacter sp. (P96567 [7]); and family 42 ␤-galactosidases from Bacillus stearothermophilus (AAA22262 [9]), Carnobacterium piscicola (AAF16519 [2]), Thermus sp.…”

Section: Discussionmentioning

confidence: 99%

Characterization of an Exo-β- d -Glucosaminidase Involved in a Novel Chitinolytic Pathway from the Hyperthermophilic Archaeon Thermococcus kodakaraensis KOD1

et al. 2003

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We previously clarified that the chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 produces diacetylchitobiose (GlcNAc 2 ) as an end product from chitin. Here we sought to identify enzymes in T. kodakaraensis that were involved in the further degradation of GlcNAc 2 . Through a search of the T. kodakaraensis genome, one candidate gene identified as a putative ␤-glycosyl hydrolase was found in the near vicinity of the chitinase gene. The primary structure of the candidate protein was homologous to the ␤-galactosidases in family 35 of glycosyl hydrolases at the N-terminal region, whereas the central region was homologous to ␤-galactosidases in family 42. The purified protein from recombinant Escherichia coli clearly showed an exo-␤-D-glucosaminidase (GlcNase) activity but not ␤-galactosidase activity. This GlcNase (GlmA Tk ), a homodimer of 90-kDa subunits, exhibited highest activity toward reduced chitobiose at pH 6.0 and 80°C and specifically cleaved the nonreducing terminal glycosidic bond of chitooligosaccharides. The GlcNase activity was also detected in T. kodakaraensis cells, and the expression of GlmA Tk was induced by GlcNAc 2 and chitin, strongly suggesting that GlmA Tk is involved in chitin catabolism in T. kodakaraensis. These results suggest that T. kodakaraensis, unlike other organisms, possesses a novel chitinolytic pathway where GlcNAc 2 from chitin is first deacetylated and successively hydrolyzed to glucosamine. This is the first report that reveals the primary structure of GlcNase not only from an archaeon but also from any organism.

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Section: Discussionmentioning

confidence: 99%

Characterization of an Exo-β- d -Glucosaminidase Involved in a Novel Chitinolytic Pathway from the Hyperthermophilic Archaeon Thermococcus kodakaraensis KOD1

et al. 2003

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“…Human ␤-Gal cDNA encodes 677 amino acid residues, which include an N-terminal 23-amino acid secretion signal (11,12) (Fig. 1A).…”

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confidence: 99%

Crystal Structure of Human β-Galactosidase

Ohto¹,

Usui²,

Ochi

et al. 2012

Journal of Biological Chemistry

107

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Background: Deficiencies in ␤-D-galactosidase cause lysosomal storage diseases. Results: This is the first report to describe the crystal structure of human ␤-Gal. Human ␤-Gal is composed of a TIM barrel domain and two ␤-domains. Conclusion: The mutations were classified as mutations directly affecting the ligand recognition, mutations inside the protein core, or mutations located in the protein surface. Significance: Structural insights into lysosomal storage diseases mutations can be demonstrated.

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“…The adult form of GM1 gangliosidosis shows mild, slowly progressing neurologic involvement like dysarthrias or gait disturbances and, except for vertebral dysplasias, little involvement of the skeleton (O'Brien, 1989). The beta-D-galactosidase cDNA (Oshima et al, 1988) and the gene (Morreau et al, 1991) have been cloned and a variety of mutations have been characterized. Defective alleles are heterogeneous and no single mutation with a particular high frequency has been found.…”

Section: Gm1 Gangliosidosesmentioning

confidence: 99%