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- W4252805890 abstract "A β-N-acetylglucosaminidase gene (nag84A) was cloned from Clostridium paraputrificum M-21 in Escherichia coli. The nag84A gene consists of an open reading frame of 4647 by encoding I549 amino acids, with a deduced molecular weight of 174,311, which have a catalytic domain belonging to family 84 of the glycoside hydrolases. Nag84A was purified from a recombinant E. coli and characterized. Although Nag84A exhibited high homology to the hyaluronidase from Clostridium perfringens, it did not degrade hyluronic acid. The enzyme hydrolyzed chitooligomers such as di-, tri-, tetra-, penta- and hexa-N-cetylchitobexaose, and synthetic substrates such as 4-methylumbelliferyl N-acetyl β-d-glucosaminide [4-MU-(G1cNAc)], but did not hydrolyze 4-MU-β-d-glucoside, 4-MU-α-d-glycoside, 4-MU-α-d-GlcNAc, 4-MU-α-d-galactoside, 4-MU-β-d-xyloside, PNP-β-d-galactoside, and PNP-α-d-xyloside. The enzyme was optimally active at 50°C and pH 6.5, and the apparent Km and Vmax values for 4-MU-(G1cNAc) were 8.5 μM and 1.39 μmol/min/mg of protein, respectively. SDS-PAGE, zymogram, and immunological analyses suggested that Nag84A was inducible by ball-milled chitin. Since Nag84A has a high molecular weight with a family 84 catalytic domain with high homology to hyaluronidases but no hyaluronidase activity, the enzyme is a novel β-N-acetylglucosaminidase different from others reported having low molecular weights and belonging to family 3 and family I8." @default.
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- W4252805890 date "2003-01-01" @default.
- W4252805890 modified "2023-10-18" @default.
- W4252805890 title "A New Type of .BETA.-N-Acetylglucosaminidase from Hydrogen-Producing Clostridium paraputrficum M-21" @default.
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- W4252805890 doi "https://doi.org/10.1263/jbb.96.268" @default.
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