Purification, Characterization and Gene Analysis of<i>N</i>-Acetylglucosaminidase from<i>Enterobacter</i>sp. G-1

Matsuo, Yasuhiro; Kurita, Masako; Park, Jae Kweon; Tanaka, Katsunori; Nakagawa, Tsuyoshi; Kawamukai, Makoto; Matsuda, Hideyuki

doi:10.1271/bbb.63.1261

Cited by 25 publications

(21 citation statements)

References 22 publications

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“…In Serratia and other bacteria, Chb participates in the catabolism of chitin, in which extracellular chitinases release chitobiose and higher ␤-1,4-linked chitooligosacccharides that are then hydrolyzed by Chb to produce GlcNAc (32,37). E. coli and other species are able to use chitobiose as a sole carbon source; the genes involved in chitobiose phosphotransferase uptake and utilization are encoded in the chbBCARFG operon (33 (Table 1).…”

Section: Discussionmentioning

confidence: 99%

Loss of a Biofilm-Inhibiting Glycosyl Hydrolase during the Emergence of Yersinia pestis

Erickson¹,

Jarrett²,

Callison³

et al. 2008

J Bacteriol

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Section: Discussionmentioning

confidence: 99%

Loss of a Biofilm-Inhibiting Glycosyl Hydrolase during the Emergence of Yersinia pestis

Erickson¹,

Jarrett²,

Callison³

et al. 2008

J Bacteriol

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“…Some bacterial NAGs were extracellular enzymes and are presumed to work in a degradation of chitooligosaccharides produced from polymeric chitin by the action of endochitinase. 13,[24][25][26] On the other hand, NAGs have been reported to be located in periplasmic space or in cytoplasm in the case of marine bacteria. 22,23,27) This intracellular localization of enzymes appears to be advantageous for an efficient hydrolysis of chitin in sea water, since hydrolyzed products can easily be taken into cells.…”

Section: Discussionmentioning

confidence: 99%

Purification, Cloning, and Sequence Analysis of β-N-Acetylglucosaminidase from the Chitinolytic BacteriumAeromonas hydrophilaStrain SUWA-9

Lan

Ozawa

Nishiwaki

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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A chitinolytic bacterium was isolated from Lake Suwa and identified as Aeromonas hydrophila strain SUWA-9. The strain grew well on a synthetic medium containing colloidal chitin as sole carbon source. Chitindegrading activity was induced by colloidal chitin or Nacetylglucosamine (GlcNAc). Most of the activity, however, was not detected in culture fluid but was associated with cells. A -N-acetylglucosaminidase was purified after it was solubilized from cells by sonication. The purified enzyme hydrolyzed N-acetylchitooligomers from dimer to pentamer and produced GlcNAc as a final product. The enzyme also hydrolyzed synthetic substrates such as p-nitrophenyl (pNP)-N-acetyl--Dglucosaminide and pNP-N-acetyl--D-galactosaminide. A gene coding for the purified -N-acetylglucosaminidase was isolated. The ORF identified is 2,661 nucleotides long and encodes a precursor protein of 887 amino acids including a signal peptide of 22 amino acid residues. The amino acid sequence deduced showed a high similarity to those of bacterial -N-acetylhexosaminidases classified in family 20 of glycosyl hydrolases.

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“…HexB also contained an N-acetylhexosaminidase-like C-terminal domain related to the N-acetyl-␤-D-glucosaminidase from Enterobacter sp. strain G-1 (44% I, 55% S) (28) (Fig. 2).…”

Section: Resultsmentioning

confidence: 99%

Genomic Analysis and Initial Characterization of the Chitinolytic System of Microbulbifer degradans Strain 2-40

et al. 2003

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Purification, Characterization and Gene Analysis ofN-Acetylglucosaminidase fromEnterobactersp. G-1

Cited by 25 publications

References 22 publications

Loss of a Biofilm-Inhibiting Glycosyl Hydrolase during the Emergence of Yersinia pestis

Loss of a Biofilm-Inhibiting Glycosyl Hydrolase during the Emergence of Yersinia pestis

Purification, Cloning, and Sequence Analysis of β-N-Acetylglucosaminidase from the Chitinolytic BacteriumAeromonas hydrophilaStrain SUWA-9

Genomic Analysis and Initial Characterization of the Chitinolytic System of Microbulbifer degradans Strain 2-40

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