TMG-chitotriomycin as a probe for the prediction of substrate specificity of β-N-acetylhexosaminidases

Hiroto Shiota; Hiroshi Kanzaki; Tadashi Hatanaka; Teruhiko Nitoda

doi:10.1016/j.carres.2013.04.024

TMG-chitotriomycin as a probe for the prediction of substrate specificity of β-N-acetylhexosaminidases

Hiroto Shiota, Hiroshi Kanzaki, Tadashi Hatanaka, Teruhiko Nitoda

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

Abstract

TMG-chitotriomycin (1) produced by the actinomycete Streptomyces annulatus NBRC13369 was examined as a probe for the prediction of substrate specificity of β-N-acetylhexosaminidases (HexNAcases). According to the results of inhibition assays, 14 GH20 HexNAcases from various organisms were divided into 1-sensitive and 1-insensitive enzymes. Three representatives of each group were investigated for their substrate specificity. The 1-sensitive HexNAcases hydrolyzed N-acetylchitooligosaccharides but not N-glycan-type oligosaccharides, whereas the 1-insensitive enzymes hydrolyzed N-glycan-type oligosaccharides but not N-acetylchitooligosaccharides, indicating that TMG-chitotriomycin can be used as a molecular probe to distinguish between chitin-degrading HexNAcases and glycoconjugate-processing HexNAcases.

Original language	English
Pages (from-to)	29-34
Number of pages	6
Journal	Carbohydrate Research
Volume	375
DOIs	https://doi.org/10.1016/j.carres.2013.04.024
Publication status	Published - 2013

Keywords

GH20 family
Inhibitor
Physiological function
Substrate specificity
TMG-chitotriomycin
β-N-Acetylhexosaminidase

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry
Organic Chemistry

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10.1016/j.carres.2013.04.024

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@article{e050518a267e4da0b1ea22c9b35f714b,

title = "TMG-chitotriomycin as a probe for the prediction of substrate specificity of β-N-acetylhexosaminidases",

abstract = "TMG-chitotriomycin (1) produced by the actinomycete Streptomyces annulatus NBRC13369 was examined as a probe for the prediction of substrate specificity of β-N-acetylhexosaminidases (HexNAcases). According to the results of inhibition assays, 14 GH20 HexNAcases from various organisms were divided into 1-sensitive and 1-insensitive enzymes. Three representatives of each group were investigated for their substrate specificity. The 1-sensitive HexNAcases hydrolyzed N-acetylchitooligosaccharides but not N-glycan-type oligosaccharides, whereas the 1-insensitive enzymes hydrolyzed N-glycan-type oligosaccharides but not N-acetylchitooligosaccharides, indicating that TMG-chitotriomycin can be used as a molecular probe to distinguish between chitin-degrading HexNAcases and glycoconjugate-processing HexNAcases.",

keywords = "GH20 family, Inhibitor, Physiological function, Substrate specificity, TMG-chitotriomycin, β-N-Acetylhexosaminidase",

author = "Hiroto Shiota and Hiroshi Kanzaki and Tadashi Hatanaka and Teruhiko Nitoda",

note = "Funding Information: The authors would like to thank Sysmex Corporation (Kobe, Japan) for generous gifts of BmGlcNAcase and BmFDL. The authors would like to thank Dr. Kazuhito Fujiyama (Osaka University) for helpful advice. This work was supported by MEXT/JSPS KAKENHI {\textquoteleft}Grant-in-Aid for Scientific Research (C), 21580128{\textquoteright} to T.N.",

year = "2013",

doi = "10.1016/j.carres.2013.04.024",

language = "English",

volume = "375",

pages = "29--34",

journal = "Carbohydrate Research",

issn = "0008-6215",

publisher = "Elsevier BV",

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T1 - TMG-chitotriomycin as a probe for the prediction of substrate specificity of β-N-acetylhexosaminidases

AU - Shiota, Hiroto

AU - Kanzaki, Hiroshi

AU - Hatanaka, Tadashi

AU - Nitoda, Teruhiko

N1 - Funding Information: The authors would like to thank Sysmex Corporation (Kobe, Japan) for generous gifts of BmGlcNAcase and BmFDL. The authors would like to thank Dr. Kazuhito Fujiyama (Osaka University) for helpful advice. This work was supported by MEXT/JSPS KAKENHI ‘Grant-in-Aid for Scientific Research (C), 21580128’ to T.N.

PY - 2013

Y1 - 2013

N2 - TMG-chitotriomycin (1) produced by the actinomycete Streptomyces annulatus NBRC13369 was examined as a probe for the prediction of substrate specificity of β-N-acetylhexosaminidases (HexNAcases). According to the results of inhibition assays, 14 GH20 HexNAcases from various organisms were divided into 1-sensitive and 1-insensitive enzymes. Three representatives of each group were investigated for their substrate specificity. The 1-sensitive HexNAcases hydrolyzed N-acetylchitooligosaccharides but not N-glycan-type oligosaccharides, whereas the 1-insensitive enzymes hydrolyzed N-glycan-type oligosaccharides but not N-acetylchitooligosaccharides, indicating that TMG-chitotriomycin can be used as a molecular probe to distinguish between chitin-degrading HexNAcases and glycoconjugate-processing HexNAcases.

AB - TMG-chitotriomycin (1) produced by the actinomycete Streptomyces annulatus NBRC13369 was examined as a probe for the prediction of substrate specificity of β-N-acetylhexosaminidases (HexNAcases). According to the results of inhibition assays, 14 GH20 HexNAcases from various organisms were divided into 1-sensitive and 1-insensitive enzymes. Three representatives of each group were investigated for their substrate specificity. The 1-sensitive HexNAcases hydrolyzed N-acetylchitooligosaccharides but not N-glycan-type oligosaccharides, whereas the 1-insensitive enzymes hydrolyzed N-glycan-type oligosaccharides but not N-acetylchitooligosaccharides, indicating that TMG-chitotriomycin can be used as a molecular probe to distinguish between chitin-degrading HexNAcases and glycoconjugate-processing HexNAcases.

KW - GH20 family

KW - Inhibitor

KW - Physiological function

KW - Substrate specificity

KW - TMG-chitotriomycin

KW - β-N-Acetylhexosaminidase

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ER -

TMG-chitotriomycin as a probe for the prediction of substrate specificity of β-N-acetylhexosaminidases

Abstract

Keywords

ASJC Scopus subject areas

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