2016 Fiscal Year Final Research Report
Studies on the energetically efficient metabolic pathway of N-glycans in intestinal bacteria
Project/Area Number |
26440022
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Structural biochemistry
|
Research Institution | Niigata University |
Principal Investigator |
|
Research Collaborator |
NAKAI Hiroyuki
|
Project Period (FY) |
2014-04-01 – 2017-03-31
|
Keywords | N-グリカン / 酵素 / 代謝 |
Outline of Final Research Achievements |
The kinetic and structural analyses of β-1,4-mannosyl-N-acetyl-glucosamine phosphorylase which is a key enzyme in novel metabolic pathway for N-glycan where phosphorylase participates, were carried out to elucidate this metabolic pathway in intestinal bacteria. The enzymes from some microbes have strict regioselectivity and acceptor specificity against N-acetyl-glucasamine and N,N’-diacetyl-chitobiose as acceptors in reverse phosphorolysis. The three-dimensional structure of β-1,4-mannosyl-N-acetyl-glucosamine phosphorylase from Bacteroides thetaiotaomicron has not yet been determined. This structure analysis is carried out continuously now. To investigate of an uncharacterized gene which is predicted to participate in N-glycan metabolism existing close to phosphorylase gene, the hydrolytic reaction of the protein encoded by this gene was examined using various N-glycans as the substrate candidates. However, this protein did not show hydrolytic reaction.
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Free Research Field |
酵素化学
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