Zobrazeno 1 - 10
of 88
pro vyhledávání: '"Masae Sekine"'
Autor:
Masae Sekine, Kumiko Sakai-Kato, Yasuaki Saitoh, Masumi Katane, Hiroshi Homma, Tetsuya Miyamoto
Publikováno v:
FEBS Letters. 595:2931-2941
The hyperthermophilic bacterium Thermotoga maritima peptidoglycan contains unusual d-lysine alongside typical d-alanine and d-glutamate. We previously identified lysine racemase and threonine dehydratase, but knowledge of d-amino acid metabolism rema
Autor:
Tetsuya Miyamoto, Yasuaki Saitoh, Masumi Katane, Masae Sekine, Kumiko Sakai-Kato, Hiroshi Homma
Publikováno v:
Bioscience, biotechnology, and biochemistry. 86(11)
Various d-amino acids play important physiological roles in mammals, but the pathways of their production remain unknown except for d-serine, which is generated by serine racemase. Previously, we found that Escherichia coli cystathionine β-lyase pos
Publikováno v:
Biochemical Journal. 477:4221-4241
Recent investigations have shown that multiple d-amino acids are present in mammals and these compounds have distinctive physiological functions. Free d-glutamate is present in various mammalian tissues and cells and in particular, it is presumably c
Autor:
Hiroshi Homma, Masae Sekine, Kumiko Sakai-Kato, Tetsuya Miyamoto, Yasuaki Saitoh, Masumi Katane
Publikováno v:
The Journal of Neuroscience. 40:7531-7544
d-Serine (d-Ser) is a coagonist for NMDA-type glutamate receptors and is thus important for higher brain function. d-Ser is synthesized by serine racemase and degraded by d-amino acid oxidase. However, the significance of these enzymes and the releva
Publikováno v:
Amino Acids. 52:487-497
Bacteria produce various D-amino acids, including non-canonical D-amino acids, to adapt to environmental changes and overcome a variety of threats. These D-amino acids are largely utilized as components of peptidoglycan, and they promote peptidoglyca
Autor:
Tetsuya Miyamoto, Toshiyuki Moriya, Masumi Katane, Yasuaki Saitoh, Masae Sekine, Kumiko Sakai‐Kato, Tairo Oshima, Hiroshi Homma
Publikováno v:
The FEBS journalReferences. 289(19)
The hyperthermophilic bacterium Thermotoga maritima has an atypical peptidoglycan that contains d-lysine alongside the usual d-alanine and d-glutamate. We previously identified a lysine racemase involved in d-lysine biosynthesis, and this enzyme also
Publikováno v:
FEMS Microbiology Letters. 369
Noncanonical D-amino acids are involved in peptidoglycan and biofilm metabolism in bacteria. Previously, we identified amino acid racemases with broad substrate specificity, including YgeA from Escherichia coli, which strongly prefers homoserine as a
Autor:
Tetsuya Miyamoto, Hiroshi Homma, Kumiko Sakai-Kato, Masumi Katane, Yasuaki Saitoh, Masae Sekine
Publikováno v:
Amino acids. 53(6)
The peptidoglycan of the hyperthermophile Thermotoga maritima contains an unusual component, d-lysine (d-Lys), in addition to the typical d-alanine (d-Ala) and d-glutamate (d-Glu). In a previous study, we identified a Lys racemase that is presumably
Autor:
Masae Sekine, Massimo Pasqualetti, Daniela Punzo, Alberto Galbusera, Masumi Katane, Francesco Errico, Hiroshi Homma, Tommaso Nuzzo, Mattia Miroballo, Alessandro Gozzi, Jean-Pierre Mothet, Alessandro Usiello, Yasuaki Saitoh
Publikováno v:
Biochimica et Biophysica Acta Proteins and Proteomics
Biochimica et Biophysica Acta Proteins and Proteomics, 2020, 1868, ⟨10.1016/j.bbapap.2020.140531⟩
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2020, 1868, ⟨10.1016/j.bbapap.2020.140531⟩
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics
Biochimica et Biophysica Acta Proteins and Proteomics, 2020, 1868, ⟨10.1016/j.bbapap.2020.140531⟩
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2020, 1868, ⟨10.1016/j.bbapap.2020.140531⟩
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics
Background Autism spectrum disorders (ASD) comprise a heterogeneous group of neurodevelopmental conditions characterized by impairment in social interaction, deviance in communication, and repetitive behaviors. Dysfunctional ionotropic NMDA and AMPA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6427ec94099d3eab034bbfb2314c4e49
http://hdl.handle.net/11588/832261
http://hdl.handle.net/11588/832261
Autor:
Masumi Katane, Sachi Koiwai, Makoto Ariyoshi, Yasuaki Saitoh, Kazuki Nakayama, Satoaki Matoba, Kenji Hamase, Hiroshi Homma, Shuhei Tateishi, Tetsuya Miyamoto, Kenichiro Nagai, Masashi Mita, Kaoruko Takaku, Masae Sekine
Publikováno v:
Archives of Biochemistry and Biophysics. 654:10-18
d-Glutamate cyclase (DGLUCY) is a unique enzyme that reversibly converts free d-glutamate to 5-oxo-d-proline and H2O. Mammalian DGLUCY is highly expressed in the mitochondrial matrix in the heart, and its downregulation disrupts d-glutamate and/or 5-