Characterization of human cystathionine γ-lyase enzyme activities toward d-amino acids

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd0607c3340f6591e7a79f4ba86c33e3
https://pubmed.ncbi.nlm.nih.gov/36085174

d-Serine and d-Alanine Regulate Adaptive Foraging Behavior in Caenorhabditis elegans via the NMDA Receptor

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::808e480f2c57f349d56e37ccf1b94202
https://doi.org/10.1523/jneurosci.2358-19.2020

Identification of a novel d-amino acid aminotransferase involved in d-glutamate biosynthetic pathways in the hyperthermophile Thermotoga maritima

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01663841b0600eeb7763e72286f733ab
https://pubmed.ncbi.nlm.nih.gov/35377552

Identification and biochemical characterization of threonine dehydratase from the hyperthermophile Thermotoga maritima

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8198eb8f495d2ff5a00bc9607e85a4a4
https://pubmed.ncbi.nlm.nih.gov/33938999

Prenatal expression of d‑aspartate oxidase causes early cerebral d‑aspartate depletion and influences brain morphology and cognitive functions at adulthood

Autor: Tommaso Nuzzo, Hiroshi Homma, Arianna De Rosa, Francesco Errico, Geppino Falco, Viviana Caputo, Masumi Katane, Alessandro Usiello, Yasuaki Saitoh, Francesca Mastrostefano, Andrea M. Isidori, Maria Egle De Stefano, Anna Di Maio, Pina Marotta

Publikováno v: Amino acids (Wien, Print) 52 (2020): 597–617. doi:10.1007/s00726-020-02839-y
info:cnr-pdr/source/autori:De Rosa A.; Mastrostefano F.; Di Maio A.; Nuzzo T.; Saitoh Y.; Katane M.; Isidori A.M.; Caputo V.; Marotta P.; Falco G.; De Stefano M.E.; Homma H.; Usiello A.; Errico F./titolo:Prenatal expression of d-aspartate oxidase causes early cerebral d-aspartate depletion and influences brain morphology and cognitive functions at adulthood/doi:10.1007%2Fs00726-020-02839-y/rivista:Amino acids (Wien, Print)/anno:2020/pagina_da:597/pagina_a:617/intervallo_pagine:597–617/volume:52

The free d-amino acid, d-aspartate, is abundant in the embryonic brain but significantly decreases after birth. Besides its intracellular occurrence, d-aspartate is also present at extracellular level and acts as an endogenous agonist for NMDA and mG

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6785722a37849813b6e305458a422ab4
http://hdl.handle.net/11573/1396063