Using 1H-and 15N-NMR spectroscopy to observe active sites of porcine cytosolic and Escherichia coli aspartate aminotransferases

Autor:	David E. Metzler, Tsuyoshi Higaki, Carol M. Metzler, Hiroyuki Kagamiyama, Ken Hirotsu, K. Kogo, Takato Yano, Agustin Kintanar, Hideyuki Hayashi, Robert D. Scott, E T Mollova, Sumio Tanase, Yoshimasa Morino, Seiki Kuramitsu, Ikuko Miyahara
Rok vydání:	1994
Předmět:	1h nmr spectroscopy biology Mutant Active site Nuclear magnetic resonance spectroscopy Aspartate Aminotransferases medicine.disease_cause Cytosol chemistry.chemical_compound chemistry Biochemistry biology.protein medicine Pyridoxal phosphate Escherichia coli
Zdroj:	Biochemistry of Vitamin B6 and PQQ ISBN: 9783034873956
DOI:	10.1007/978-3-0348-7393-2_9
Popis:	Studies of aspartate aminotransferases (AspAT) under a variety of conditions by 1H NMR spectroscopy have allowed assignment of some downfield resonances. We report new results using specific active site mutants of porcine cytosolic and E. coli AspATs as well as HMQC — NMR spectroscopy on15N-containing E. coli AspAT.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::7d10b20c6fea8cb2f6fa7a68e863571f https://doi.org/10.1007/978-3-0348-7393-2_9 Zobrazit plný text záznamu