Zobrazeno 1 - 7
of 7
pro vyhledávání: '"E T, Mollova"'
Autor:
Ikuko Miyahara, David E. Metzler, Agustin Kintanar, Hideyuki Hayashi, Hiroyuki Kagamiyama, Ken Hirotsu, E T Mollova
Publikováno v:
Biochemistry. 36:615-625
Aspartate aminotransferase from Escherichia coli, an 88 kDa enzyme, was uniformly and selectively enriched with 15N and was studied by heteronuclear multiple-quantum coherence NMR spectroscopy in H2O. Good resolution was obtained for the downfield re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b2013f2420fd984a92a88cdcf4d3797
https://doi.org/10.1021/bi9615811
https://doi.org/10.1021/bi9615811
Autor:
Y Morino, E T Mollova, Carol M. Metzler, David E. Metzler, S Tanase, T Higaki, K Kogo, Robert D. Scott
Publikováno v:
Journal of Biological Chemistry. 269:28017-28026
Continuing a previous investigation (Kintanar, A., Metzler, C. M., Metzler, D. E., and Scott, R. D. (1991) J. Biol. Chem. 266, 17222-17229), we have recorded 1H NMR spectra at 500 MHz in the 10-18-ppm range for the 93-kDa porcine cytosolic aspartate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fb8478da01237b1cf1bb027ebf279ece
https://doi.org/10.1016/s0021-9258(18)46889-5
https://doi.org/10.1016/s0021-9258(18)46889-5
Autor:
Hideyuki Hayashi, Robert D. Scott, Carol M. Metzler, Seiki Kuramitsu, Ken Hirotsu, E T Mollova, T. Yano, I. Miyahara, David E. Metzler, Hiroyuki Kagamiyama
Publikováno v:
Journal of Biological Chemistry. 269:28027-28033
We have recorded 500-MHz 1H NMR spectra in the 10-18-ppm range for aspartate aminotransferase from Escherichia coli and for three specific mutant forms. Histidine 143 has been replaced by either alanine or asparagine. In the third mutant, tryptophan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::95e2d0d09cfb12eb1136008c99efb61c
https://doi.org/10.1016/s0021-9258(18)46890-1
https://doi.org/10.1016/s0021-9258(18)46890-1
Publikováno v:
Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins ISBN: 9783034895491
Downfield resonances from hydrogen bonded protons are delicate sensors of changes in charge distribution in active sites. They indicate that a tight electrostatic interaction of the phenolate oxygen with the charged amino group of substrate, coenzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9ed27606e674dda439358ff7a16ba5df
https://doi.org/10.1007/978-3-0348-8397-9_30
https://doi.org/10.1007/978-3-0348-8397-9_30
Autor:
D E, Metzler, C M, Metzler, E T, Mollova, R D, Scott, S, Tanase, K, Kogo, T, Higaki, Y, Morino
Publikováno v:
The Journal of biological chemistry. 269(45)
Continuing a previous investigation (Kintanar, A., Metzler, C. M., Metzler, D. E., and Scott, R. D. (1991) J. Biol. Chem. 266, 17222-17229), we have recorded 1H NMR spectra at 500 MHz in the 10-18-ppm range for the 93-kDa porcine cytosolic aspartate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6a2b73d31d383564199b010c813d24f3
https://pubmed.ncbi.nlm.nih.gov/7961736
https://pubmed.ncbi.nlm.nih.gov/7961736
Autor:
D E, Metzler, C M, Metzler, R D, Scott, E T, Mollova, H, Kagamiyama, T, Yano, S, Kuramitsu, H, Hayashi, K, Hirotsu, I, Miyahara
Publikováno v:
The Journal of biological chemistry. 269(45)
We have recorded 500-MHz 1H NMR spectra in the 10-18-ppm range for aspartate aminotransferase from Escherichia coli and for three specific mutant forms. Histidine 143 has been replaced by either alanine or asparagine. In the third mutant, tryptophan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::362a241e36b1137651b9680bf3e89f4a
https://pubmed.ncbi.nlm.nih.gov/7961737
https://pubmed.ncbi.nlm.nih.gov/7961737
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
Publikováno v:
Biochemistry of Vitamin B6 and PQQ ISBN: 9783034873956
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7d10b20c6fea8cb2f6fa7a68e863571f
https://doi.org/10.1007/978-3-0348-7393-2_9
https://doi.org/10.1007/978-3-0348-7393-2_9