Using 1H-and 15N-NMR spectroscopy to observe active sites of porcine cytosolic and Escherichia coli aspartate aminotransferases-Reference-Cited by-同舟云学术

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

Published:1994 Issue: Volume: Page:55-59
ISSN:
Container-title:Biochemistry of Vitamin B6 and PQQ
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Author:

Metzler D. E.,Metzler C. M.,Mollova E. T.,Scott R. D.,Kintanar A.,Tanase S.,Kogo K.,Higaki T.,Morino Y.,Kagamiyama H.,Yano T.,Kuramitsu S.,Hayashi H.,Hirotsu K.,Miyahara I.

Publisher

Birkhäuser Basel

Link

http://link.springer.com/content/pdf/10.1007/978-3-0348-7393-2_9.pdf

Reference3 articles.

1. Kintanar, A., Metzler, C. M., Metzler, D. E., and Scott, R. D. (1991) NMR Observations of Exchangeable Protons of Pyridoxal Phosphate and Histidine Residues in Cytosolic Aspartate Aminotransferase. J. Biol. Chem. 266, 17222–17229.

2. Metzler, D.E., Metzler, C.M., Mollova, E.T., Scott, R. D., Tanase, S., Kogo, K., Higaki, T. and Morino, Y. (1994) NMR Studies of 1H Resonances in the 10–18 ppm Range for Cytosolic Aspartate Aminotransferase. J. Biol. Chem. 269 In press.

3. Scott, RD, Jin, P., Miura, R., Chu, W.C., Kintanar, A.,Metzler, C. M.,Metzler, D. E. (1991) In: Fukui, T., Kagamiyama, H., Soda, K. and Wada, H. (eds): Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds as Cofactors“ Pergamon Press, Oxford, pp. 129–143.

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1. 1H and15N NMR Spectroscopy of Aspartate Aminotransferase and Related Schiff Bases and Tautomerism in Enzyme Active Sites;Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins;2000