Zobrazeno 1 - 10 of 37 pro vyhledávání: '"D E Metzler"'
1
Is pyridoxal 5′-phosphate an affinity label for phosphate-binding sites in proteins?: The case of bovine glutamate dehydrogenase
Autor: Paul C. Engel, D E Metzler, Z Valinger
Publikováno v: Biochemical Journal. 294:835-839
The effects of pyridoxal 5′-phosphate (PalP) on ox liver glutamate dehydrogenase (94% inactivation by 1.8 mM reagent at pH 7 and 25 degrees C) have been compared with those of three analogues, 5′-deoxypyridoxal (96% inactivation), pyridoxal 5′-
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6e23a34fad3e83ac992c59f2e3bbd28
https://doi.org/10.1042/bj2940835
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4
Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate
Autor: S, Rhee, M M, Silva, C C, Hyde, P H, Rogers, C M, Metzler, D E, Metzler, A, Arnone
Publikováno v: The Journal of biological chemistry. 272(28)
Two high resolution crystal structures of cytosolic aspartate aminotransferase from pig heart provide additional insights into the stereochemical mechanism for ligand-induced conformational changes in this enzyme. Structures of the homodimeric native
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dc2dddcab3ee96845fd68df66050ad25
https://pubmed.ncbi.nlm.nih.gov/9211866
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6
NMR studies of 1H resonances in the 10-18-ppm range for cytosolic aspartate aminotransferase
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
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7
NMR studies of 1H resonances in the 10-18-ppm range for aspartate aminotransferase from Escherichia coli
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
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8
NMR observation of exchangeable protons of pyridoxal phosphate and histidine residues in cytosolic aspartate aminotransferase
Autor: A, Kintanar, C M, Metzler, D E, Metzler, R D, Scott
Publikováno v: The Journal of biological chemistry. 266(26)
Observation of the 93-kDa cytosolic aspartate aminotransferase by 500-MHz 1H NMR spectroscopy in H2O has revealed a series of resonances in the 10-18 ppm range arising from exchangeable protons. One of these (peak A) has been assigned to the proton b
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d1f998c548ee9c588232078fba77f89c
https://pubmed.ncbi.nlm.nih.gov/1654326
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9
Equilibria and absorption spectra of tryptophanase
Autor: C M, Metzler, R, Viswanath, D E, Metzler
Publikováno v: The Journal of biological chemistry. 266(15)
Tryptophanase (tryptophan: indole-lyase) from Escherichia coli has been isolated in the holoenzyme form and its absorption spectra and acid-base chemistry have been reevaluated. Apoenzyme has been prepared by dialysis against sodium phosphate and L-a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2927a2d3d5cf18c2b7c3427a0b9f88de
https://pubmed.ncbi.nlm.nih.gov/2033039
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