Zobrazeno 1 - 10
of 73
pro vyhledávání: '"Eugene E. Dekker"'
Publikováno v:
Archives of Biochemistry and Biophysics. 358:211-221
l -Threonine dehydrogenase catalyzes the NAD + -dependent oxidation of threonine forming 2-amino-3-ketobutyrate. Chemical modification of Cys-38 of Escherichia coli threonine dehydrogenase, whose residue aligns with the catalytic zinc-binding residue
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86ea80016fbe4541c4de2c99b00b8ef1
https://doi.org/10.1006/abbi.1998.0845
https://doi.org/10.1006/abbi.1998.0845
Publikováno v:
Inorganica Chimica Acta. :215-221
Escherichia coliL-threonine dehydrogenase (TDH) is a homotetrameric protein which contains one Zn2+ ion per subunit and is a member of the medium chain, Zn2+-containing alcohol/polyol dehydrogenase family. TDH was subjected to extended X-ray absorpti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3dbf50c33f9ee45105ab8a21db82d788
https://doi.org/10.1016/s0020-1693(97)06107-0
https://doi.org/10.1016/s0020-1693(97)06107-0
Autor:
Adam R. Johnson, Eugene E. Dekker
Publikováno v:
Protein Science. 5:382-390
L-Threonine dehydrogenase (TDH) from Escherichia coli is rapidly inactivated and develops a new absorbance peak at 347 nm when incubated with N-ethyl-5-phenylisoxazolium-3'-sulfonate (Woodward's reagent K, WRK). The cofactors, NAD+ or NADH (1.5 mM),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9151e0435608798e600a96b87120232f
https://doi.org/10.1002/pro.5560050223
https://doi.org/10.1002/pro.5560050223
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1253:208-214
The oxidation of L-threonine to 2-amino-ketobutyrate, as catalyzed by L-threonine dehydrogenase, is the first step in the major pathway for threonine catabolism in both eukaryotes and prokaryotes. Threonine dehydrogenase of E. coli has considerable a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95eaf2e62345c5aade212e48919dbed5
https://doi.org/10.1016/0167-4838(95)00162-2
https://doi.org/10.1016/0167-4838(95)00162-2
Autor:
John P. Marcus, Eugene E. Dekker
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1164:299-304
2-Amino-3-ketobutyrate ligase catalyzes the reversible, pyridoxal 5′-phosphate-dependent condensation of glycine with acetyl CoA forming the unstable intermediate, 2-amino-3-ketobutyrate. Several independent lines of evidence indicate that the pure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a4afcedd8e8c18fd83d7dd56b37f9a4
https://doi.org/10.1016/0167-4838(93)90262-p
https://doi.org/10.1016/0167-4838(93)90262-p
Autor:
John P. Marcus, Eugene E. Dekker
Publikováno v:
Biochemical and Biophysical Research Communications. 190:1066-1072
2-Amino-3-ketobutyrate can be readily formed enzymatically by the action of L-threonine dehydrogenase. A convenient assay for determining the half-life of this beta-keto acid is afforded by its rapid and quantitative conversion to glycine (+ acetyl C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9f8a58857151ec155303e50d1f02958
https://doi.org/10.1006/bbrc.1993.1157
https://doi.org/10.1006/bbrc.1993.1157
Autor:
Eugene E. Dekker, R P Kitson
Publikováno v:
Journal of Biological Chemistry. 267:10507-10514
2-Keto-4-hydroxyglutarate aldolase, which catalyzes the reversible cleavage of 2-keto-4-hydroxyglutarate, yielding pyruvate plus glyoxylate, has been purified from extracts of bovine kidney to apparent homogeneity as judged by polyacrylamide gel elec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b0dd56aadbb61d34332e2410a810c785
https://doi.org/10.1016/s0021-9258(19)50046-1
https://doi.org/10.1016/s0021-9258(19)50046-1
Publikováno v:
Ciba Foundation Symposium - Biosynthesis of Terpenes and Sterols
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f25d5f43559f423a2f7d1e37f4dc7f1
https://doi.org/10.1002/9780470719121.ch5
https://doi.org/10.1002/9780470719121.ch5
Autor:
Eugene E. Dekker, B R Epperly
Publikováno v:
Journal of Biological Chemistry. 266:6086-6092
Pure L-threonine dehydrogenase from Escherichia coli is a tetrameric protein (Mr = 148,000) with 6 half-cystine residues/subunit; its catalytic activity as isolated is stimulated 5-10-fold by added Mn2+ or Cd2+. The peptide containing the 1 cysteine/
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fac504a53ba506b56de28e84cb690be2
https://doi.org/10.1016/s0021-9258(18)38087-6
https://doi.org/10.1016/s0021-9258(18)38087-6
Autor:
Harry C. Winter, Eugene E. Dekker
Publikováno v:
Plant Physiology. 95:206-212
4-Methyleneglutamine amidohydrolase has been extracted and purified over 1000-fold from 14-day-old peanut (Arachis hypogaea) leaves by modification of methods described previously. The purified enzyme shows two bands of activity and three to four ban
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb6482d34dcdd33b187afc6559116f87
https://doi.org/10.1104/pp.95.1.206
https://doi.org/10.1104/pp.95.1.206