Zobrazeno 1 - 10
of 224
pro vyhledávání: '"Mary Ellen Jones"'
Autor:
Keith Shostak, Mary Ellen Jones
Publikováno v:
Biochemistry. 31:12155-12161
Pyrimidine nucleotides were tested as substrates for pure yeast orotidylate decarboxylase in an attempt to gain insight into the nature of the catalytic mechanism of the enzyme. Substitutions of the 5-position in the pyrimidine ring of the orotidylat
Autor:
Mary Ellen Jones, J B Bell
Publikováno v:
Journal of Biological Chemistry. 266:12662-12667
Orotidine 5'-monophosphate decarboxylase (ODCase) has been overexpressed in yeast 15C cells transformed with a plasmid carrying the URA3 gene that encodes ODCase. Twenty g of cells having ODCase activity equal to 30 mg of pure enzyme per liter of cel
Publikováno v:
Biochemistry. 30:6216-6223
Orotidine-5'-monophosphate decarboxylase (ODCase) from Saccharomyces cerevisiae displays an observed 13C kinetic isotope effect of 1.0247 +/- 0.0008 at 25 degrees C, pH 6.8. The observed isotope effect is sensitive to changes in the reaction medium,
Autor:
W C Small, Mary Ellen Jones
Publikováno v:
Journal of Biological Chemistry. 265:18668-18672
The oxidation of proline to glutamate in mitochondria requires two enzymes, proline oxidase and pyrroline 5-carboxylate (P5C) dehydrogenase. In this paper we report an 800-fold purification P5C dehydrogenase from rat liver mitochondria to yield an es
Autor:
Thomas W. Traut, Mary Ellen Jones
Publisher Summary The importance of maintaining balanced pyrimidine nucleotide metabolism is evident because it has been shown that many biosynthetic pathways are dependent on pyrimidines. Pyrimidine nucleotides are also important for the continued b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::985b283afba372a262cfcebec5e0f075
https://doi.org/10.1016/s0079-6603(08)60142-7
https://doi.org/10.1016/s0079-6603(08)60142-7
Human UMP synthase is a bifunctional protein containing two separate catalytic domains, orotate phosphoribosyltransferase (EC 2.4.2.10) and orotidine-5′-phosphate decarboxylase (EC 4.1.1.23). These studies address the question of why the last two r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a325bf2a18cf3cfe87cac38ca4f88a8c
Autor:
Mary Ellen Jones, Laura R. Livingstone, Byoung-Don Han, Michael J. Yablonski, Daniel A. Pasek
Publikováno v:
Biochemistry. 34(34)
Human uridine monophosphate (UMP) synthase, a bifunctional protein containing orotate phsophoribosyltransferase (OPRTase, EC 2.4.2.10) and orotidine 5'-monophosphate decarboxylase (ODCase, EC 4.1.1.23) activities, has been overproduced by constructio
Autor:
Mary Ellen Jones, Jeffrey A. Smiley
Publikováno v:
Biochemistry. 31(48)
The presence of a proton-donating catalytic amino acid side chain in orotidylate decarboxylase (ODCase) was sought by site-directed mutagenesis. Replacement of yeast ODCase Lys93 with a cysteine resulted in a mutant protein (K93C) with no measurable
Autor:
Mary Ellen Jones
Publisher Summary This chapter discusses orotidylate decarboxylase of yeast and man. Uridylic acid (UMP) biosynthesis is essential for most living organisms, providing the precursor of the three pyrimidine trinucleotides as well as for the synthesis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c3d481289869f2c7ebf88ba9145d0613
https://doi.org/10.1016/b978-0-12-152833-1.50024-1
https://doi.org/10.1016/b978-0-12-152833-1.50024-1
Autor:
Mary Ellen Jones
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461577058
I will present the recently established mechanism (1,2) for the reaction catalyzed by orotidylate decarboxylases (ODCases) and detail the characteristics of one altered ODCase that we have prepared using biotechnology. The modified protein shows the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fd72a7e2edd769d8cda857b5652daf79
https://doi.org/10.1007/978-1-4615-7703-4_68
https://doi.org/10.1007/978-1-4615-7703-4_68