Zobrazeno 1 - 10
of 137
pro vyhledávání: '"Jesse C. Rabinowitz"'
Autor:
Jesse C. Rabinowitz, Jae Mahn Song
Publikováno v:
FEBS Letters. 376:229-232
The yeast ADE3(1–333) gene which encodes a truncated protein containing the N-terminal 5,10-methylene-tetrahydrofolate (THF) dehydrogenase (D)/5,10-methynyl-THF cyclohydrolase (C) domain of cytoplasmic trifunctional C1-THF synthase is able to compl
Publikováno v:
Yeast. 11:383-389
A gene designated RPL19A has been identified in the region downstream from the 3′-end of the Saccharomyces cerevisiae MIS1 gene encoding the mitochondrial C1-tetrahydrofolate synthase. The gene codes for the yeast ribosomal protein YL19 which exhib
Autor:
J M Nour, Jesse C. Rabinowitz
Publikováno v:
Journal of Biological Chemistry. 267:16292-16296
The one-carbon metabolism enzymes 10-formyltetrahydrofolate synthetase (EC 6.3.4.3), 5,10-methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9), and 5,10-methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5) can be found on a single trifunctional prote
Autor:
Linda D'Ari, Jesse C. Rabinowitz
Publikováno v:
Journal of Biological Chemistry. 266:23953-23958
We have purified the enzyme 5,10-methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5) from Escherichia coli to homogeneity by a newly devised procedure. The enzyme has been purified at least 2,000-fold in a 31% yield. The specific activity of the enz
Autor:
Jesse C. Rabinowitz, J M Nour
Publikováno v:
Journal of Biological Chemistry. 266:18363-18369
One-carbon metabolism mediated by folate coenzymes plays an essential role in several major cellular processes. In the prokaryotes studied, three folate-dependent enzymes, 10-formyltetrahydrofolate synthetase (EC 6.3.4.3), 5,10-methenyltetrahydrofola
Autor:
Jesse C. Rabinowitz, R L Vellanoweth
Publikováno v:
Journal of Bacteriology. 173:67-72
Gene 6 mRNA of Bacillus subtilis phage phi 29 is inefficiently translated under standard in vitro conditions by Escherichia coli, while it is efficiently translated by the in vitro system derived from B. subtilis. This is a rare example of the inabil
Autor:
Barry L. Stoddard, Edwin Cheung, Jesse C. Rabinowitz, David H. Dyer, Jie-Yu Huang, Linda D'Ari
Publikováno v:
Proteins: Structure, Function, and Genetics. 27:322-324
A bifunctional enzyme that catalyzes the conversion of formyltetrahydro- folate to methylene-tetrahydrofolate (5,10- methenyltetrahydrofolate cyclohydrolase and 5,10- methylene tetrahydrofolate dehydroge- nase), has been subcloned from a cDNAlibrary,
Autor:
Jesse C. Rabinowitz, Edwin Cheung, Jie-Yu Huang, Barry L. Stoddard, Jill M. Bolduc, Linda D'Ari
Publikováno v:
Proteins: Structure, Function, and Genetics. 27:319-321
The monofunctional enzyme 10-formyltetrahydrofolate synthetase (THFS), which is responsible for the recruitment of single carbon units from the formate pool into a variety of folate-dependent biosynthetic pathways, has been subcloned, purified, and c
Autor:
Jesse C. Rabinowitz, David H. Dyer, Betty W. Shen, Barry L. Stoddard, Jie-Yu Huang, Linda D'Ari
The structure of a bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/cyclohydrolase from Escherichia coli has been determined at 2.5 A resolution in the absence of bound substrates and compared to the NADP-bound structure of the homologous e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a31824731220012a399ef43992e5dada
https://europepmc.org/articles/PMC2144347/
https://europepmc.org/articles/PMC2144347/
Autor:
Jae Mahn Song, Jesse C. Rabinowitz
The protein product of the ADE3 gene of the yeast Saccharomyces cerevisiae has been identified as the cytoplasmic trifunctional C1-tetrahydrofolate (THF) synthase, which possesses 10-formyl-THF synthetase (EC 6.3.4.3), 5,10-methenyl-THF cyclohydrolas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b67eb8e8c5f54d173f69621dc9e92da
https://europepmc.org/articles/PMC46150/
https://europepmc.org/articles/PMC46150/