Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Cyclohydrolase activity"'
Autor:
Li Na Zhao, Philipp Kaldis
Methylenetetrahydrofolate dehydrogenase/cyclohydrolase (MTHFD2) is a new drug target that is expressed in cancer cells but not in normal adult cells, which provides an Achilles heel to selectively kill cancer cells. Despite the availability of crysta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8178133bdce0cf5d9bc48688754fbee3
https://doi.org/10.1101/2021.11.03.467155
https://doi.org/10.1101/2021.11.03.467155
Autor:
Francis Ramond, Irène Ceballos, Paul Kuentz, Sandrine Marie, Kareen Billiemaz, Bénédicte Héron, Marie-Françoise Vincent, Marlène Rio, Monique Piraud, Anne-Sophie Denommé-Pichon, Renaud Touraine, Apolline Imbard
Publikováno v:
Journal of inherited metabolic diseaseREFERENCES. 43(6)
5-Amino-4-imidazolecarboxamide-ribosiduria (AICA)-ribosiduria is an exceedingly rare autosomal recessive condition resulting from the disruption of the bifunctional purine biosynthesis protein PURH (ATIC), which catalyzes the last two steps of de nov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::199e8b68384227c6da3dfd704f873251
https://pubmed.ncbi.nlm.nih.gov/32557644
https://pubmed.ncbi.nlm.nih.gov/32557644
Autor:
Shivjee Sah, Umesh Varshney
Publikováno v:
Biochemistry. 54:3504-3513
Methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) catalyzes interconversion of 5,10-methylene-tetrahydrofolate and 10-formyl-tetrahydrofolate in the one-carbon metabolic pathway. In some organisms, the essential requirement of 10-formyl-t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b208a7a70ba3ac9b839b3c81647aa14
https://doi.org/10.1021/acs.biochem.5b00400
https://doi.org/10.1021/acs.biochem.5b00400
Publikováno v:
IndraStra Global.
Most organisms possess bifunctional FolD 5,10-methylenetetrahydrofolate (5,10-CH2-THF) dehydrogenase-cyclohydrolase] to generate NADPH and 10-formyltetrandrofolate (10-CHO-THF) required in various metabolic steps. In addition, some organisms includin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe09eb96733ec9fee37f3c8c1a59f0be
https://igi.indrastra.com/items/show/190331
https://igi.indrastra.com/items/show/190331
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:1590-1594
In bacteria and eukaryotes, the last two steps of de novo purine biosynthesis are catalyzed by bifunctional purine-biosynthesis protein (PurH), which is composed of two functionally independent domains linked by a flexible region. The N-terminal doma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c5b43f2c82c41e133bad1948722794d
https://doi.org/10.1107/s1744309111039960
https://doi.org/10.1107/s1744309111039960
Autor:
Janis M. O'Donnell, Christopher D. Funderburk, Kevin M. Bowling, Zhinong Huang, Wendi S. Neckameyer, Nirmala Karnik, Dong Xu, Faiza Ferdousy
Publikováno v:
Journal of Biological Chemistry. 283:31449-31459
The signaling functions of dopamine require a finely tuned regulatory network for rapid induction and suppression of output. A key target of regulation is the enzyme tyrosine hydroxylase, the rate-limiting enzyme in dopamine synthesis, which is activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0cdae979e79b87502d5fe976b5bb72af
https://doi.org/10.1074/jbc.m802552200
https://doi.org/10.1074/jbc.m802552200
Publikováno v:
Biochemistry. 47:205-217
Purine biosynthesis requires ten enzymatic steps in higher organisms while prokaryotes require an additional enzyme for step six. In most organisms steps nine and ten are catalyzed by the purH gene product, a bifunctional enzyme with both 5-formamino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcaad778e81966a901b3ae9b9a0dc323
https://doi.org/10.1021/bi701406g
https://doi.org/10.1021/bi701406g
Publikováno v:
Bioorganic Chemistry. 24:220-228
The methenyltetrahydrofolate cyclohydrolase activity of the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase domain catalyzes the conversion of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. We have observed that in th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d2e1dfaf4be53e45630fdc894e48d658
https://doi.org/10.1006/bioo.1996.0020
https://doi.org/10.1006/bioo.1996.0020
Publikováno v:
Archives of Biochemistry and Biophysics. 442:133-139
Mouse fibroblasts in which the mthfd2 gene encoding mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase (NMDMC) was previously inactivated were infected with retroviral expression constructs of dehydrogenase/cyclohydrol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::247e54227ac6d80e6457b9329a2b53b6
https://doi.org/10.1016/j.abb.2005.07.022
https://doi.org/10.1016/j.abb.2005.07.022
Publikováno v:
Biochemistry. 44:13163-13171
5,10-Methylenetetrahydrofolate dehydrogenase (MTD) catalyzes the reversible oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate. This reaction is critical for the supply of one-carbon units at the required oxidation states fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::964e52419c6117b3e43830b6228cf2b3
https://doi.org/10.1021/bi051038x
https://doi.org/10.1021/bi051038x