Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Syam Sundar, Neti"'
Autor:
Syam Sundar Neti, Debangsu Sil, Douglas M. Warui, Olga A. Esakova, Amy E. Solinski, Dante A. Serrano, Carsten Krebs, Squire J. Booker
Publikováno v:
ACS Bio & Med Chem Au. 2:509-520
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::57da87028848702da2d6e8abf77d83c9
https://doi.org/10.1021/acsbiomedchemau.2c00018
https://doi.org/10.1021/acsbiomedchemau.2c00018
Autor:
Douglas M. Warui, Debangsu Sil, Kyung-Hoon Lee, Syam Sundar Neti, Olga A. Esakova, Hayley L. Knox, Carsten Krebs, Squire J. Booker
Publikováno v:
ACS biomed chem Au. 2(5)
Lipoyl synthase (LS) catalyzes the last step in the biosynthesis of the lipoyl cofactor, which is the attachment of sulfur atoms at C6 and C8 of an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d66aa4221a8eee66c6588872b9862db
https://pubmed.ncbi.nlm.nih.gov/36281303
https://pubmed.ncbi.nlm.nih.gov/36281303
Autor:
Syam Sundar, Neti, Debangsu, Sil, Douglas M, Warui, Olga A, Esakova, Amy E, Solinski, Dante A, Serrano, Carsten, Krebs, Squire J, Booker
Publikováno v:
ACS biomed chem Au. 2(5)
Lipoic acid is an eight-carbon sulfur-containing biomolecule that functions primarily as a cofactor in several multienzyme complexes. It is biosynthesized as an attachment to a specific lysyl residue on one of the subunits of these multienzyme comple
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::99ea8f1085a62d0823fa750ef8aa46cc
https://pubmed.ncbi.nlm.nih.gov/36281299
https://pubmed.ncbi.nlm.nih.gov/36281299
Autor:
Yang Jiang, Syam Sundar Neti, Ian Sitarik, Priya Pradhan, Philip To, Yingzi Xia, Stephen D. Fried, Squire J. Booker, Edward P. O’Brien
The specific activity of enzymes can be altered over long time scales in cells by synonymous mutations, which change an mRNA molecules sequence but not the encoded proteins primary structure. How this happens at the molecular level is unknown. Here,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f81bff7a128fbcfc54a997f453490b2f
https://doi.org/10.1101/2021.08.18.456802
https://doi.org/10.1101/2021.08.18.456802
Autor:
Yang Jiang, Syam Sundar Neti, Ian Sitarik, Priya Pradhan, Philip To, Yingzi Xia, Stephen D. Fried, Squire J. Booker, Edward P. O’Brien
Publikováno v:
Nature chemistry.
The specific activity of enzymes can be altered over long timescales in cells by synonymous mutations that alter a messenger RNA molecule's sequence but not the encoded protein's primary structure. How this happens at the molecular level is unknown.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7299ec82933d9ab2a7d65832c9332910
https://pubmed.ncbi.nlm.nih.gov/36471044
https://pubmed.ncbi.nlm.nih.gov/36471044
Publikováno v:
Journal of the American Chemical Society. 140:12900-12908
Type 1 and type 2 isopentenyl diphosphate:dimethylallyl diphosphate isomerase (IDI-1 and IDI-2) catalyze the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), the fundamental building blocks for biosynthesis of i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b267ae64e4d69741812ae985f8c7e190
https://doi.org/10.1021/jacs.8b07274
https://doi.org/10.1021/jacs.8b07274
Publikováno v:
Biochemistry. 55:4229-4238
Type 2 isopentenyl diphosphate:dimethylallyl diphosphate isomerase (IDI-2) catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the isoprenoid biosynthetic pathway. The enzyme from Streptomyces pneum
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cbdb9c088548443dfec539d3b41f523
https://doi.org/10.1021/acs.biochem.6b00564
https://doi.org/10.1021/acs.biochem.6b00564
Autor:
Syam Sundar Neti, C. Dale Poulter
Publikováno v:
The Journal of Organic Chemistry. 81:5087-5092
Flavin mononucleotide (FMN) is a coenzyme for numerous proteins involved in key cellular and physiological processes. Isotopically labeled flavin is a powerful tool for studying the structure and mechanism of flavoenzyme-catalyzed reactions by a vari
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1e4f7fe1fcd752a11d198cba607206f
https://doi.org/10.1021/acs.joc.6b00640
https://doi.org/10.1021/acs.joc.6b00640
Autor:
Syam Sundar Neti, Johan Wouters, Heidi L. Schubert, C. Dale Poulter, Rita M. Cornish, Jérôme de Ruyck, Matthew Walter Janczak, André Matagne, Steven Cary Rothman
Isopentenyl diphosphate isomerase (IDI) is a key enzyme in the isoprenoid biosynthetic pathway and is required for all organisms that synthesize isoprenoid metabolites from mevalonate. Type 1 IDI (IDI-1) is a metalloprotein that is found in eukaryote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4644d3e274dd38df823a9c62f6b9600d
https://europepmc.org/articles/PMC4215930/
https://europepmc.org/articles/PMC4215930/