Zobrazeno 1 - 10
of 127
pro vyhledávání: '"C, Grubmeyer"'
Autor:
A Vinitsky, C Grubmeyer
Publikováno v:
Journal of Biological Chemistry. 268:26004-26010
The pncB gene of Salmonella typhimurium was used to develop an overexpression system for nicotinate phosphoribosyltransferase (NAPRTase, EC 2.4.2.11), which forms nicotinate mononucleotide (NAMN) and PPi from nicotinate and alpha-D-5-phosphoribosyl-1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::394854b618172b322e359d06c5d6fe1d
https://doi.org/10.1016/s0021-9258(19)74485-8
https://doi.org/10.1016/s0021-9258(19)74485-8
Publikováno v:
Journal of Biological Chemistry. 268:14182-14188
The 4-electron oxidoreductase L-histidinol dehydrogenase (HDH, EC 1.1.1.23) oxidizes the amino alcohol histidinol to histidine via an aldehyde-level intermediate at a single active site. The enzyme contains two Zn2+ per dimer, and treatment with meta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a0ac89f364f0f8149f4849b48c072d3
https://doi.org/10.1016/s0021-9258(19)85225-0
https://doi.org/10.1016/s0021-9258(19)85225-0
Autor:
M.B. Bhatia, C. Grubmeyer
Publikováno v:
Archives of Biochemistry and Biophysics. 303:321-325
Orotate phosphoribosyltranferase (OPRTase) catalyzes the formation of orotidine 5'-monophosphate from the nitrogenous base orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate (PRPP). While it is known that Mg2+ is necessary for catalysis, the mechan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1775b49f03f667b88c2fc6592e239480
https://doi.org/10.1006/abbi.1993.1290
https://doi.org/10.1006/abbi.1993.1290
Autor:
C M, Li, P C, Tyler, R H, Furneaux, G, Kicska, Y, Xu, C, Grubmeyer, M E, Girvin, V L, Schramm
Publikováno v:
Nature structural biology. 6(6)
The proposed transition state for hypoxanthine-guanine phosphoribosyltransferases (HGPRTs) has been used to design and synthesize powerful inhibitors that contain features of the transition state. The iminoribitols (1S)-1-(9-deazahypoxanthin-9-yl)-1,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f736f526abe415ac7b374d7bfd3a1767
https://pubmed.ncbi.nlm.nih.gov/10360346
https://pubmed.ncbi.nlm.nih.gov/10360346
Publikováno v:
The Journal of biological chemistry. 268(27)
Orotate phosphoribosyltransferase (OPRTase; EC 2.4.2.10) catalyzes the formation of the nucleotide orotidine-5'-monophosphate from orotate and 5-phosphoribosyl-1-pyrophosphate (PRPP). The bacterial enzyme, unlike its mammalian homolog, is monofunctio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::154321e5a5733aa3a3ed049c72ab57b4
https://pubmed.ncbi.nlm.nih.gov/8376388
https://pubmed.ncbi.nlm.nih.gov/8376388
Autor:
C, Grubmeyer
Publikováno v:
Advances in experimental medicine and biology. 284
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::94d47224a64f51caca2b05920caf2d74
https://pubmed.ncbi.nlm.nih.gov/2053472
https://pubmed.ncbi.nlm.nih.gov/2053472
Autor:
C Grubmeyer, H S Penefsky
Publikováno v:
Journal of Biological Chemistry. 256:3728-3734
Occupancy of only one of two hydrolytic sites on beef heart mitochondrial ATPase (F1) by the radioactive ATP analog, 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-[gamma-32P]-triphosphate (TNP-[gamma-32P]ATP) is associated with a low rate of hydrolysis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::905eb870472faa32cdf400f8eb0004e6
https://doi.org/10.1016/s0021-9258(19)69515-3
https://doi.org/10.1016/s0021-9258(19)69515-3
Publikováno v:
Journal of Biological Chemistry. 262:13765-13772
The photoaffinity analog of ATP, 3'-O-(4-benzoyl) benzoyl ATP (BzATP), was used to covalently modify the catalytic sites on the beef heart mitochondrial F1-ATPase. In the absence of actinic illumination, BzATP was a slow substrate for the enzyme (Vma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8441d4cec21ac9d7541889c3e3675e2f
https://doi.org/10.1016/s0021-9258(19)76492-8
https://doi.org/10.1016/s0021-9258(19)76492-8
Publikováno v:
Journal of Biological Chemistry. 257:12092-12100
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3532fcb2c96d3f123f7c16cfbde4d1cc
https://doi.org/10.1016/s0021-9258(18)33683-4
https://doi.org/10.1016/s0021-9258(18)33683-4
Autor:
H S Penefsky, C Grubmeyer
Publikováno v:
Journal of Biological Chemistry. 256:3718-3727
The ribose-modified nucleotides 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP) and TNP-ADP were used to probe the catalytic sites on soluble beef heart mitochondrial adenosine triphosphatase (F1). Both compounds were potent compet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::15b58abf2981a5e044a7dda4fdfc0a56
https://doi.org/10.1016/s0021-9258(19)69514-1
https://doi.org/10.1016/s0021-9258(19)69514-1