Zobrazeno 1 - 10 of 68 pro vyhledávání: '"V. L. Schramm"'
1
Transition-state analogs as inhibitors of human and malarial hypoxanthine-guanine phosphoribosyltransferases
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
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3
Molecular cloning and expression of a purine-specific N-ribohydrolase from Trypanosoma brucei brucei. Sequence, expression, and molecular analysis
Autor: R, Pellé, V L, Schramm, D W, Parkin
Publikováno v: The Journal of biological chemistry. 273(4)
N-Ribohydrolases, including the inosine-adenosine-guanosine-preferring (IAG) nucleoside hydrolase, have been proposed to be involved in the nucleoside salvage pathway of protozoan parasites and may constitute rational therapeutic targets for the trea
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0aef9cd1a94d614f808d7d8736c6b130
https://pubmed.ncbi.nlm.nih.gov/9442052
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4
Guanosine-inosine-preferring nucleoside N-glycohydrolase from Crithidia fasciculata
Autor: B, Estupiñán, V L, Schramm
Publikováno v: The Journal of biological chemistry. 269(37)
Protozoan parasites are incapable of de novo purine biosynthesis and obtain purines by salvage pathways. A nucleoside hydrolase which prefers inosine and uridine as substrates (IU-nucleoside hydrolase) has been characterized and implicated in purine
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8b8d4662bf1305fef6f1840d82beed7f
https://pubmed.ncbi.nlm.nih.gov/8083208
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5
Electrostatic potential surfaces of the transition state for AMP deaminase and for (R)-coformycin, a transition state inhibitor
Autor: P C, Kline, V L, Schramm
Publikováno v: The Journal of biological chemistry. 269(35)
The transition state for the hydrolysis of AMP by AMP deaminase has been characterized by heavy atom kinetic isotope effects (Merkler, D.J., Kline, P.C., Weiss, P., and Schramm, V.L. (1993) Biochemistry 32, 12993-13001). The experimentally establishe
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::99a26a2e7262426065554cfb9a6a28db
https://pubmed.ncbi.nlm.nih.gov/8071366
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7
Mutagenic analysis of AMP nucleosidase from Escherichia coli. Deletion of a region similar to AMP deaminase and peptide characterization by mass spectrometry
Autor: K, Kvalnes-Krick, J E, Labdon, X, Ma, E, Nieves, V L, Schramm
Publikováno v: The Journal of biological chemistry. 268(12)
AMP nucleosidase (EC 3.2.2.4) from Escherichia coli and AMP deaminase (EC 3.5.4.6) from bakers' yeast are proposed to regulate cellular AMP levels under allosteric control of the activator ATP and the inhibitor, PO4. Both enzymes contain catalytic si
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f432889e8aab4dfb04cfaeb4df13f4d9
https://pubmed.ncbi.nlm.nih.gov/8473316
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8
Yeast AMP deaminase. Catalytic activity in Schizosaccharomyces pombe and chromosomal location in Saccharomyces cerevisiae
Autor: P, Sollitti, D J, Merkler, B, Estupiñán, V L, Schramm
Publikováno v: The Journal of biological chemistry. 268(6)
The AMP deaminase gene was mapped to chromosome XIII of Saccharomyces cerevisiae strain JM1901. The AMP deaminase gene is located near SUP5, GAL80, SUF7, and SUF22. The presence of AMP deaminase in the fission yeast Schizosaccharomyces pombe was exam
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::75326373921bf53d31c403b0a2be29ee
https://pubmed.ncbi.nlm.nih.gov/8440738
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9
Nucleoside hydrolase from Crithidia fasciculata. Metabolic role, purification, specificity, and kinetic mechanism
Autor: D W, Parkin, B A, Horenstein, D R, Abdulah, B, Estupiñán, V L, Schramm
Publikováno v: The Journal of biological chemistry. 266(31)
Crithidia fasciculata cells grown on complex medium with added [8-14C, 5'-3H]inosine or [8-14C,5'-3H]adenosine metabolize greater than 50% of the salvaged nucleosides through a pathway involving N-glycoside bond cleavage. Cell extracts contain a subs
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::42214ca3ead5993f8489643bae6c5261
https://pubmed.ncbi.nlm.nih.gov/1939115
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10
Inactivation of chicken mitochondrial phosphoenolpyruvate carboxykinase by o-phthalaldehyde
Autor: C Y, Chen, F A, Emig, V L, Schramm, D E, Ash
Publikováno v: The Journal of biological chemistry. 266(25)
Chicken liver mitochondrial phosphoenolpyruvate carboxykinase is inactivated by o-phthalaldehyde. The inactivation followed pseudo first-order kinetics, and the second-order rate constant for the inactivation process was 29 M-1 s-1 at pH 7.5 and 25 d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::07d4c51f10a3ad49c6ca54c5ae8d5241
https://pubmed.ncbi.nlm.nih.gov/1885594
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