Zobrazeno 1 - 10
of 365
pro vyhledávání: '"W. W. CLELAND"'
Publikováno v:
Biochemistry
Oxamate, an isosteric and isoelectronic inhibitory analogue of pyruvate, enhances the rate of enzymatic decarboxylation of oxaloacetate in the carboxyl transferase domain of pyruvate carboxylase (PC). It is unclear, though, how oxamate exerts a stimu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d019251780472b1706142d5e70f1838
https://doi.org/10.1021/bi400075t
https://doi.org/10.1021/bi400075t
Autor:
Laurie A. Reinhardt, Patrick Menden, Paul D. Cook, James B. Thoden, W. W. Cleland, Hazel M. Holden
Publikováno v:
Biochemistry. 51:3433-3444
N-Acetylperosamine is an unusual dideoxysugar found in the O-antigens of some Gram-negative bacteria, including the pathogenic Escherichia coli strain O157:H7. The last step in its biosynthesis is catalyzed by PerB, an N-acetyltransferase belonging t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95d3daae1d3becacb59ae7a3fab3cb13
https://doi.org/10.1021/bi300197h
https://doi.org/10.1021/bi300197h
Publikováno v:
Biochemistry. 47:11158-11163
A kinetic investigation of the hydrolysis of semicarbazide by urease gives a relatively flat log V/ K versus pH plot between pH 5 and 8. A log V m versus pH plot shows a shift of the optimum V m toward lower pH when compared to urea. These results ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6225a4576d37c4e741970e019f4f6f8b
https://doi.org/10.1021/bi801338c
https://doi.org/10.1021/bi801338c
Publikováno v:
The Journal of Organic Chemistry. 70:1737-1744
Multiple isotope effects have been measured for the acid-catalyzed hydrolysis of methyl formate in 0.5 M HCl at 20 degrees C. The isotope effects in the present investigation include the carbonyl carbon (13k = 1.028 +/- 0.001), the carbonyl oxygen (1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0b48fe6efe92eeae6b259e8ae64f760
https://doi.org/10.1021/jo0402733
https://doi.org/10.1021/jo0402733
Publikováno v:
Archives of Biochemistry and Biophysics. 396:219-224
l -Ribulokinase is unusual among kinases since it phosphorylates all four 2-ketopentoses with almost the same kcat values. The Km's differ, however, being 0.14 mM for l - and 0.39 mM for d -ribulose and 3.4 mM for l - and 16 mM for d -xylulose. In ad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fccc13938f4c966390e5139e39bcba9
https://doi.org/10.1006/abbi.2001.2613
https://doi.org/10.1006/abbi.2001.2613
Publikováno v:
Archives of Biochemistry and Biophysics. 396:43-48
Human malic enzyme was studied by steady state kinetics, deuterium isotope effects, and 13 C isotope effects with both the physiological dinucleotide cofactor and several alternate cofactors. The log V vs pH profile with NAD revealed two p K a values
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b032a453c59f3accacba9f075c401845
https://doi.org/10.1006/abbi.2001.2598
https://doi.org/10.1006/abbi.2001.2598
Publikováno v:
Biochemistry. 41:415-421
15N isotope effects and solvent deuterium isotope effects have been measured for the hydrolytic deamination of cytidine catalyzed by Escherichia coli cytidine deaminase and for the uncatalyzed reaction proceeding spontaneously in neutral solution at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc0aa940cb609420406aee862ba207f4
https://doi.org/10.1021/bi011410i
https://doi.org/10.1021/bi011410i
Publikováno v:
Journal of the American Chemical Society. 123:9246-9253
The remote label method was used to measure primary and secondary (18)O isotope effects in the alkaline hydrolysis of O,O-diethylphosphorylcholine iodide (DEPC) and the primary (18)O effect in the alkaline hydrolysis of O,O-diethyl-m-nitrobenzyl phos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::188244911e3d59226ee445ccfdacee4b
https://doi.org/10.1021/ja011025g
https://doi.org/10.1021/ja011025g
Publikováno v:
Biochemistry. 40:2972-2977
The transition-state structure for the reaction catalyzed by kanamycin nucleotidyltransferase has been determined from kinetic isotope effects. The primary (18)O isotope effects at pH 5.7 (close to the optimum pH) and at pH 7.7 (away from the optimum
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67552a35ec761b27ecee3d1536a04056
https://doi.org/10.1021/bi002557x
https://doi.org/10.1021/bi002557x
Publikováno v:
Biochimica et Biophysica Acta
The (13)C isotope effect for the conversion of prephenate to phenylpyruvate by the enzyme prephenate dehydratase from Methanocaldococcus jannaschii is 1.0334+/-0.0006. The size of this isotope effect suggests that the reaction is concerted. From the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfc90efdf22adcf1862879e26422eecb