Guanosine diphosphate d-glucose glucohydrolase

A new enzyme has been found in yeast, which catalyzes the hydrolysis of guanosine diphosphate glucose to guanosine diphosphate and glucose. The enzyme was purified about 130-fold and its kinetic properties were studied. The enzymic activity seems to be strictly specific for guanosine diphosphate glu...

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Detalles Bibliográficos
Autor principal: Sonnino, S.
Otros Autores: Carminatti, H., Cabib, E.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1966
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
LEADER 04266caa a22006617a 4500
001 PAPER-1669
003 AR-BaUEN
005 20230518203101.0
008 190411s1966 xx ||||fo|||| 00| 0 eng|d
024 7 |2 scopus  |a 2-s2.0-0014028957 
024 7 |2 cas  |a glucose, 50-99-7, 84778-64-3; glycosidase, 9032-92-2; magnesium, 7439-95-4; mannose, 31103-86-3, 3458-28-4; Glucose, 50-99-7; Glycoside Hydrolases, EC 3.2.1.; Guanine Nucleotides; Magnesium, 7439-95-4; Mannose, 31103-86-3 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a ABBIA 
100 1 |a Sonnino, S. 
245 1 0 |a Guanosine diphosphate d-glucose glucohydrolase 
260 |c 1966 
270 1 0 |m Sonnino, S.; Instituto de Investigaciones Bioquímicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490 Buenos Aires (28), Argentina 
506 |2 openaire  |e Política editorial 
520 3 |a A new enzyme has been found in yeast, which catalyzes the hydrolysis of guanosine diphosphate glucose to guanosine diphosphate and glucose. The enzyme was purified about 130-fold and its kinetic properties were studied. The enzymic activity seems to be strictly specific for guanosine diphosphate glucose, with a Km of 0.23 mm. The enzyme is active over a wide range of pH values, from 5 to 9. Guanosine diphosphate inhibits competitively and Mg++ partially relieves the inhibition. The enzyme appears to exist in soluble form in the cytoplasm. The possible significance of guanosine diphosphate glucose glucohydrolase and of sugar nucleotide phosphorylase in the control of the intracellular concentration of guanosine diphosphate glucose and guanosine diphosphate mannose is discussed. © 1966.  |l eng 
536 |a Detalles de la financiación: 8ervice 
536 |a Detalles de la financiación: Foundation for the National Institutes of Health 
536 |a Detalles de la financiación: Rockefeller Foundation 
536 |a Detalles de la financiación: 1 Dedicated to Luis F. Leloir on the occasion of his sixtieth birthday. ? This investigation was supported in part 1)~ research grant GM 03-l-12 from the National Institutes Health, Llnited States Public Health 8ervice; by the Consejo National de Investiga-ciones Cientificas y TBcnicas (Reptiblica Argentina,); and by the Rockefeller Foundation. 3 Career investigator of the Consejo National de Investigaciones Cientificas y Tficnicns (R,e-ptihlica Argentina). 4 It is generally acknowledged catalyzed by pyrophosphorylases ceeds toward the synthesis under conditions prevailing 
593 |a Instituto de Investigaciones Bioquímicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490 Buenos Aires (28), Argentina 
690 1 0 |a GLUCOSE 
690 1 0 |a GLYCOSIDASE 
690 1 0 |a GUANINE NUCLEOTIDE 
690 1 0 |a MAGNESIUM 
690 1 0 |a MANNOSE 
690 1 0 |a ARTICLE 
690 1 0 |a CHROMATOGRAPHY 
690 1 0 |a ELECTROPHORESIS 
690 1 0 |a ENZYMOLOGY 
690 1 0 |a GEL CHROMATOGRAPHY 
690 1 0 |a KINETICS 
690 1 0 |a METABOLISM 
690 1 0 |a SACCHAROMYCES 
690 1 0 |a CHROMATOGRAPHY 
690 1 0 |a CHROMATOGRAPHY, GEL 
690 1 0 |a ELECTROPHORESIS 
690 1 0 |a GLUCOSE 
690 1 0 |a GLYCOSIDE HYDROLASES 
690 1 0 |a GUANINE NUCLEOTIDES 
690 1 0 |a KINETICS 
690 1 0 |a MAGNESIUM 
690 1 0 |a MANNOSE 
690 1 0 |a SACCHAROMYCES 
700 1 |a Carminatti, H. 
700 1 |a Cabib, E. 
773 0 |d 1966  |g v. 116  |h pp. 26-33  |k n. C  |p Arch. Biochem. Biophys.  |x 00039861  |w (AR-BaUEN)CENRE-1377  |t Archives of Biochemistry and Biophysics 
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856 4 0 |u https://doi.org/10.1016/0003-9861(66)90007-5  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00039861_v116_nC_p26_Sonnino  |y Handle 
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