Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Peter D. Robison"'
Autor:
Peter D. Robison, H.Richard Levy
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 445:475-485
1. Both Mn2+ and Co2+ can replace Mg2+ as the required divalent cation for all activities of the enzyme complex between anthranilate synthase (chorismate pyruvate-lyase (amino-accepting), EC 4.1.3.27) and anthranilate-5-phosphoribosylpyrophosphate ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::788832a960668d119a4b16dfeb5cfb61
https://doi.org/10.1016/0005-2744(76)90101-7
https://doi.org/10.1016/0005-2744(76)90101-7
Autor:
Peter D. Robison
Publikováno v:
Biotechnology Letters. 6:119-122
When grown on cellulose or xylan, Trichoderma reesei (strain Rut C-30) produced extra-cellular enzymes which could hydrolyze both cellulose and xylan to their respective monosaccharides. At low O2 saturation, β -glucosidase activity is greatly reduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f9eb9105df9ae196fb182ecc54c7a9b4
https://doi.org/10.1007/bf00127301
https://doi.org/10.1007/bf00127301
Autor:
Peter D. Robison, F. Robert Tabita
Publikováno v:
FEBS Letters. (2):369-372
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::795445951232a862f67b722e8b38d1fa
Autor:
Peter D. Robison, F. Robert Tabita
Publikováno v:
Biochemical and biophysical research communications. 88(1)
Ribulose bisphosphate carboxylase from Rhodospirillum rubrum is inactivated by low concentrations of tetranitromethane. Addition of the substrate ribulose 1,5-bisphosphate and preincubation with Mg+2 and HCO 3 − both protect against inactivation. A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec179397c8714507e67a54896d57d18a
https://pubmed.ncbi.nlm.nih.gov/110331
https://pubmed.ncbi.nlm.nih.gov/110331
Publikováno v:
Archives of biochemistry and biophysics. 193(1)
The binding of Mn 2+ to the anthranilate synthetase-phosphoribosyltransferase enzyme complex from Salmonella typhimurium was examined by electron paramagnetic resonance studies. Two types of binding sites were observed: one to two tight sites with a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b6d3f440210778a191d3408cbd36331
https://pubmed.ncbi.nlm.nih.gov/222217
https://pubmed.ncbi.nlm.nih.gov/222217
Autor:
Peter D. Robison, H.Richard Levy
Publikováno v:
Archives of biochemistry and biophysics. 193(1)
Both uncomplexed subunits of the anthranilate synthetase-phosphoribosyltransferase enzyme complex from Salmonella typhimurium have an absolute requirement for divalent metal ions which can be satisfied by Mg 2+ , Mn 2+ , or Co 2+ . The metal ion kine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac109fc92d81528c1983fc671ae95d8e
https://pubmed.ncbi.nlm.nih.gov/378135
https://pubmed.ncbi.nlm.nih.gov/378135