Zobrazeno 1 - 10
of 138
pro vyhledávání: '"William A. Bridger"'
Autor:
Hinkle, Peter C.
Publikováno v:
American Scientist, 1984 Mar 01. 72(2), 204-204.
Externí odkaz:
https://www.jstor.org/stable/27852579
Autor:
Hers, H. G.
Publikováno v:
The Quarterly Review of Biology, 1984 Dec 01. 59(4), 463-464.
Externí odkaz:
https://www.jstor.org/stable/2828295
Autor:
William A. Bridger, Leslie D. Hicks, William T. Wolodko, Edward R. Brownie, Michael N.G. James, Kim Oikawa, Cyril M. Kay, Jean-Christophe Rochet, Marie E. Fraser
Publikováno v:
Biochemistry. 39:11291-11302
Pig heart CoA transferase (EC 2.8.3.5) has been shown previously to adopt a homodimeric structure, in which each subunit has a molecular weight of 52 197 and consists of N- and C-domains linked by a hydrophilic linker or "hinge". Here we identify and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e70fc69bb3e014be7cace5c3c275dcee
https://doi.org/10.1021/bi0003184
https://doi.org/10.1021/bi0003184
Publikováno v:
Journal of Molecular Biology. 285:1633-1653
Succinyl-CoA synthetase (SCS) carries out the substrate-level phosphorylation of GDP or ADP in the citric acid cycle. A molecular model of the enzyme from Escherichia coli, crystallized in the presence of CoA, has been refined against data collected
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e389cbc287f4e4bae932d5cf4cd9e9fd
https://doi.org/10.1006/jmbi.1998.2324
https://doi.org/10.1006/jmbi.1998.2324
Autor:
Marie E. Fraser, Michael N.G. James, William A. Bridger, Darrin L. Bailey, William T. Wolodko
Publikováno v:
Journal of Molecular Biology. 285:1655-1666
Succinyl-CoA synthetase (SCS) catalyzes the substrate-level phosphorylation step of the citric acid cycle. The enzyme from Escherichia coli is an (αβ)2-heterotetramer with two active sites, one in each αβ-dimer. To determine whether the two activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::15c67299adfd1465e2c3484d910647a2
https://doi.org/10.1006/jmbi.1998.2325
https://doi.org/10.1006/jmbi.1998.2325
Publikováno v:
Journal of Biological Chemistry. 272:21151-21159
We have identified two distinct cDNAs encoding the alpha-subunit of pig heart succinyl-CoA synthetase. The derived amino acid sequence of one of these, PHalpha57, is highly similar to the alpha-subunit of the rat liver precursor enzyme. The second cD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a83f59a34e5e1f18df448f6a65d5a722
https://doi.org/10.1074/jbc.272.34.21151
https://doi.org/10.1074/jbc.272.34.21151
Autor:
Kim Oikawa, Jean-Christophe Rochet, Leslie D. Hicks, Cyril M. Kay, William T. Wolodko, William A. Bridger
Publikováno v:
Biochemistry. 36:8807-8820
The enzyme CoA transferase from porcine heart (EC 2.8.3.5) is a homodimer; each subunit consists of two domains linked by a hydrophilic "hinge" region. We have prepared separate DNA segments encoding each of these domains. Incorporation of these two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e2401128398ccfc43fd9bad2e51da96
https://doi.org/10.1021/bi9703002
https://doi.org/10.1021/bi9703002
Publikováno v:
The Breast Journal. 3:142-146
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a7538bf6f8997bf50466add7687d998f
https://doi.org/10.1111/j.1524-4741.1997.tb00158.x
https://doi.org/10.1111/j.1524-4741.1997.tb00158.x
Publikováno v:
Protein Science. 3:975-981
The enzyme CoA transferase (succinyl-CoA:3-ketoacid coenzyme A transferase [3-oxoacid CoA transferase], EC 2.8.3.5) is essential for the metabolism of ketone bodies in the mammalian mitochondrion. It is known that its catalytic mechanism involves the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::127348888d43923605a0a0a4ef484066
https://doi.org/10.1002/pro.5560030613
https://doi.org/10.1002/pro.5560030613
Publikováno v:
Protein Science. 2:1255-1262
The form of succinyl-CoA synthetase found in mammalian mitochondria is known to be an alpha beta dimer. Both GTP- and ATP-specific isozymes are present in various tissues. We have isolated essentially identical complementary DNA clones encoding the b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44f6ee5d850fd298d84aefcfeff80dc7
https://doi.org/10.1002/pro.5560020808
https://doi.org/10.1002/pro.5560020808