Zobrazeno 1 - 10
of 53
pro vyhledávání: '"William A. Bridger"'
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
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
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
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
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
Publikováno v:
The Breast Journal. 3:142-146
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
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
Autor:
Guohua Fong, William A. Bridger
Publikováno v:
Biochemistry. 31:5661-5664
Succinyl-CoA synthetase of Escherichia coli (alpha 2B2 subunit structure) has been shown to fold and assemble without participation by molecular chaperones. Renaturation experiments showed that purified bacterial chaperone GroEL has no effect on the
Autor:
William A. Bridger, Tianwei Lin
Publikováno v:
Journal of Biological Chemistry. 267:975-978
We have isolated a full-length cDNA clone encoding the cytoplasmic precursor to pig heart mitochondrial CoA transferase (succinyl-CoA:3-ketoacid coenzyme A transferase (3-oxoacid CoA transferase, EC 2.8.3.5], a key enzyme for ketone body catabolism.