Results 11 to 20 of about 746 (145)

Structural studies on dihydrolipoyl transacetylase : the core component of the pyruvate dehydrogenase complex of Azotobacter vinelandii [PDF]

, 1988
The studies described in this thesis deal with the structure of the Azotobactervinelandii dihydrolipoyl transacetylase, the core component (E 2 ) of the pyruvate dehydrogenase complex. in all organisms the pyruvate dehydrogenase complex is closely related to the 2-oxoglutarate dehydrogenase complex and, if present, the branched-chain 2-oxoacid ...
J.R.O. Hanemaaijer
core   +5 more sources

A kinetic study of dihydrolipoyl transacetylase from bovine kidney.

Journal of Biological Chemistry, 1975
The mammalian pyruvate dehydrogenase complex contains a core, consisting of dihydrolipoyl transacetylase, to which pyruvate dehydrogenase and dihydrolipoyl dehydrogenase are joined. This report describes studies on the kinetic mechanism of the transacetylase-catalyzed reaction between [1-14C]acetyl-CoA and dihydrolipoamide.
Peter Butterworth, Chun-Chien Tsai, Michael H. Eley, T.E. Roche, Lester J. Reed   +4 more
openalex   +3 more sources

DLAT activates EMT to promote HCC metastasis by regulating GLUT1-mediated aerobic glycolysis [PDF]

Molecular Medicine
Background Metabolic reprogramming is a hallmark of hepatocellular carcinoma (HCC) progression, driving aberrant cellular processes in response to pathological stimuli.
Qian Yin, Yinye Yao, Jiaojiao Ni, Yiwen Zhang, Jia Wu, Hui Zeng, Wei Wu, Wei Zhuo, Jieer Ying, Jingjing Li   +9 more
doaj   +2 more sources

Site‐directed mutagenesis of the dihydrolipoyl transacetylase component (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii [PDF]

European Journal of Biochemistry, 1991
Site‐directed mutagenesis was performed in the protease‐sensitive region, between the lipoyl and catalytic domains and in the catalytic domain, of the dihydrolipoyl transacetylase component (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii.
Egbert Schulze, Adrie H. Westphal, Hans Boumans, Arie de KOK   +3 more
openalex   +3 more sources

Mitochondrial transport and metabolism of the vitamin B-derived cofactors thiamine pyrophosphate, coenzyme A, FAD and NAD+, and related diseases: A review [PDF]

IUBMB Life, Volume 74, Issue 7, Page 592-617, July 2022., 2022
Multiple mitochondrial matrix enzymes playing key roles in metabolism require cofactors for their action. Due to the high impermeability of the mitochondrial inner membrane, these cofactors need to be synthesized within the mitochondria or be imported ...
Fiermonte G., Monne M., Palmieri F., Palmieri L.   +3 more
core   +2 more sources

Sequential ¹H and ¹⁵N nuclear magnetic resonance assignments and secondary structure of the N‐terminal lipoyl domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii [PDF]

European Journal of Biochemistry, 1994
The N‐terminal lipoyl domain (79 residues) of the transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii has been sub‐cloned and produced in Escherichia coli. Over‐expression exceeds the capacity of E. coli cells to lipoylate all expressed lipoyl domain, but addition of lipoic acid to the growth medium results in ...
Axel Berg, Arie de KOK, Jacques Vervoort
openalex   +4 more sources

Separation of Protein X from the Dihydrolipoyl Transacetylase Component of the Mammalian Pyruvate Dehydrogenase Complex and Function of Protein X

Journal of Biological Chemistry, 1989
The dihydrolipoyl transacetylase (E2)-protein X-kinase subcomplex was resolved to produce an oligomeric transacetylase that was free of protein X and kinase subunits. We investigated the properties of this transacetylase E2 oligomer and of a form of the subcomplex from which only the lipoyl-bearing domain of protein X (XL) was removed.
SUSAN L. POWERS‐GREENWOOD, Mohammed Rahmatullah, Gary A. Radke, T.E. Roche   +3 more
openalex   +3 more sources

The domain structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii [PDF]

European Journal of Biochemistry, 1987
Limited proteolysis with trypsin has been used to study the domain structure of the dihydrolipoyltransacetylase (E2) component of the pyruvate dehydrogenase complex of Azotobacter vinelandii. Two stable end products were obtained and identified as the N-terminal lipoyl domain and the C-terminal catalytic domain.
Roeland Hanemaaijer, Arie de KOK, P. Jollès, C. Veeger   +3 more
openalex   +4 more sources

Mechanism of formation and significance of antimitochondrial autoantibodies in the pathogenesis of primary biliary cholangitis [PDF]

Exploration of Immunology
Primary biliary cholangitis (PBC) is a chronic cholestatic progressive liver disease associated with cholangiopathies. The detection of antimitochondrial autoantibodies (AMAs) plays an important role in the diagnosis of classical PBC.
Vasiliy Ivanovich Reshetnyak, Igor Veniaminovich Maev   +1 more
doaj   +3 more sources

Properties of the pyruvate dehydrogenase kinase bound to and separated from the dihydrolipoyl transacetylase-protein X subcomplex and evidence for binding of the kinase to protein X.

Journal of Biological Chemistry, 1986
Studies were conducted on four pyruvate dehydrogenase kinase-containing fractions: purified pyruvate dehydrogenase complex, the dihydrolipoyl transacetylase-protein X-kinase subcomplex (E2.X.K), a kinase fraction (K fraction) prepared from the E2.X.K subcomplex, and a kinase fraction generated by limited trypsin-digestion of E2.X.K.
Mohammed Rahmatullah, Joseph M. Jilka, Gary A. Radke, T.E. Roche   +3 more
openalex   +3 more sources