Biomaterial Database

Time-resolved fluorescence studies on the dihydrolipoyl transacetylase (E2) component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. 1988

R Hanemaaijer, and R Masurel, and A J Visser, and A de Kok, and C Veeger

Department of Biochemistry, Agricultural University, Wageningen, The Netherlands.

The dihydrolipoyl transacetylase (E2) component of A. vinelandii PDC and its lipoyl domain shows similar dynamic properties as revealed with fluorescence anisotropy decay of lipoyl-bound IAANS. The lipoyl domain (32.6 kDa), containing three almost identical subdomains shows a mode of rotation characteristic for a protein of about 30 kDa. A similar rotation is found in E2, indicating an independent rotational mobility of the whole domain in the multimeric E2 core (1.6 MDa). No independent rotation of a single lipoyl subdomain (10 kDa) is observed. The E1 component, in contrast to the E3 component, shows interaction with the lipoyl domain.

UI	MeSH Term	Description	Entries
D009282	Naphthalenesulfonates	A class of organic compounds that contains a naphthalene moiety linked to a sulfonic acid salt or ester.
D011768	Pyruvate Dehydrogenase Complex	A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)	Complex, Pyruvate Dehydrogenase,Dehydrogenase Complex, Pyruvate
D005454	Fluorescence Polarization	Measurement of the polarization of fluorescent light from solutions or microscopic specimens. It is used to provide information concerning molecular size, shape, and conformation, molecular anisotropy, electronic energy transfer, molecular interaction, including dye and coenzyme binding, and the antigen-antibody reaction.	Anisotropy, Fluorescence,Fluorescence Anisotropy,Polarization, Fluorescence,Anisotropies, Fluorescence,Fluorescence Anisotropies,Fluorescence Polarizations,Polarizations, Fluorescence
D005456	Fluorescent Dyes	Chemicals that emit light after excitation by light. The wave length of the emitted light is usually longer than that of the incident light. Fluorochromes are substances that cause fluorescence in other substances, i.e., dyes used to mark or label other compounds with fluorescent tags.	Flourescent Agent,Fluorescent Dye,Fluorescent Probe,Fluorescent Probes,Fluorochrome,Fluorochromes,Fluorogenic Substrates,Fluorescence Agents,Fluorescent Agents,Fluorogenic Substrate,Agents, Fluorescence,Agents, Fluorescent,Dyes, Fluorescent,Probes, Fluorescent,Substrates, Fluorogenic
D000123	Acetyltransferases	Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.	Acetyltransferase
D001395	Azotobacter	A genus of gram-negative, aerobic bacteria found in soil and water. Its organisms occur singly, in pairs or irregular clumps, and sometimes in chains of varying lengths.
D051047	Dihydrolipoyllysine-Residue Acetyltransferase	An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.	Acetyl-CoA-Dihydrolipoamide S-Acetyltransferase,Dihydrolipoamide Acetyltransferase,Dihydrolipoamide S-Acetyltransferase,Dihydrolipoyl Acetyltransferase,Dihydrolipoyl Transacetylase,Lipoate Acetyltransferase,Pyruvate Dehydrogenase Complex E2,Acetyl CoA Dihydrolipoamide S Acetyltransferase,Acetyltransferase, Dihydrolipoamide,Acetyltransferase, Dihydrolipoyl,Acetyltransferase, Dihydrolipoyllysine-Residue,Acetyltransferase, Lipoate,Dihydrolipoamide S Acetyltransferase,Dihydrolipoyllysine Residue Acetyltransferase,S-Acetyltransferase, Acetyl-CoA-Dihydrolipoamide,S-Acetyltransferase, Dihydrolipoamide,Transacetylase, Dihydrolipoyl