BIOMAT Database Logo BIOMAT Database Logo

[Localization of the arginine residues in the substrate-binding centers of muscle pyruvate dehydrogenase]. 1985

L S Khaĭlova, and N S Nemeria, and O V Lukin

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D010658 Phenylglyoxal A reagent that is highly selective for the modification of arginyl residues. It is used to selectively inhibit various enzymes and acts as an energy transfer inhibitor in photophosphorylation.
D010856 Columbidae Family in the order COLUMBIFORMES, comprised of pigeons or doves. They are BIRDS with short legs, stout bodies, small heads, and slender bills. Some sources call the smaller species doves and the larger pigeons, but the names are interchangeable. Columba livia,Doves,Pigeons,Domestic Pigeons,Feral Pigeons,Rock Doves,Rock Pigeons,Domestic Pigeon,Dove,Dove, Rock,Doves, Rock,Feral Pigeon,Pigeon,Pigeon, Domestic,Pigeon, Feral,Pigeon, Rock,Pigeons, Domestic,Pigeons, Feral,Pigeons, Rock,Rock Dove,Rock Pigeon
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
D011773 Pyruvates Derivatives of PYRUVIC ACID, including its salts and esters.
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001120 Arginine An essential amino acid that is physiologically active in the L-form. Arginine Hydrochloride,Arginine, L-Isomer,DL-Arginine Acetate, Monohydrate,L-Arginine,Arginine, L Isomer,DL Arginine Acetate, Monohydrate,Hydrochloride, Arginine,L Arginine,L-Isomer Arginine,Monohydrate DL-Arginine Acetate
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining

Related Publications

L S Khaĭlova, and N S Nemeria, and O V Lukin
Arginine residues in the active centers of muscle pyruvate dehydrogenase.
March 1984, Biochemistry international,
L S Khaĭlova, and N S Nemeria, and O V Lukin
Localization of tryptophan residues in thiamine pyrophosphate-binding sites of pyruvate dehydrogenase from pigeon breast muscle.
October 1984, Biochemistry international,
L S Khaĭlova, and N S Nemeria, and O V Lukin
[Role of muscle pyruvate dehydrogenase histidine residues in thiamine pyrophosphate binding].
January 1976, Ukrains'kyi biokhimichnyi zhurnal,
L S Khaĭlova, and N S Nemeria, and O V Lukin
Organization and functioning of muscle pyruvate dehydrogenase active centers.
January 1989, Annals of the New York Academy of Sciences,
L S Khaĭlova, and N S Nemeria, and O V Lukin
The substrate-mediated inactivation of the pyruvate dehydrogenase component of the pigeon breast muscle pyruvate dehydrogenase complex.
October 1983, Biochemistry international,
L S Khaĭlova, and N S Nemeria, and O V Lukin
Ultrastructural localization of pyruvate dehydrogenase in rat heart muscle.
March 1973, Histochemie. Histochemistry. Histochimie,
L S Khaĭlova, and N S Nemeria, and O V Lukin
6-Phosphogluconate dehydrogenase from Lactococcus lactis: a role for arginine residues in binding substrate and coenzyme.
February 1999, The Biochemical journal,
L S Khaĭlova, and N S Nemeria, and O V Lukin
[Structure of glyceraldehyde-3-phosphate dehydrogenase from rat muscle. Localization of arginine residues modified by 2,3-butanedione].
November 1982, Biokhimiia (Moscow, Russia),
L S Khaĭlova, and N S Nemeria, and O V Lukin
[Identification of catalytic centers in a decarboxylating element of muscle pyruvate dehydrogenase].
January 1987, Doklady Akademii nauk SSSR,
L S Khaĭlova, and N S Nemeria, and O V Lukin
Chemical modification of the essential arginine residues of pyruvate dehydrogenase prevents its phosphorylation by kinase.
September 1996, FEBS letters,
Copied contents to your clipboard!