All individuals in MeSH

Label Id Description
Pyruvate Dehydrogenase (Lipoamide)-Phosphatase D011769 [(Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43. ]
Pyruvate Dehydrogenase Acetyl-Transferring Kinase D000081382 [A pyruvate dehydrogenase kinase isozyme located in the mitochondria which converts PYRUVATE to ACETYL CoA in the CITRIC ACID CYCLE, phosphorylates SERINE residues on pyruvate dehydrogenase using ATP, and plays a key role in the regulation of GLUCOSE and fatty acid metabolism. ]
Pyruvate Dehydrogenase Complex D011768 [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) ]
Pyruvate Dehydrogenase Complex Deficiency Disease D015325 [An inherited metabolic disorder caused by deficient enzyme activity in the PYRUVATE DEHYDROGENASE COMPLEX, resulting in deficiency of acetyl CoA and reduced synthesis of acetylcholine. Two clinical forms are recognized: neonatal and juvenile. The neonatal form is a relatively common cause of lactic acidosis in the first weeks of life and may also feature an erythematous rash. The juvenile form presents with lactic acidosis, alopecia, intermittent ATAXIA; SEIZURES; and an erythematous rash. (From J Inherit Metab Dis 1996;19(4):452-62) Autosomal recessive and X-linked forms are caused by mutations in the genes for the three different enzyme components of this multisubunit pyruvate dehydrogenase complex. One of the mutations at Xp22.2-p22.1 in the gene for the E1 alpha component of the complex leads to LEIGH DISEASE. ]
Pyruvate Kinase D011770 [ATP:pyruvate 2-O-phosphotransferase. A phosphotransferase that catalyzes reversibly the phosphorylation of pyruvate to phosphoenolpyruvate in the presence of ATP. It has four isozymes (L, R, M1, and M2). Deficiency of the enzyme results in hemolytic anemia. EC 2.7.1.40. ]
Pyruvate Metabolism, Inborn Errors D015323 [Hereditary disorders of pyruvate metabolism. They are difficult to diagnose and describe because pyruvate is a key intermediate in glycolysis, gluconeogenesis, and the tricarboxylic acid cycle. Some inherited metabolic disorders may alter pyruvate metabolism indirectly. Disorders in pyruvate metabolism appear to lead to deficiencies in neurotransmitter synthesis and, consequently, to nervous system disorders. ]
Pyruvate Oxidase D011771
Pyruvate Synthase D050743 [A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE. ]
Pyruvate, Orthophosphate Dikinase D011772 [An enzyme that catalyzes the reaction of ATP, pyruvate, and orthophosphate to form AMP plus phosphoenolpyruvate plus pyrophosphate. EC 2.7.9.1. ]
Pyruvates D011773 [Derivatives of PYRUVIC ACID, including its salts and esters. ]
Pyruvic Acid D019289 [An intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed) ]
Pyrvinium Compounds D011774
Pythiosis D058968 [A granulomatous disease caused by the aquatic organism PYTHIUM insidiosum and occurring primarily in horses, cattle, dogs, cats, fishes, and rarely in humans. It is classified into three forms: ocular, cutaneous, and arterial. ]
Pythium D011775 [A genus of destructive root-parasitic OOMYCETES in the family Pythiaceae, order Peronosporales, commonly found in cultivated soils all over the world. Differentiation of zoospores takes place in a vesicle. ]
Pyuria D011776 [The presence of white blood cells (LEUKOCYTES) in the urine. It is often associated with bacterial infections of the urinary tract. Pyuria without BACTERIURIA can be caused by TUBERCULOSIS, stones, or cancer. ]
Q Fever D011778 [An acute infectious disease caused by COXIELLA BURNETII. It is characterized by a sudden onset of FEVER; HEADACHE; malaise; and weakness. In humans, it is commonly contracted by inhalation of infected dusts derived from infected domestic animals (ANIMALS, DOMESTIC). ]
Q beta Replicase D011777 [An enzyme that catalyzes the replication of the RNA of coliphage Q beta. EC 2.7.7.-. ]
Q-SNARE Proteins D050682 [SNARE proteins in which the central amino acid residue of the SNARE motif is a GLUTAMINE. They are classified separately from the R-SNARE PROTEINS where the central amino acid residue of the SNARE motif is an ARGININE. Subfamilies, the QA-SNARES; QB-SNARES; and QC-SNARES are grouped by the position of their SNARE motif-containing-domains in the SNARE complex and by their sequence similarities. ]
Q-Sort D011779 [A personality assessment technique in which the subject or observer indicates the degree to which a standardized set of descriptive statements actually describes the subject. The term reflects "sorting" procedures occasionally used with this technique. ]
Qa-SNARE Proteins D050765 [A subfamily of Q-SNARE PROTEINS which occupy the same position as syntaxin 1A in the SNARE complex and which also are most similar to syntaxin 1A in their AMINO ACID SEQUENCE. This subfamily is also known as the syntaxins, although a few so called syntaxins are Qc-SNARES. ]