pyruvate dehydrogenase
(redirected from PDH complex)Also found in: Encyclopedia.
py·ru·vate de·hy·dro·gen·ase
a structurally distinct collection of enzymes containing pyruvate dehydrogenase (lipoamide), dihydrolipoyl transacetylase, and dihydrolipoyl dehydrogenase.
pyruvate dehydrogenase
(1) Puruvate dehydrogenase (cytochrome), EC 1.2.2.2 (a deleted enzyme name, now covered by pyruvate dehydrogenase (quinone), EC 1.2.5.1).(2) Pyruvate dehydrogenase (acetyl-transferring), EC 1.2.4.1.
muscle enzymes
the table lists some of the most often-mentioned enzymes present in skeletal muscle, with their locations and functions. Apart from actomyosin and myosin ATPases which are associated with the contractile mechanism, they are by no means specific to muscle, being present and highly active also in other tissues. See also Krebs cycle, muscle fibre types.| Name Site | Catalyses… |
| Actomyosin ATPase (amATPase) myosin head groups | hydrolysis (Mg-dependent and triggered by rise in [Ca2+]) of terminal phosphate group of ATP when head-group is in interaction with actin, releasing energy that powers force- generation. (Compare myosin ATPase) |
| Creatine kinase (CK) cytoplasm | transfer of phosphate group from creatine phosphate to ADP, producing ATP and creatine. Isoenzymes can be distinguished in blood when either skeletal or cardiac muscle has been damaged. |
| Hexokinase (HK) cytoplasm | 'capture' of glucose after uptake from the blood, by conversion to the impermeant glucose 6-phosphate, in type 1 muscle fibres, which utilize glucose directly. |
| Lactate dehydrogenase (LDH) cytoplasm | reduction of pyruvate to lactate when oxygen tension is low, and the converse when it is high. Isoenzymes can be distinguished in blood when either skeletal or cardiac muscle has been damaged. |
| Myosin ATPase (mATPase) myosin head groups | hydrolysis (Ca2+ dependent, Mg2+ independent) of terminal phosphate group of ATP by head group alone, not interacting with actin (so not contraction-producing: cf actomyosin ATPase). Basic histochemical marker for fast vs. slow fibres. |
| Phosphofructokinase (PFK) cytoplasm | conversion of fructose 6-phosphate to fructose 1,6-diphosphate; rate-limiting for glycolysis, and sensitive to very many stimulatory and inhibitory influences. |
| Phosphorylase (PPL) cytoplasm | removal of hexose units, one at a time, from glycogen, to form glucose 1-phosphate: rate-limiting enzyme of, and histochemical marker for, glycogenolysis. |
| Pyruvate dehydrogenase (PDH) mitochondrial envelope | oxidative decarboxylation of pyruvate (from cytoplasm) to form acetyl CoA, which thence feeds into tricarboxylic acid (Krebs) cycle |
| Sarcoplasmic reticulum ATPase (srATPase) SR membrane | pumping of [Ca2+] back into SR after its electrically stimulated release |
| Succinate dehydrogenase (SDH) mitochondrial inner membrane | oxidation of succinate to fumarate, in tricarboxylic acid (Krebs) cycle. Histochemical marker for aerobic capacity. |
pyruvate
a salt, ester or anion of pyruvic acid. The term is used interchangeably with pyruvic acid. Pyruvate is the end product of glycolysis and may be metabolized in the body to lactate or to acetyl CoA. In yeast it is metabolized to ethanol.
pyruvate carboxylase
an enzyme concerned in the conversion of pyruvate to oxaloacetic acid.
pyruvate dehydrogenase
actively concerned in the decarboxylation of pyruvate to acetyl CoA and CO2.
pyruvate kinase
a glycolytic pathway enzyme (called also PK) which catalyzes the formation of pyruvate from phosphoenolpyruvate (PEP). A deficiency of the enzyme is a hereditary defect in humans and occurs also in Beagle and Basenji dogs, causing a familial nonspherocytic anemia.
pyruvate transaminase