| mitochondrial swelling | Increase in volume of mitochondria due to an influx of fluid; it occurs in hypotonic solutions due to osmotic pressure and in isotonic solutions as a result of altered permeability of the membranes of respiring mitochondria. (12 Dec 1998) |
|---|---|
| disease, mitochondrial | Mutations (changes) in the mitochondrial chromosome are responsible for a number of disorders including an eye disease (Leber's hereditary optic atrophy), a type of epilepsy (called MERRF which stands for Myoclonus Epilepsy with Ragged Red Fibres), and a cause of dementia (called MELAS for Mitochondrial Encephalopathy, Lactic Acidosis and Stroke-like episodes). All mitochondrial diseases were entirely enigmatic before it was discovered that they were due to mutations not in regular chromosomes but the mitochondrial chromosome. (12 Dec 1998) |
| DNA, mitochondrial | Double-stranded DNA of mitochondria. In eukaryotes, the mitochondrial genome is circular and codes for ribosomal rnas, transfer rnas, and about 10 proteins. (12 Dec 1998) |
| alkaline D-peptidase | <enzyme> A penicillin-recognizing enzyme from bacillus cereus; has beta-lactamase activity; genbank d86380 Registry number: EC 3.4.99.- Synonym: ADP gene product, alkaline d-stereospecific endopeptidase (26 Jun 1999) |
| aspartyllysine peptidase | <enzyme> From human intestinal brush border; stabilised by zn+2 Registry number: EC 3.4.13.- Synonym: zn-stable aspartyllysine peptidase (26 Jun 1999) |
| C5a peptidase | <enzyme> Streptococcus pyogenes enzyme inactivates complement 5a by cleaving at lysine 68, removing a six-amino acid fragment Pharmacological action: complement inactivators Registry number: EC 3.4.99.- Synonym: streptococcus c5a peptidase, gbs c5a-ase, group b streptococci c5a-ase, scpa protein (26 Jun 1999) |
| matrix processing peptidase | <enzyme> From matrix fraction of rat liver mitochondria; cleaves mitochondrial protein precursors; inhibited by metal chelators and reactived by mn2+; classified as EC 3.4.24.64 Registry number: EC 3.4.24.- Synonym: mitochondrial processing peptidase, mitochondrial processing protease, alpha-mpp, beta-mpp, p-52 protein, rat, p-55 protein, rat, mas1 protein, yeast, mas2 protein, yeast (26 Jun 1999) |
| peptidase | <enzyme> Alternative name for a protease. (18 Nov 1997) |
| peptidase D | <enzyme> An enzyme cleaving aminoacyl-l-proline bonds in dipeptides containing a C-terminal prolyl residue; a deficiency of this enzyme results in hyperimidodipeptiduria. Synonym: imidodipeptidase, peptidase D, prolidase. (05 Mar 2000) |
| peptidase P | <enzyme> A hydrolase cleaving C-terminal dipeptides from a variety of substrates, including angiotensin I, which is converted to angiotensin II and histidylleucine. An important step in the metabolism of certain vasopressor agents. It is a chloride-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. Only single dipeptides are released from angiotensin I and bradykinin because of the lack of activity on bonds involving proline. It may also have endopeptidase activity on some substrates. Registry number: EC 3.4.15.1 Synonym: carboxycathepsin, dipeptidyl carboxypeptidase, kinase II, peptidase P. (22 Sep 2002) |
| procollagen peptidase | <enzyme> The proteases that remove the terminal extension peptides of procollagen, deficiency of these enzymes leads to dermatosparaxis or Ehlers Danlos syndrome. (18 Nov 1997) |
| pyroglutamyl-peptidase I | <enzyme> An enzyme that catalyses the release of a n-terminal pyroglutamyl group from a polypeptide provided the next residue is not proline. It is inhibited by thiol-blocking reagents and occurs in mammalian tissues, microorganisms, and plants. Registry number: EC 3.4.19.3 (12 Dec 1998) |
| PZ-PLGPA peptidase | <enzyme> Endopeptidase from treponema denticola Registry number: EC 3.4.21.- (26 Jun 1999) |
| signal peptidase | A peptide present on proteins that are destined either to be secreted or to be membrane components. It is usually at the N terminus and normally absent from the mature protein. Normally refers to the sequence (ca 20 amino acids) that interacts with signal recognition particle and directs the ribosome to the endoplasmic reticulum where co translational insertion takes place. Could also refer to sequences that direct post translational uptake by organelles. Signal peptides are highly hydrophobic but with some positively charged residues. The signal sequence is normally removed from the growing peptide chain by signal peptidase, a specific protease located on the cisternal face of the endoplasmic reticulum. See: signal recognition particle. (18 Nov 1997) |
| signal peptidase complex | A peptide present on proteins that are destined either to be secreted or to be membrane components. It is usually at the N terminus and normally absent from the mature protein. Normally refers to the sequence (ca 20 amino acids) that interacts with signal recognition particle and directs the ribosome to the endoplasmic reticulum where co translational insertion takes place. Could also refer to sequences that direct post translational uptake by organelles. Signal peptides are highly hydrophobic but with some positively charged residues. The signal sequence is normally removed from the growing peptide chain by signal peptidase, a specific protease located on the cisternal face of the endoplasmic reticulum. See: signal recognition particle. (18 Nov 1997) |