| cytochrome C hydrolase | <enzyme> From yeast mitochondrial inner membrane Registry number: EC 3.4.- (26 Jun 1999) |
|---|---|
| cytochrome C-methionine methyltransferase | <enzyme> Forms s-methylmethionine Registry number: EC 2.1.1.- Synonym: cyt c-met methyltransferase (26 Jun 1999) |
| cytochrome C methyltransferase | <enzyme> From crithida oncopelti Registry number: EC 2.1.1.- (26 Jun 1999) |
| cytochrome-c oxidase | <enzyme> An enzyme complex of the inner mitochondrial membrane that catalyses the reaction between ferrocytochrome c and oxygen to yield ferricytochrome c and water. It is associated with the pumping of protons and the resultant phosphorylation of ADP to ATP. The reaction is the terminal event in the electron transport scheme by which oxygen is used for fuel combustion. It is a part of Complex IV of the respiratory chain. A deficiency of one or more of the polypeptides of this complex results in neuronal loss in brain leading to psychomotor retardation and neurodegenerative disease. Synonym: cytochrome aa3, indophenol oxidase, indophenolase. Chemical name: Ferricytochrome-c:oxygen oxidoreductase Registry number: EC 1.9.3.1 (12 Dec 1998) |
| cytochrome-c peroxidase | <enzyme> A haemprotein which catalyses the oxidation of ferrocytochrome c to ferricytochrome c in the presence of hydrogen peroxide. Chemical name: Ferrocytochrome c:hydrogen-peroxide oxidoreductase Registry number: EC 1.11.1.5 (12 Dec 1998) |
| cytochrome c reductase | <enzyme> A flavoprotein containing iron. Cytochrome c may act as receptor. The enzyme reversibly catalyses the oxidation of NADH to NAD and reduced acceptor. An inherited deficiency of this complex results in overwhelming acidosis. Synonym: cytochrome c reductase. Chemical name: NADH:(acceptor) oxidoreductase Registry number: EC 1.6.99.3 (12 Dec 1998) |
| cytochrome C synthetase | <enzyme> Forms cytochrome c from the apoprotein + hemin, requires NADPH; mechanism not given 9/81 Registry number: EC 4.99.- Synonym: cytochrome c haem lyase, hccs gene product (26 Jun 1999) |
| cytochrome d | <chemical> Cytochromes (electron-transporting proteins) with a tetrapyrrolic chelate of iron as a prosthetic group in which the degree of conjugation of double bonds is less than in porphyrin. Chemical name: Cytochrome d (12 Dec 1998) |
| cytochrome oxidase | <enzyme> Terminal enzyme of the electron transport chain that accepts electrons from (i.e. Oxidizes) cytochrome C and transfers electrons to molecular oxygen. (18 Nov 1997) |
| cytochrome p-450 | <biochemistry> Enzymes of the electron transport chain that are pigmented by virtue of their haem prosthetic groups. They are highly conserved isozymes which are key components of the mixed-function oxidase system responsible for the biotransformation of many foreign compounds to mutagens and carcinogens. Most mammals have several distantly related phenobarbital-inducible gene subfamilies. (21 Jun 2000) |
| cytochrome p-450 cyp11b2 | <enzyme> A multifunctional enzyme that catalyses the conversion of corticosterone to 18-hydroxycorticosterone and the subsequent conversion of 18-hydroxycorticosterone to aldosterone. Registry number: EC 1.14.99.- (12 Dec 1998) |
| cytochrome p-450 cyp1a1 | <enzyme> A cytochrome p-450 enzyme capable of activating procarcinogenic polycyclic hydrocarbons and halogenated aromatic hydrocarbons into mutagenic compounds. Ethoxyresorufin acts as a substrate for cyp1a1 and measurement of ethoxyresorufin o-deethylase provides a more direct method of detection for this enzyme. Registry number: EC 1.- (12 Dec 1998) |
| cytochrome p-450 cyp1a2 | <enzyme> A polycyclic aromatic hydrocarbon-inducible cytochrome which is of significant clinical interest due to the large number of drug interactions associated with induction and inhibition of theophylline. Caffeine is considered to be a model substrate for this enzyme. It also metabolises theophylline and antipyrene. Environmental factors including cigarette smoking, charbroiled meat, cruciferous vegetables, and a number of drugs including phenytoin, phenobarbital, and omeprazole produce increases in cyp1a2 activity. Registry number: EC 1.- (12 Dec 1998) |
| cytochrome p-450 cyp2b1 | <enzyme> A major cytochrome p-450 enzyme which is inducible by phenobarbital in both the liver and small intestine. It is active in the metabolism of compounds like pentoxyresorufin, testosterone, and androstenedione. Cyp2b1 also mediates the activation of cyclophosphamide and ifosfamide to mutagens. Registry number: EC 1.- (12 Dec 1998) |
| cytochrome p-450 cyp2d6 | <enzyme> A polymorphic enzyme that catalyses the hydroxylation of debrisoquine. It also metabolises several antidepressants and neuroleptics. This enzyme is deficient in up to 10 percent of the population. Registry number: EC 1.14.99.- (12 Dec 1998) |
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|