| CCO | cytochrome C oxidase |
|---|---|
| COX | cytochrome c oxidase |
| CYC | cyclophosphamide; cytochrome C |
| CYT | cytochrome |
| cyt | cytochrome; cytology, cytological; cytoplasm, cytoplasm |
| SDR | Short-chain dehydrogenases/reductases |
|---|---|
| cytochrome a,a3 | cytochrome oxidase |
| CYP | cytochrome P |
| CYT | Cytochrome |
| COI | Cytochrome Oxidase I |
| cytochrome reductases | <enzyme> Registry number: EC 1.6.2. (12 Dec 1998) |
|---|
| ribonucleotide reductases | <enzyme> Registry number: EC 1.17.4 (12 Dec 1998) |
|---|---|
| pyrroline carboxylate reductases | <enzyme> A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD(p)h. Includes both the 2-oxidoreductase (ec 1.5.1.1) and the 5-oxidoreductase (ec 1.5.1.2). The former also reduces 1-piperidine-2-carboxylate to pipecolate and the latter also reduces 1-pyrroline-3-hydroxy-5-carboxylate to hydroxyproline. Registry number: EC 1.5.1.- (12 Dec 1998) |
| hydroxymethylglutaryl CoA reductases | <enzyme> In the biosynthesis of cholesterol, these enzymes catalyze the reduction of one of the carboxyl groups of beta-hydroxy, beta-methylglutaryl CoA to yield mevalonic acid.4 requires NADP, EC 1.1.1.88 requires NAD. Chemical name: (S)-Mevalonate:NAD+ oxidoreductase (CoA-acylating) Registry number: EC 1.1.1.88 (12 Dec 1998) |
| nitrate reductases | <enzyme> Registry number: EC 1.- (12 Dec 1998) |
| nitrite reductases | <enzyme> A group of enzymes that oxidise diverse nitrogenous substances to yield nitrite. Registry number: EC 1. (12 Dec 1998) |
| sulfite reductases | <enzyme> Hydrogen sulfide:(acceptor) oxidoreductases. Enzymes which reversibly catalyze the oxidation of hydrogen sulfide in the presence of various acceptors to sulfite and a reduced acceptor. Utilises NADP+ as the acceptor. Utilises oxidised ferredoxin as acceptor and EC 1.8.99.1 will utilise a variety of acceptors. Registry number: EC 1.8.- (12 Dec 1998) |
| quinone reductases | <enzyme> NAD(p)h:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. (NAD(p)h dehydrogenase (quinone)) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol. Registry number: EC 1.6.99. (12 Dec 1998) |
| core II protein, ubiquinol-cytochrome c reductase | <chemical> Member of the mitochondrial-protein-processing family; protein found in subunits of ubiquinol-cytochrome c reductase; amino acid sequence given in first source Synonym: core II protein, uccreductase (26 Jun 1999) |
| core I protein, ubiquinol-cytochrome c reductase | <chemical> Member of the mitochondrial-protein-processing family; protein found in subunits of ubiquinol-cytochrome c reductase; amino acid sequence given in first source Synonym: core I protein, uccreductase (26 Jun 1999) |
| porphyrin cytochrome c peroxidase | <enzyme> From yeast; haem group of cytochrome c peroxidase (EC 1.11.1.5) replaced by protoporphyrin ix Registry number: EC 1.11.1.- Synonym: pcc-peroxidase (26 Jun 1999) |
| cytochrome | <biochemistry> Any electron transfer haemoprotein having a mode of action in which the transfer of a single electron is effected by a reversible valence change of the central iron atom of the haem prosthetic group between the +2 and +3 oxidation states. Classified as cytochromes a in which the haem contains a formyl side chain, cytochromes b, which contain protohaem or a closely similar haem that is not covalently bound to the protein, cytochromes C in which protohaem or other haem is covalently bound to the protein and cytochromes d in which the iron tetrapyrrole has fewer conjugated double bonds than the haems have. Well known cytochromes have been numbered consecutively within groups and are designated by subscripts (beginning with no subscript), for example cytochromes C, c1, C2,. New cytochromes are named according to the wavelength in nanometres of the absorption maximum of the a band of the iron (II) form in pyridine, for example, C 555. Origin: Gr. Chroma = colour (18 Nov 1997) |
| cytochrome a | <chemical> Cytochromes (electron-transporting proteins) in which the haem prosthetic group is haem a, i.e., the iron chelate of cytoporphyrin ix. Chemical name: Cytochrome a (12 Dec 1998) |
| cytochrome aa3 | <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 b | <chemical> Cytochromes (electron-transporting proteins) with protoheme or a related haem as the prosthetic group. The prosthetic group is not covalently bound to the protein moiety. Chemical name: Cytochrome b (12 Dec 1998) |
| cytochrome b5 | <chemical> A cytochrome occurring in the endoplasmic reticulum that acts as an intermediate electron carrier in some reactions catalyzed by mixed function oxidases, e.g., fatty acid desaturation. It further activates molecular oxygen for an attack on the substrate. Mw 16kda. Chemical name: Cytochrome b5 (12 Dec 1998) |
Synonyms : Reductases, Cytochrome
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