|
Carbonyl Cyanide m-Chlorophenyl Hydrazone
|
D002258 |
[A proton ionophore. It is commonly used as an uncoupling agent and inhibitor of photosynthesis because of its effects on mitochondrial and chloroplast membranes.
] |
|
Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone
|
D002259 |
[A proton ionophore that is commonly used as an uncoupling agent in biochemical studies.
] |
|
Carbonyl Reductase (NADPH)
|
D000074409 |
[NADPH-dependent reductase that catalyzes the reduction of many carbonyl compounds including QUINONES; PROSTAGLANDINS; and XENOBIOTICS.
] |
|
Carboplatin
|
D016190 |
[An organoplatinum compound that possesses antineoplastic activity.
] |
|
Carboprost
|
D002260 |
[A nonsteroidal abortifacient agent that is effective in both the first and second trimesters of PREGNANCY.
] |
|
Carboxin
|
D002261 |
[A systemic agricultural fungicide and seed treatment agent.
] |
|
Carboxy-Lyases
|
D002262 |
[Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
] |
|
Carboxyhemoglobin
|
D002263 |
|
|
Carboxyl and Carbamoyl Transferases
|
D019878 |
[A group of enzymes that catalyze the transfer of carboxyl- or carbamoyl- groups. EC 2.1.3.
] |
|
Carboxylesterase
|
D043182 |
[Carboxylesterase is a serine-dependent esterase with wide substrate specificity. The enzyme is involved in the detoxification of XENOBIOTICS and the activation of ester and of amide PRODRUGS.
] |
|
Carboxylic Acids
|
D002264 |
[Organic compounds containing the carboxy group (-COOH). This group of compounds includes amino acids and fatty acids. Carboxylic acids can be saturated, unsaturated, or aromatic.
] |
|
Carboxylic Ester Hydrolases
|
D002265 |
[Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.
] |
|
Carboxymethylcellulose Sodium
|
D002266 |
[A cellulose derivative which is a beta-(1,4)-D-glucopyranose polymer. It is used as a bulk laxative and as an emulsifier and thickener in cosmetics and pharmaceuticals and as a stabilizer for reagents.
] |
|
Carboxypeptidase B
|
D043424 |
[A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. The enzyme catalyzes the preferential cleavage of a C-terminal peptidyl-L-lysine or arginine. It was formerly classified as EC 3.4.2.2 and EC 3.4.12.3.
] |
|
Carboxypeptidase B2
|
D025901 |
[A carboxypeptidase that removes C-terminal lysine or arginine from peptides and proteins. Carboxypeptidase B2 (CPB2) is released into the circulation as a proenzyme which is activated by the THROMBIN-THROMBOMODULIN complex. Activated CPB2 is involved in modulating a variety of processes by cleaving and inactivating various circulating proteins and peptides that are its substrates including FIBRIN; KININS; and ANAPHYLATOXINS.
] |
|
Carboxypeptidase H
|
D043423 |
[A ZINC-containing exopeptidase primarily found in SECRETORY VESICLES of endocrine and neuroendocrine cells. It catalyzes the cleavage of C-terminal ARGININE or LYSINE residues from polypeptides and is active in processing precursors of PEPTIDE HORMONES and other bioactive peptides.
] |
|
Carboxypeptidases
|
D002268 |
[Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
] |
|
Carboxypeptidases A
|
D043422 |
[Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC 3.4.2.1 and EC 3.4.12.2.
] |
|
Carbuncle
|
D002270 |
[An infection of cutaneous and subcutaneous tissue that consists of a cluster of boils. Commonly, the causative agent is STAPHYLOCOCCUS AUREUS. Carbuncles produce fever, leukocytosis, extreme pain, and prostration.
] |
|
Carbutamide
|
D002271 |
[A sulfonylurea antidiabetic agent with similar actions and uses to CHLORPROPAMIDE. (From Martindale, The Extra Pharmacopoeia, 30th ed, p277)
] |