Category: Enzymes

  • Cathepsin G

    Cathepsin G plays an important role in eliminating intracellular pathogens and breaking down tissues at inflammatory sites, as well as in anti-inflammatory response

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  • Acid phosphatase (systematic name phosphate-monoester phosphohydrolase (acid optimum)) is an enzyme that frees attached phosphoryl groups from other molecules during digestion

    Acid phosphatase (EC 3.1.3.2, systematic name phosphate-monoester phosphohydrolase (acid optimum)) is an enzyme that frees attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase. It is stored in lysosomes and functions when these fuse with endosomes, which are acidified while they function; therefore, it has an acid pH optimum. This enzyme is present in many animal and plant…

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  • Microsomal prostaglandin E synthase-1 (mPGES-1)

    Microsomal prostaglandin E synthase-1 (mPGES-1)

    Microsomal prostaglandin E synthase-1 (mPGES-1) or Prostaglandin E synthase is an enzyme that in humans is encoded by the PTGES gene. The protein encoded by this gene is a glutathione-dependent prostaglandin E synthase. The expression of this gene has been shown to be induced by proinflammatory cytokine interleukin 1 beta (IL1B). Its expression can also be induced by tumor suppressor protein TP53, and may be involved in…

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  • β-Glucuronidases

    For α-glucuronidase, see alpha-glucuronidase. β-Glucuronidase β-Glucuronidase asymmetric unit showing active site residues Glu451, Tyr504, and Glu540, along with the potentially supporting Asn450 residue Identifiers Symbol GUSB NCBI gene 2990 HGNC 4696 OMIM 611499 RefSeq NM_000181 UniProt P08236 Other data EC number 3.2.1.31 Locus Chr. 7 q11.21 β-Glucuronidases are members of the glycosidase family of enzymes that catalyze breakdown of complex carbohydrates. Human β-glucuronidase is…

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  • Ferrochelatase catalyses the eighth and terminal step in the biosynthesis of heme, converting protoporphyrin IX into heme B

    Ferrochelatase catalyses the eighth and terminal step in the biosynthesis of heme, converting protoporphyrin IX into heme B

    Protoporphyrin ferrochelatase (EC 4.98.1.1, formerly EC 4.99.1.1, or ferrochelatase; systematic name protoheme ferro-lyase (protoporphyrin-forming)) is an enzyme encoded by the FECH gene in humans. Ferrochelatase catalyses the eighth and terminal step in the biosynthesis of heme, converting protoporphyrin IX into heme B. It catalyses the reaction: protoheme + 2 H+ = protoporphyrin + Fe2+ Function Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX in the heme biosynthesis…

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  • Transferrins

    Transferrins are not limited to only binding to iron but also to different metal ions.

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  • Erepsin

    Erepsin is a mixture of enzymes contained in a protein fraction found in the intestinal juices that digest peptones into amino acids. It is produced and secreted by the intestinal glands in the ileum and the pancreas, but it is also found widely in other cells. It is, however, a term now rarely used in scientific literature as more precise terms are preferred. History Erepsin was discovered at the…

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  • Digestive enzymes

    Digestive enzymes

    Digestive enzymes are a group of enzymes that break down polymeric macromolecules into their smaller building blocks, in order to facilitate their absorption into the cells of the body. Digestive enzymes are found in the digestive tracts of animals (including humans) and in the tracts of carnivorous plants, where they aid in the digestion of food, as well as inside cells,…

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  • Digestive enzymes

    In carnivorous plants digestive enzymes and acids break down insects and in some plants small animals. In some plants the leaf collapses on the prey to increase contact, others have a small vessel of digestive liquid. Then digestion fluids are used to digest the prey to get at the needed nitrates and phosphorus. The absorption of the needed nutrients are usually more efficient…

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