Ananain

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Ananain
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EC no. 3.4.22.31
CAS no. 119129-70-3
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Ananain (EC 3.4.22.31, stem bromelain , fruit bromelain) is an enzyme. [1] [2] This enzyme catalyses the following chemical reaction

Hydrolysis of proteins with broad specificity for peptide bonds. Best reported small molecule substrate Bz-Phe-Val-Arg-NHMec

This enzyme is isolated from stem of pineapple plant, Ananas comosus .

Related Research Articles

<span class="mw-page-title-main">Pineapple</span> Species of flowering plant in the family Bromeliaceae

The pineapple is a tropical plant with an edible fruit; it is the most economically significant plant in the family Bromeliaceae.

In biology and biochemistry, protease inhibitors, or antiproteases, are molecules that inhibit the function of proteases. Many naturally occurring protease inhibitors are proteins.

Bromelain is an enzyme extract derived from the stems of pineapples, although it exists in all parts of the fresh pineapple. The extract has a history of folk medicine use. As an ingredient, it is used in cosmetics, as a topical medication, and as a meat tenderizer.

<span class="mw-page-title-main">Papain</span> Widely used enzyme extracted from papayas

Papain, also known as papaya proteinase I, is a cysteine protease enzyme present in papaya and mountain papaya. It is the namesake member of the papain-like protease family.

<span class="mw-page-title-main">Cysteine protease</span> Class of enzymes

Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad.

<span class="mw-page-title-main">Cystatin</span> Group of endogenous cysteine proteinase inhibitors

The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of an alpha helix lying on top of an anti-parallel beta sheet. The family is subdivided as described below.

<span class="mw-page-title-main">Cathepsin B</span> Protein-coding gene in the species Homo sapiens

Cathepsin B belongs to a family of lysosomal cysteine proteases known as the cysteine cathepsins and plays an important role in intracellular proteolysis. In humans, cathepsin B is encoded by the CTSB gene. Cathepsin B is upregulated in certain cancers, in pre-malignant lesions, and in various other pathological conditions.

Fruit bromelain is an enzyme. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Ficain</span>

Ficain also known as ficin, debricin, or higueroxyl delabarre is a proteolytic enzyme extracted from the latex sap from the stems, leaves, and unripe fruit of the American wild fig tree Ficus insipida.

<span class="mw-page-title-main">Actinidain</span> Class of enzymes

Actinidain is a type of cysteine protease enzyme found in fruits including kiwifruit, pineapple, mango, banana, figs, and papaya. This enzyme is part of the peptidase C1 family of papain-like proteases.

<span class="mw-page-title-main">Cathepsin L1</span> Protein-coding gene in the species Homo sapiens

Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. The protein is a cysteine cathepsin, a lysosomal cysteine protease that plays a major role in intracellular protein catabolism.

<span class="mw-page-title-main">Chymopapain</span> Enzyme

Chymopapain is a proteolytic enzyme isolated from the latex of papaya. It is a cysteine protease which belongs to the papain-like protease (PLCP) group. Because of its proteolytic activity, it is the main molecule in the process of chemonucleolysis, used in some procedures like the treatment of herniated lower lumbar discs in the spine by a nonsurgical method.

Glycyl endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

Caricain is an enzyme. This enzyme catalyses the following chemical reaction: Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain

Histolysin is an enzyme. This enzyme catalyses the following chemical reaction

Adenain is an enzyme. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Zingibain</span>

Zingibain, zingipain, or ginger protease is a cysteine protease enzyme found in ginger rhizomes. It catalyses the preferential cleavage of peptides with a proline residue at the P2 position. It has two distinct forms, ginger protease I (GP-I) and ginger protease II (GP-II).

<span class="mw-page-title-main">PA clan of proteases</span>

The PA clan is the largest group of proteases with common ancestry as identified by structural homology. Members have a chymotrypsin-like fold and similar proteolysis mechanisms but can have identity of <10%. The clan contains both cysteine and serine proteases. PA clan proteases can be found in plants, animals, fungi, eubacteria, archaea and viruses.

Bromelain, a concentrate of proteolytic enzymes from the pineapple plant, is used in medicine. It is approved in the European Union for the debridement of severe burn wounds under the brand name Nexobrid. It was developed by MediWound.

<span class="mw-page-title-main">Asparagine endopeptidase</span> Class of enzymes

Asparagine endopeptidase is a proteolytic enzyme from C13 peptidase family which hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. It is also known as asparaginyl endopeptidase, citvac, proteinase B, hemoglobinase, PRSC1 gene product or LGMN, vicilin peptidohydrolase and bean endopeptidase. In humans it is encoded by the LGMN gene.

References

  1. Rowan AD, Buttle DJ, Barrett AJ (November 1988). "Ananain: a novel cysteine proteinase found in pineapple stem". Archives of Biochemistry and Biophysics. 267 (1): 262–70. doi:10.1016/0003-9861(88)90031-8. PMID   3196029.
  2. Rowan AD, Buttle DJ, Barrett AJ (March 1990). "The cysteine proteinases of the pineapple plant". The Biochemical Journal. 266 (3): 869–75. PMC   1131219 . PMID   2327970.