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C3-convertase

class of enzymes

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Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionNov 29, 2024
Entity authorityQ5008114 ↗
Source-derived summary

C3 convertase (C4bC2b, formerly C4b2a) belongs to family of serine proteases and is necessary in innate immunity as a part of the complement system which eventuate in opsonisation of particles, release of inflammatory peptides, C5 convertase formation and cell lysis.

C3 convertase can be used to refer to the form produced in the alternative pathway (C3bBb) or the classical and lectin pathways (C4bC2b, formerly C4b2a). Once formed, both C3 convertases will catalyze the proteolytic cleavage of C3 into C3a and C3b (hence the name "C3-convertase").

The smaller fragment called C3a serves to increase vascular permeability and promote extravasation of phagocytes, while the larger C3b fragment can be used as an opsonin or bind to either type of C3 convertase to form the trimolecular C5 convertase to activate C5 for the membrane attack complex.

Formation

C3 convertase formation can occur in three different pathways: the classical, lectin, and alternative pathways.

Alternative pathway

Cleavage of complement C3 by a free floating convertase, thrombin, plasmin or even a bacterial enzyme leads to formation of C3a and C3b fragments. C3b, the larger fragment, becomes covalently attached to the microbial surface or to the antibody molecules through the thioester domain at the site of complement activation. After cleavage and binding to cell surface, the C3b fragment is ready to bind a plasma protein called Factor B. The Factor B (a zymogen) is cleaved by a plasma serine protease Factor D releasing a small fragment called Ba and generating a larger fragment called Bb that remains attached to C3b. Also Mg2+ ions are necessary for forming a functional C3 convertase. Thus, the alternative C3 convertase (C3bBb) is formed and is able to cleave C3 via its dimeric Bb subunit.

Editorial summary

This brief starts where responsible research should: with the source description of “C3-convertase” as class of enzymes. Everything that follows is an evidence route, not borrowed authority.

Editorial reviewA practical starting point whose main value is the path it opens into stronger specialist and primary sources. The current 283-word lead offers orientation but no explicit four-digit date, so chronology should not be assumed. The selected authority fields contribute no independent date. The account is most persuasive where C3-convertase, class and enzymes can be independently traced.
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The subject matters to the general reference register because the source frames it as class of enzymes. Its deeper value depends on whether names, dates, institutions and citations support that framing.

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Vocabulary and entity names are the principal evidence signals here, because they determine the precision of every later search. The source revision retrieved here is dated Nov 29, 2024. The linked authority identifier is Q5008114. None of the 0 selected statements returned an explicit reference.

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Source & attribution

This entry incorporates text from “C3-convertase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.