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Diglyceride acyltransferase

class of enzymes

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General referenceInterpretive dossier study · Crown Archives visual atlas
Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionJul 29, 2026
Entity authorityQ3706488
Source-derived summary

Diglyceride acyltransferase (or O-acyltransferase), DGAT, catalyzes the formation of triglycerides (triacylglycerols) from diacylglycerol and acyl-CoA. The reaction catalyzed by DGAT is considered the terminal and only committed step in the acyl-CoA-dependent triglyceride synthesis, universally important in animal, plants, and microorganisms. The conversion is essential for intestinal absorption (i.e. DGAT1) and adipose tissue formation (i.e. DGAT2) in mammalian. DGAT1 are homologous to other membrane-bound O-acyltransferases, but not all other DGATs.

Isoforms

Two important DGAT isozymes are encoded by the genes DGAT1 and DGAT2. Although both isozymes catalyze similar reactions, they share no sequence homology, which is similar to other DGATs reported in various organisms. The location of DGAT1 and DGAT2 in other organisms, as well as other DGATs have been reported in various literatures.

DGAT1 is mainly located in absorptive enterocyte cells that line the intestine and duodenum where it reassembles triglycerides that were decomposed through lipolysis in the process of intestinal absorption. DGAT1 reconstitutes triglycerides in a committed step after which they are packaged together with cholesterol and proteins to form chylomicrons.

Editorial summary

“Diglyceride acyltransferase” enters the record as class of enzymes. Crown Archives preserves that source wording while asking what Diglyceride, acyltransferase and class can confirm, complicate or overturn.

Editorial reviewA concise reference frame for defining the subject, testing terminology and identifying the institution closest to the evidence. The current 172-word lead offers orientation but no explicit four-digit date, so chronology should not be assumed. The selected authority fields contribute no independent date. Its strongest next move is a source search built around Diglyceride, acyltransferase and class.
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“Diglyceride acyltransferase” is worth following because a concise public description often conceals a longer documentary argument. Here, Diglyceride, acyltransferase and class provides the most credible route into that argument.

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The citation trail is more important than the brevity of the summary: it shows where individual claims can be examined in context. The source revision retrieved here is dated Jul 29, 2026. The linked authority identifier is Q3706488. None of the 0 selected statements returned an explicit reference.

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Source & attribution

This entry incorporates text from Diglyceride acyltransferase” 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.