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2-hydroxyacyl-CoA lyase

class of enzymes

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Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionJul 3, 2026
Entity authorityQ2813814 ↗
Source-derived summary

2-Hydroxyacyl-CoA lyase (EC 4.1.2.63) is an enzyme found in the peroxisomes of eukaryotes that catalyzes the following leading-up step of alpha oxidation:

a 2-hydroxy-3-methyl fatty acyl-CoA = a 2-methyl-branched fatty aldehyde + formyl-CoA

an (R)-2-hydroxy-long-chain-fatty acyl-CoA = a long-chain fatty aldehyde + formyl-CoA

It requires thiamine diphosphate (ThDP) as cofactor.

In animals

The entry is intended to mainly represent the class of enzymes examplified by human HACL1 (gene), which can catalyze both reactions and is found in the peroxisome. It is required for handling phytanic acid.

Humans and other mammals have another similar enzymes that only catalyzes reaction (2) and is instead located in the endoplasmic reticulum, HACL2 (gene). This one participates in phytosphingosine degradation.

In fungi

Both the baker's yeast and the fission yeast have a Pxp1 gene corresponding to this activity, as annotated on UniProt by sequence similarity (not by experimental characterization of enzyme activity). These two versions are known to appear in the cytoplasm and the peroxisome based on experimental evidence listed in UniProt.

In plants

Both the mouse-ear cress (Arath) and the rice have a HACL gene corresponding to this activity, as annotated on UniProt by sequence similarity (not by experimental characterization of enzyme activity). The Arath version is experimentally detected in the cytoplasm, peroxisome, and plastid.

In other organisms

UniProt reports that the social ameoba Dictyostelium discoideum has a version of this enzyme, as annotated on UniProt by sequence similarity (not by experimental characterization of enzyme activity).

Editorial summary

Begin with the source’s own compact description: “2-hydroxyacyl-CoA lyase” is class of enzymes. The dossier treats that line as a proposition to test through 2-hydroxyacyl-CoA, lyase and class, not as a finished interpretation.

Editorial reviewA concise reference frame for defining the subject, testing terminology and identifying the institution closest to the evidence. The current 242-word lead offers orientation but no explicit four-digit date, so chronology should not be assumed. The selected authority fields contribute no independent date. For this dossier, 2-hydroxyacyl-CoA, lyase and class is the immediate research focus.
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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 Jul 3, 2026. The linked authority identifier is Q2813814. None of the 0 selected statements returned an explicit reference.

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Source & attribution

This entry incorporates text from “2-hydroxyacyl-CoA lyase” 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.