2-hydroxyacyl-CoA lyase
| 2-hydroxyacyl-CoA lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.2.63 | ||||||||
| Alt. names | 2-Hydroxyphytanoyl-CoA lyase (technically narrower) | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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:[1]
- 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.[1]
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.[2]
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).[1] These two versions are known to appear in the cytoplasm and the peroxisome based on experimental evidence listed in UniProt.[3]
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).[1] The Arath version is experimentally detected in the cytoplasm, peroxisome, and plastid.[4]
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).[1]
References
External links
Media related to 2-hydroxyphytanoyl-CoA lyase at Wikimedia Commons- 2-hydroxyphytanoyl-coenzyme+A+lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)