Aliases: PALMCOX.
ACOX1 (acyl-CoA oxidase 1) is named by 2 disorder entries.
ai-gene-review gives ACOX1's core molecular function as acyl-CoA oxidase activity, acting in fatty acid beta-oxidation using acyl-CoA oxidase; hydrogen peroxide biosynthetic process; and very long-chain fatty acid beta-oxidation in the peroxisomal matrix. This is the first, FAD-dependent step of peroxisomal beta-oxidation, which passes electrons to oxygen and so produces hydrogen peroxide.
Both entries that name ACOX1 type it as causative: Mitchell Syndrome; and Peroxisomal Acyl-CoA Oxidase Deficiency. They are allelic disorders with opposite mechanisms.
In the recessive disorder the variants are germline, the gene sits on the node ACOX1 Straight-Chain Acyl-CoA Oxidase Deficiency, and the functional impact is recorded as loss of function. ClinGen rates that relationship definitive.
In Mitchell syndrome the recurrent p.Asn237Ser variant is germline (usually de novo), the gene sits on the node ACOX1 N237S Gain-of-Function Acyl-CoA Oxidase Hyperactivity, and the functional impact is recorded as gain of function: the same acyl-CoA oxidase activity is increased rather than lost, and the excess hydrogen peroxide damages glia. ClinGen rates this relationship definitive as well.
The KB annotates ACOX1 nodes with fatty acid beta-oxidation using acyl-CoA oxidase; and very long-chain fatty acid beta-oxidation, and both terms are among ai-gene-review's core processes for the gene (2 shared by exact identifier).
ClinGen classifies ACOX1 for 2 diseases, and 0 of them lack a dismech entry.
Underlined values are claims re-computed from the knowledge base each time this page is built. The tables below are the source of truth.
ACOX1 is a FAD-dependent peroxisomal straight-chain acyl-CoA oxidase that catalyzes the initial oxidative step of fatty-acid beta-oxidation. It converts 2,3-saturated fatty acyl-CoAs to (2E)-enoyl-CoAs and transfers electrons to molecular oxygen, producing hydrogen peroxide. Its substrate range includes medium-, long- and very-long-chain fatty acyl-CoAs and prostaglandin CoA esters; it also contributes to peroxisomal dicarboxylic-acid degradation and the chain-shortening step of DHA synthesis. The enzyme forms homodimers and enters the peroxisomal matrix through its C-terminal SKL targeting signal. Full-length component A can be cleaved into complementary B and C chains that together retain activity. Alternative isoforms differ in chain-length preference. Biallelic loss of function causes peroxisomal acyl-CoA oxidase deficiency with VLCFA accumulation. The recurrent dominant p.N237S gain-of-function variant stabilizes the dimer and increases oxidase activity and oxidative stress, producing the distinct neuropathy Mitchell syndrome.
Relationship is the entry's genetic[].relationship_type. untyped means the entry has a genetic record for the gene but does not type it; its free-text association is shown instead.
| Disorder | Relationship | Where the gene appears |
|---|---|---|
| Mitchell Syndrome |
causative
germline
gain of function
CLINGEN: definitive
|
mechanism: ACOX1 N237S Gain-of-Function Acyl-CoA Oxidase Hyperactivity
|
| Peroxisomal Acyl-CoA Oxidase Deficiency |
causative
germline
loss of function
CLINGEN: definitive
|
mechanism: ACOX1 Straight-Chain Acyl-CoA Oxidase Deficiency
|
An entry matches when ClinGen's MONDO disease is the entry's own disease term, a subtype term, or an exact-match mapping. An amber status marks an entry ClinGen supports the gene for (Definitive, Strong or Moderate) whose own record does not type it. A Limited, Disputed or Refuted tier on such an entry is not a gap.
| ClinGen disease | MOI | Classification | dismech entry |
|---|---|---|---|
| peroxisomal acyl-CoA oxidase deficiency MONDO:0009919 | AR | Definitive 2022-11-04 |
Peroxisomal Acyl-CoA Oxidase Deficiency
causative
|
| Mitchell syndrome MONDO:0030073 | AD | Definitive 2025-12-05 |
Mitchell Syndrome
causative
|
Identity from HGNC (snapshot 2026-10-01). Page layers are described in the gene pages documentation.