GO_REF:0000002

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000033

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000041

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000044

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000120

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000121

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

PMID:11060344

Mitochondrial and peroxisomal targeting of 2-methylacyl-CoA racemase in humans.

Human AMACR carries a C-terminal PTS1 variant recognised by Pex5p and N-terminal mitochondrial targeting information; basis of the human-donor localization transfers and the likely source of the (removed) signaling receptor binding transfer.

"The enzyme activity is found not only in peroxisomes but also is present in mitochondria of human liver and fibroblasts."

PMID:11060359

Subcellular localization and physiological role of alpha-methylacyl-CoA racemase.

AMACR localizes to peroxisomes and mitochondria and has physiological roles in branched-chain lipid metabolism.

"Subcellular localization and physiological role of alpha-methylacyl-CoA racemase."

PMID:11964182

The role of alpha-methylacyl-CoA racemase in bile acid synthesis.

Alpha-methylacyl-CoA racemase participates in bile acid synthesis through an alternative peroxisomal pathway.

"The role of alpha-methylacyl-CoA racemase in bile acid synthesis."

PMID:14561759

Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease.

Rat liver peroxisome proteomics identifies peroxisomal proteins and supports peroxisomal localization context.

"Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease."

PMID:7649182

Purification and characterization of an alpha-methylacyl-CoA racemase from human liver.

Purified alpha-methylacyl-CoA racemase accepts pristanoyl-CoA and trihydroxycoprostanoyl-CoA and supports peroxisomal/mitochondrial lipid metabolism context.

"Purification and characterization of an alpha-methylacyl-CoA racemase from human liver."

PMID:8020470

Purification and properties of an alpha-methylacyl-CoA racemase from rat liver.

Purified rat liver AMACR catalyzes interconversion of alpha-methyl-branched acyl-CoA stereoisomers.

"Purification and properties of an alpha-methylacyl-CoA racemase from rat liver."

PMID:9106621

Molecular cloning and expression of a 2-arylpropionyl-coenzyme A epimerase: a key enzyme in the inversion metabolism of ibuprofen.

Rat Amacr/2-arylpropionyl-CoA epimerase cloning and expression support alpha-methylacyl-CoA racemase activity.

"Molecular cloning and expression of a 2-arylpropionyl-coenzyme A epimerase: a key enzyme in the inversion metabolism of ibuprofen."

file:rat/Amacr/Amacr-deep-research-falcon.md

Falcon (Edison Scientific) deep research report: Rat Amacr / AMACR (UniProt P70473) functional annotation

AMACR is a cofactor-independent racemase/epimerase that inverts the C2 (alpha-carbon) stereochemistry of 2-methyl-branched acyl-CoA thioesters, interconverting (2R) and (2S) forms.

"AMACR is a **cofactor-independent racemase/epimerase** that catalyzes the **stereochemical inversion (racemization/epimerization) at C2 (α-carbon)** of **2-methyl-branched acyl-CoA thioesters**, converting **(2R) ↔ (2S)** forms."
Pristanoyl-CoA and chain-shortened derivatives from branched-chain lipid metabolism are among the best-supported AMACR substrate classes.

"**Pristanoyl-CoA** and **chain-shortened derivatives** from branched-chain lipid metabolism."
AMACR acts on CoA esters of bile-acid side-chain intermediates, particularly DHCA-CoA and THCA-CoA stereoisomers.

"**CoA esters of bile-acid side-chain intermediates**, particularly **DHCA-CoA** and **THCA-CoA** stereoisomers (commonly discussed as 25R/25S-related stereochemistry)."
AMACR enables catabolism of dietary or isoprenoid-derived alpha-methyl-branched fatty acids in the phytanic to pristanic acid axis by converting the 2R-enantiomer to the 2S-enantiomer used by beta-oxidation.

"AMACR is positioned as a key node enabling catabolism of dietary or isoprenoid-derived **α-methyl-branched fatty acids**, particularly in the **phytanic → pristanic acid** metabolic axis, by converting the 2R-enantiomer to the 2S-enantiomer used by β-oxidation."
AMACR participates in side-chain shortening of C27 bile-acid intermediates (DHCA/THCA) that contributes to formation of mature bile acids.

"AMACR also participates in metabolism/processing of **C27 bile-acid intermediates** (DHCA/THCA) during side-chain shortening steps that contribute to formation of mature bile acids."
Rat-focused evidence places AMACR/racemase activity in both peroxisomes and mitochondria, with purification from rat liver mitochondrial fractions despite peroxisomal targeting features in the sequence.

"Primary rat-focused evidence indicates AMACR/racemase activity occurs in **both peroxisomes and mitochondria**, and that AMACR was purified from **rat liver mitochondrial fractions** (monomeric protein ~45–47 kDa) despite peroxisomal targeting features in the sequence."
Rat AMACR ends in the tetrapeptide KANL, a PTS1-like peroxisomal targeting signal.

"Rat AMACR ends in the tetrapeptide **KANL**, described as a **PTS1-like** peroxisomal targeting signal."
AMACR localization should be represented as dual-organelle biology with species- and study-dependent partitioning, not as exclusively peroxisomal.

"This should be represented as **dual-organelle biology with species- and study-dependent partitioning**, not as exclusively peroxisomal."