ACAT1 Human
Description
ACAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
IHMGSCAENT AKKLNIARNE QDAYAINSYT RSKAAWEAGK FGNEVIPVTV TVKGQPDVVV KEDEEYKRVD FSKVPKLKTV FQKENGTVTA ANASTLNDGA AALVLMTADA AKRLNVTPLA RIVAFADAAV EPIDFPIAPV YAASMVLKDV GLKKEDIAMW EVNEAFSLVV LANIKMLEID
PQKVNINGGA VSLGHPIGMS GARIVGHLTH ALKQGEYGLA SICNGGGGAS AMLIQKL.
Product Science Overview
The ACAT1 gene is located on chromosome 11q22.3-q23.1 and spans approximately 27 kilobases. It contains twelve exons interrupted by eleven introns . The gene’s promoter region lacks a TATA box but contains multiple GC-rich sequences and CAAT boxes, which are essential for transcription factor binding .
The human ACAT1 gene produces a chimeric mRNA through trans-splicing, a process where separate transcripts from chromosomes 1 and 7 are spliced together . This results in the translation of two isoforms: a 50-kDa ACAT1 and a 56-kDa isoform, both of which are enzymatically active .
The ACAT1 protein is a homotetramer composed of 427 amino acids, with a molecular weight of approximately 45.1 kDa . It has nine transmembrane domains, with the active site containing a histidine residue at the 460th position .
ACAT1 is a mitochondrially localized enzyme that catalyzes the reversible formation of acetoacetyl-CoA from two molecules of acetyl-CoA . This reaction is a critical step in the ketone body metabolism and cholesterol biosynthesis pathways . The enzyme is unique in its ability to use 2-methyl-branched acetoacetyl-CoA as a substrate, making it a distinct thiolase .
The enzyme’s activity is regulated by potassium ions, which bind near the CoA binding site and the catalytic site, causing a structural change in the active site loop . This regulation is essential for the enzyme’s function in various metabolic processes.
Mutations in the ACAT1 gene are associated with 3-ketothiolase deficiency, an inborn error of isoleucine catabolism . This condition is characterized by the urinary excretion of 2-methyl-3-hydroxybutyric acid, 2-methylacetoacetic acid, tiglylglycine, and butanone . Patients with this deficiency may present with metabolic acidosis, developmental delay, and other clinical symptoms.
Recombinant human ACAT1 is produced using various expression systems to study its structure, function, and potential therapeutic applications . The recombinant protein is often tagged with histidine to facilitate purification and characterization . This allows researchers to investigate the enzyme’s role in metabolic pathways and its potential as a target for therapeutic interventions.
