HMGCL Human, Sf9
Sf9, Baculovirus cells.
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase, 3-Hydroxymethyl-3-Methylglutaryl-Coenzyme A Lyase, 3-Hydroxy-3-Methylglutarate-CoA Lyase, Hydroxymethylglutaricaciduria, HMG-CoA Lyase, EC 4.1.3.4, HL, Mitochondrial 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA Lyase, Mitochondrial, 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA lyase, mitochondrial, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase.
Greater than 90.0% as determined by SDS-PAGE.
Description
HMGCL Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 305 amino acids (28-325 a.a.) and having a molecular mass of 32.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). HMGCL is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase, 3-Hydroxymethyl-3-Methylglutaryl-Coenzyme A Lyase, 3-Hydroxy-3-Methylglutarate-CoA Lyase, Hydroxymethylglutaricaciduria, HMG-CoA Lyase, EC 4.1.3.4, HL, Mitochondrial 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA Lyase, Mitochondrial, 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA lyase, mitochondrial, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase.
Sf9, Baculovirus cells.
MTLPKRVKIV EVGPRDGLQN EKNIVSTPVK IKLIDMLSEA GLSVIETTSF VSPKWVPQMG DHTEVLKGIQ KFPGINYPVL TPNLKGFEAA VAAGAKEVVI FGAASELFTK KNINCSIEES FQRFDAILKA AQSANISVRG YVSCALGCPY EGKISPAKVA EVTKKFYSMG CYEISLGDTI GVGTPGIMKD MLSAVMQEVP LAALAVHCHD TYGQALANTL MALQMGVSVV DSSVAGLGGC PYAQGASGNL ATEDLVYMLE GLGIHTGVNL QKLLEAGNFI CQALNRKTSS KVAQATCKLH HHHHH.
Product Science Overview
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase, commonly referred to as HMG-CoA lyase, is a crucial enzyme in human metabolism. This enzyme is encoded by the HMGCL gene located on chromosome 1 . It plays a significant role in ketogenesis, the process by which ketone bodies are produced, and in the catabolism of the amino acid leucine .
HMG-CoA lyase is a mitochondrial enzyme that catalyzes the cleavage of (S)-3-hydroxy-3-methylglutaryl-CoA into acetyl-CoA and acetoacetate . This reaction is essential for the production of ketone bodies, which serve as an alternative energy source to glucose, especially during periods of fasting or strenuous exercise . The enzyme requires a divalent metal ion as a co-factor for its activity .
The HMGCL gene encodes a 34.5-kDa protein that is localized to the mitochondrion and peroxisome . Multiple isoforms of the protein exist due to alternative splicing, with the major isoform being highly expressed in the liver . The structure of HMG-CoA lyase has been resolved by X-ray crystallography, revealing that the protein functions as a dimer . The active site of the enzyme involves substrate binding across a cavity located at the C-terminal end of a beta-barrel structure .
The recombinant form of HMG-CoA lyase, expressed in Sf9 cells, is used for various research and therapeutic purposes. Sf9 cells, derived from the fall armyworm Spodoptera frugiperda, are commonly used in biotechnology for the production of recombinant proteins. These cells are particularly advantageous for expressing human proteins due to their ability to perform post-translational modifications similar to those in mammalian cells.
Mutations in the HMGCL gene can lead to HMG-CoA lyase deficiency, a rare metabolic disorder characterized by hypoketotic hypoglycemia and metabolic acidosis . This condition results from the inability to properly break down leucine and produce ketone bodies, leading to an accumulation of organic acids in the body . Early diagnosis and management are crucial for preventing severe metabolic crises in affected individuals.
