2. Metabolic Disease

Metabolic Disease

Metabolic Disease

Related Products

PDF 53.7 MB

Metabolic diseases is defined by a constellation of interconnected physiological, biochemical, clinical, and metabolic factors that directly increases the risk of cardiovascular disease, type 2 diabetes mellitus, and all cause mortality. Associated conditions include hyperuricemia, fatty liver (especially in concurrent obesity) progressing to nonalcoholic fatty liver disease, polycystic ovarian syndrome (in women), erectile dysfunction (in men), and acanthosis nigricans. Metabolic disease modeling is an essential component of biomedical research and a mandatory prerequisite for the treatment of human disease. Somatic genome editing using CRISPR/Cas9 might be used to establish novel metabolic disease models.

Cat. No. Product Name CAS No. Purity Chemical Structure
  • HY-E70898A
    Trehalose-6-phosphate hydrolase, Bacillus subtilis
    Trehalose-6-phosphate hydrolase, Bacillus subtilis (EC 3.2.1.93), belongs to the hydrolase family and is a glycosidase that hydrolyzes O- and S-glycoside compounds. Trehalose-6-phosphate hydrolase participates in the metabolism of starch and sucrose. Its substrates are α,α'-trehalose-6-phosphate and water, and its products are D-glucose and D-glucose-6-phosphate.
    Trehalose-6-phosphate hydrolase, Bacillus subtilis
  • HY-E70898C
    Topoisomerase IV, E. coli
    Topoisomerase IV, E. coli (EC 5.99.1.) is prepared by overexpressing the parC and parE subunits in E. coli. Topoisomerase IV is supplied as a heterotetramer complex in Dilution buffer.
    Topoisomerase IV, E. coli
  • HY-E70899A
    Topoisomerase IV, Staphylococcus aureus
    Topoisomerase IV, Staphylococcus aureus (EC 5.99.1.) is prepared by overexpressing the subunits in E.coli.
    Topoisomerase IV, Staphylococcus aureus
  • HY-E70899B
    Topoisomerase IV, Pseudomonas aeruginosa
    Topoisomerase IV, Pseudomonas aeruginosa (EC 5.99.1.) is prepared by overexpressing the subunits in E. coli. Topoisomerase IV is supplied as a heterotetramer complex in Dilution buffer.
    Topoisomerase IV, Pseudomonas aeruginosa
  • HY-E70913A
    Phosphotransacetylase, Bacillus stearothermophilus 98%
    Phosphotransacetylase, Bacillus stearothermophilus (EC 2.3.1.8) converts coenzyme A to acetyl-CoA. Phosphotransacetylase, Bacillus stearothermophilus (EC 2.3.1.8) belongs to the transtransferase family and participates in three metabolic pathways: taurine and linolenic acid metabolism, pyruvate metabolism, and propionic acid metabolism.
    Phosphotransacetylase, Bacillus stearothermophilus
  • HY-E70913B
    Phosphotransacetylase, Leuconostoc mesenteroides
    Phosphotransacetylase, Leuconostoc mesenteroides (EC 2.3.1.8) converts coenzyme A to acetyl-CoA. Phosphotransacetylase, Leuconostoc mesenteroides (EC 2.3.1.8) belongs to the transtransferase family and participates in three metabolic pathways: taurine and linolenic acid metabolism, pyruvate metabolism, and propionic acid metabolism.
    Phosphotransacetylase, Leuconostoc mesenteroides
  • HY-E70919A
    Nitrile hydratase, Rhodopseudomonas palustris
    Nitrile hydratase, Rhodopseudomonas palustris (EC 4.2.1.84) is a mononuclear iron or non-corrinoid cobalt enzyme that catalyse the hydration of diverse nitriles to their corresponding amides.
    Nitrile hydratase, Rhodopseudomonas palustris
  • HY-E70919B
    Nitrile hydratase, Rhodococcus erythropolis
    Nitrile hydratase, Rhodococcus erythropolis (EC 4.2.1.84) is a mononuclear iron or non-corrinoid cobalt enzyme that catalyse the hydration of diverse nitriles to their corresponding amides.
    Nitrile hydratase, Rhodococcus erythropolis
  • HY-E70930A
    Pyroglutamate Aminopeptidase, Pyrococcus furiosus
    Pyroglutamate Aminopeptidase, Pyrococcus furiosus (EC 3.4.19.3), is an enzyme capable of digesting proteins. Pyroglutamate Aminopeptidase specifically acts on the N-terminal pyroglutamic acid, cleaving it from proteins and peptide chains, thereby promoting Edman degradation.
    Pyroglutamate Aminopeptidase, Pyrococcus furiosus
  • HY-E70933A
    Protease, Rhizopus sp.
    Protease, Rhizopus sp. is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain.
    Protease, Rhizopus sp.
  • HY-E70936A
    Glycerokinase, Bacillus stearothermophilus
    Glycerokinase, Bacillus stearothermophilus (EC 2.7.1.30) is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. Glycerokinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol.
    Glycerokinase, Bacillus stearothermophilus
  • HY-E70936B
    Glycerokinase, Cellulomonas sp.
    Glycerokinase, Cellulomonas sp. (EC 2.7.1.30) is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. Glycerokinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol.
    Glycerokinase, Cellulomonas sp.
  • HY-E70936C
    Glycerokinase, Escherichia coli
    Glycerokinase, Escherichia coli (EC 2.7.1.30) is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. Glycerokinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol.
    Glycerokinase, Escherichia coli
  • HY-E70940A
    Sphingomyelinase, Streptomyces sp.
    Sphingomyelinase, Streptomyces sp. (EC 3.1.4.12) is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. Sphingomyelinase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide.
    Sphingomyelinase, Streptomyces sp.
  • HY-E70940B
    Sphingomyelinase, Bacillus cereus 98%
    Sphingomyelinase, Bacillus cereus (EC 3.1.4.12) is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. Sphingomyelinase, Bacillus cereus (EC 3.1.4.12) is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide.
    Sphingomyelinase, Bacillus cereus
  • HY-E70960A
    L-Glutamic Dehydrogenase (NADP), Candida utilis
    L-Glutamic Dehydrogenase (NADP), Candida utilis (EC 1.4.1.4) catalyzes the conversion of glutamate to α-ketoglutarate.
    L-Glutamic Dehydrogenase (NADP), Candida utilis
  • HY-E70961A
    γ-Glutamyltranspeptidase, Equine
    γ-Glutamyltranspeptidase, Equine (EC 2.3.2.2) is an enzyme capable of transferring the γ-glutamyl functional group. γ-Glutamyltranspeptidase, Equine (EC 2.3.2.2) catalyzes the transfer of the γ-glutamyl group of glutathione to a receptor, which can be an amino acid, peptide, or water (to produce glutamate).
    γ-Glutamyltranspeptidase, Equine
  • HY-E70963A
    L-Lactic Dehydrogenase, Chicken
    L-Lactic Dehydrogenase, Chicken (EC 1.1.1.27) is used for research on lactic acid metabolism and enzymatic mechanisms.
    L-Lactic Dehydrogenase, Chicken
  • HY-E70964A
    Leucine Aminopeptidase, Porcine
    Leucine Aminopeptidase, Porcine (EC 3.4.11.1) is a proteolytic enzyme which hydrolyzes the peptide bond adjacent to a free amino group. Leucine Aminopeptidase, Porcine (EC 3.4.11.1) rapidly catalyzes the hydrolysis of leucine containing peptides and also catalyzes the hydrolytic release of other amino acids located at the N-terminal end of various peptides and proteins.
    Leucine Aminopeptidase, Porcine
  • HY-E70989A
    D-Fructose Dehydrogenase, Gluconobacter sp.
    D-Fructose Dehydrogenase, Gluconobacter industrius (EC 1.1.99.11) is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius) .D-Fructose Dehydrogenase consists of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. D-Fructose Dehydrogenase is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively.
    D-Fructose Dehydrogenase, Gluconobacter sp.
Cat. No. Product Name / Synonyms Application Reactivity