Abcam, ab315213, Anti-Homocitrate Synthase antibody [31F5]

Size: 100µL
Mouse Monoclonal Homocitrate Synthase antibody.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:31F5,
Isotype:IgG1,
Carrier free:No,
Reacts with:Saccharomyces cerevisiae

Properties and Storage Information:
Form-Liquid, Storage buffer-pH: 7 - 8Preservative: 0.03% Sodium azideConstituents: PBS, 50% Glycerol (glycerin, glycerine), Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Homocitrate Synthase also known as homocitrate synthase enzyme or Lys20 is involved in lysine biosynthesis. It catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate an initial step in the lysine biosynthesis pathway. The enzyme has a mass of approximately 44 kDa. Homocitrate synthase is expressed in various organisms including bacteria fungi and plants. It typically localizes in the mitochondrial matrix in eukaryotic cells where it performs its enzymatic function.
Biological function summary
The enzyme plays a pivotal role in the synthesis of lysine an essential amino acid. Lysine is used by cells for protein synthesis and other metabolic functions. Homocitrate synthase functions as part of the alpha-aminoadipate pathway where it forms a complex or acts sequentially with other enzymes to ensure proper lysine production. This enzyme is essential for maintaining adequate lysine levels within organisms that cannot synthesize lysine through other pathways.
Pathways
Homocitrate synthase occupies a central position within the alpha-aminoadipate pathway of lysine biosynthesis. This metabolic pathway leads to the conversion of homocitrate to alpha-ketoadipate eventually resulting in lysine production. The pathway is interconnected with other metabolic processes such as the tricarboxylic acid (TCA) cycle. Related proteins in these pathways include additional enzymes such as saccharopine dehydrogenase and homoisocitrate dehydrogenase which continue the transformation of substrates downstream from homocitrate.
Defects in lysine biosynthesis do not impact human health directly because humans do not produce lysine endogenously. However plant and microbial homocitrate synthase affect agricultural industries. Pathogens with altered lysine biosynthesis pose risks to plants by challenging normal cellular functions in crops. Furthermore antibiotics target pathways similar to those involving homocitrate synthase in pathogens to inhibit bacterial growth. Targeted inhibition affects proteins like dihydrodipicolinate synthase which cooperates in lysine biosynthesis offering avenues for controlling pathogen proliferation.