AAT Bioquest offers a comprehensive selection of substrates and assay kits for measuring the activity of diverse hydrolysis enzymes beyond the common phosphatase, protease, and nuclease categories. This collection includes reagents for detecting ATPases, GTPases, cholinesterases, lactamases, neuraminidases, and sphingomyelinases. The Amplite® and PhosphoWorks™ assay platforms provide optimized, ready-to-use kits with enhanced sensitivity for both fluorimetric and colorimetric detection, while individual fluorogenic and chromogenic substrates offer flexibility for custom assay development.

ATPases and GTPases are phosphoanhydride hydrolases that catalyze ATP or GTP hydrolysis, releasing inorganic phosphate (Pi) or pyrophosphate (PPi) as reaction products. These enzymes are involved in critical cellular processes including active transport, signal transduction, cytoskeletal dynamics, and protein synthesis. Monitoring phosphate or pyrophosphate release provides a direct, universal method for measuring ATPase and GTPase activity without the need for specialized substrates.

Cholinesterases are critical enzymes in neurotransmission that hydrolyze acetylcholine to terminate synaptic signaling. Acetylcholinesterase (AChE) is predominantly found at neuromuscular junctions and in the brain, while butyrylcholinesterase (BChE) is synthesized in the liver and circulates in plasma. These enzymes are important targets for Alzheimer's disease therapeutics and are inhibited by organophosphate pesticides and nerve agents, making activity assays essential for drug development and toxicology studies.

Beta-lactamases are bacterial enzymes that hydrolyze the beta-lactam ring found in penicillin, cephalosporin, and carbapenem antibiotics, representing a major mechanism of antibiotic resistance. Detecting beta-lactamase activity and screening for inhibitors are critical for antibiotic resistance research and drug development programs. Our optimized kits support both direct activity measurement and high-throughput inhibitor screening applications.

Neuraminidases (sialidases) cleave terminal sialic acid residues from glycoproteins, glycolipids, and oligosaccharides. These enzymes play important roles in viral infection (influenza neuraminidase), bacterial pathogenesis, and mammalian lysosomal function. Neuraminidase inhibitors such as oseltamivir (Tamiflu) are important antiviral therapeutics, making neuraminidase activity assays valuable for drug discovery and viral research.

Sphingomyelinases (SMases) cleave sphingomyelin to produce ceramide and phosphocholine. Different isoforms are classified by pH optima (acidic, neutral) and cation dependence. These enzymes are implicated in membrane signaling, apoptosis, and various disease states including Niemann-Pick disease. Sphingomyelinase activity assays are important tools for studying lipid metabolism and sphingolipid signaling pathways.