Enzyme

<p>Glucosidases are enzymes belonging to the family of oxidoreductases. They catalyse the hydrolysis of starches to simple sugars. Glucosidase is widely used in the food, carbohydrate and biofuels industries. In recent years, its applicability has expanded to biotechnology for its potential application in bioenzymatic fuel cells.</p>

<p>Tyrosinase-IN-2, a potent tyrosinase inhibitor, may help in skin lightening and food preservation research.</p>

<p>Maltose phosphorylase (systematic name maltose:phosphate 1-beta-D-glucosyltransferase; EC 2.4.1.8) is an enzyme that catalyzes the following reaction:  maltose + Pi ⇌ D-glucose + beta-D-glucose 1-phosphate  One unit of maltose phosphorylase will produce 1.0 μmole of D-Glucose from maltose per minute at pH 7.0 and 30°C.</p>

<p>Choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the following reaction: choline + O2 + H20 ⇌ betaine aldehyde + H2O2One unit of choline oxidase will form 1 μmole of H2O2 by oxidizing choline to betaine aldehyde per min at pH 8.0 and 37 °C. You can remove the build-up of hydrogen peroxide using catalase.</p>

<p>Glucose Dehydrogenase is an enzyme, which is typically derived from microbial sources such as bacteria and fungi. It functions by catalyzing the oxidation of glucose to gluconolactone, concurrently reducing a cofactor such as NAD⁺ or PQQ. This biochemical reaction is critical in various analytical applications due to its specificity and efficiency in glucose detection.Glucose Dehydrogenase is widely employed in the development of biosensors and diagnostic assays. Its primary application is in blood glucose monitoring devices, where its ability to accurately quantify glucose levels is crucial for managing diabetes. Additionally, it is utilized in research and development settings for biochemical assays that require precise glucose measurements. The enzyme's rapid and specific action on glucose molecules makes it an indispensable tool in both clinical and laboratory environments, contributing to advancements in biosensing technologies and metabolic studies.</p>

<p>Lysozyme is a bacteriolytic enzyme, which is primarily derived from hen egg whites. It functions by hydrolyzing the β-1,4-glycosidic linkages in the peptidoglycan layer of bacterial cell walls, particularly in Gram-positive bacteria. This enzymatic activity results in the lysis and subsequent death of the bacterial cells, providing a potent antimicrobial effect.</p>

<p>From pigeon breast muscle - Carnitine acetyltransferase (EC 2.3.1.7, also Carnitine O-acetyltransferase) is an enzyme that catalyzes the following chemical reaction: acetyl-CoA + carnitine ⇌ CoA + acetylcarnitine</p>

<p>Invertase is an enzyme that catalyzes the hydrolysis of sucrose to glucose and fructose and can be found in plants and microorganisms</p>

<p>hCAII-IN-9 inhibits hCA II/IX/XII with IC50s of 1.18, 0.17, 2.99 μM; not BBB permeable.</p>

<p>Acetylcholinesterase is an enzyme that breaks down acetylcholine</p>

<p>A proteolytic enzyme synthesized by the HIV cell as part of the GagPol polyprotein</p>

<p>Nucleoside phosphorylase (Purine nucleoside phosphorylase, PNP, PNPase, inosine phosphorylase, inosine-guanosine phosphorylase; EC 2.4.2.1) is an enzyme that catalyzes the following reaction:  purine nucleoside + Pi ⇌ purine + alpha-D-ribose 1-phosphate  One unit of nucleoside phosphorylase will phosphorylate 1.0 micromole of inosine to hypoxanthine and alpha-D-ribose 1-phosphate per min at pH 7.4 and 25°C.</p>

<p>hCAI/II-IN-6 is a selective and orally active inhibitor of human carbonic anhydrase (CA).</p>

<p>Cocarboxylase hydrochloride is a coenzyme derivative, which is primarily sourced from thiamine (vitamin B1). It plays a crucial role in biochemical processes by facilitating the enzymatic decarboxylation of alpha-keto acids within the cellular environment. This action is fundamental in energy production as it aids in the conversion of pyruvate to acetyl-CoA, subsequently entering the citric acid cycle. Cocarboxylase hydrochloride’s involvement in carbohydrate metabolism is especially vital for tissues with high metabolic rates, such as the heart and brain.</p>

<p>E. coli recombinant α-2,6 sialyltransferase from Neisseria meningitidis. One unit is defined as the amount of enzyme that catalyses the formation of 1 μmol CMP-Neu5Ac from CTP and Neu5Ac per minute at 37 ºC.Activity: 100U/mg</p>

<p>selectively deamidates gluten peptides, which results in strongly enhanced T cell-stimulatory activity.  It has also been used in a study to improve quantifiable assays to fully characterize the role of transglutaminase in diseases such as Huntington′s disease and Alzheimer′s disease.</p>

<p>75u/mg - Glyceraldehyde 3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12) is an enzyme that catalyzes the following reaction:  glyceraldehyde 3-phosphate + NAD+ + Pi ⇌ glycerate 1,3-bisphosphate + NADH + H+  One unit of GAPDH will convert 1.0 μmole of glyceraldehyde 3-phosphate into glycerate 1,3-bisphosphate per minute at pH 8.5 and 37 °C in the presence of NAD+ and phosphate. NAD+ is available here.</p>

<p>Myokinase (Adenylate kinase, EC 2.7.4.3) catalyzes interconversion between ATP, ADP and AMP by catalyzing the following reaction:ATP + AMP ⇌ 2 ADPOne unit of Myokinase will convert 1.0 µmol ATP and 1.0 µmol AMP to 2.0 µmol ADP per min at 25°C and pH 7.5.</p>

<p>E. coli recombinant sialic acid aldolase (EC 4.1.3.3) from Pasteurella multocida.  One unit is defined as the amount of enzyme that catalyses the formation of 1 umol Neu5Ac from ManNAc and Pyruvate per minute at 37 ℃.Activity: 9U/mg</p>

<p>beta-Galactosidase (EC 3.2.1.23, shortly beta-Gal, also know as lactase) catalyses the hydrolysis of beta-d-galactoside in the presence of water to galactose and alcohol, or lactose into glucose and galactose. beta-Gal has a molecular weight of 540,000 and is composed of four identical subunits of MW 135,000, each with an independent active site. The enzyme has divalent metals as cofactors, with chelated Mg2+ ions required to maintain active site conformation. The molecule contains numerous sulfhydryl groups and is glycosylated.</p>