Enzymes in Recombinant Proteins

<p>Lyticase is a lysing enzyme that is designed to lyse cells in a biological sample. It contains an optimized wild-type guanine nucleotide-binding protein and has been shown to have high enzyme activities. Lyticase has also been shown to be active against opportunistic fungal strains, such as Candida glabrata, by disrupting their cell membranes. Lyticase is classified as a signal peptide with nuclear DNA, which allows it to be used in wastewater treatment applications. The enzyme can also be used for the analysis of the Toll-like receptor (TLR) response of microbes due to its electrochemical impedance spectroscopy properties.</p>

<p>Protease enzymes break down proteins and are essential for many biological processes, including digestion, cellular regulation and blood clotting. They are also used in many industrial and biotechnological applications for example in food processing and in detergents.</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>DNase I (Deoxyribonuclease I, EC 3.1.21.1) is an endonuclease that cleaves DNA, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3'. On average it produces tetranucleotides. One unit of the DNase I will increase the absorbance of 260nm light at a rate of 0.001/minute in 1 ml reaction volume at 25°C.</p>

<p>Carboxypeptidase Y (EC 3.4.16.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues and it remains active in the presence of urea at low to moderate concentrations. One unit of the Carboxypeptidase Y will hydrolyze 1.0 μmole of a chromogenic peptide substrate, releasing C-terminal alanine and generating a light-absorbing product.</p>

<p>Butyrylcholinesterase is an enzyme made in the liver and found mainly in blood plasma. Butyrylcholinesterase (EC 3.1.1.8), also known as BChE or BuChE, is a nonspecific cholinesterase enzyme that hydrolyses choline-based esters. One unit of Butyrylcholinesterase will hydrolyze 1.0 μmole of butyrylcholine to choline and butyrate per minute at pH 8.0 and 37 °C.</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>Superoxide dismutase is an enzyme that catalyzes the conversion of harmful superoxide into hydrogen peroxide and oxygen.</p>

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

<p>Proteinase K is used for the general digestion of proteins and removal of protein contamination in nucleic acids. Addition of Protease K also stabilizes nucleic acids by degrading any nucleases present. Proteinase K is active in wide range of pH range, in the presence of SDS, urea and Guanidinium chloride at low to moderate concentrations. Proteinase K is also known under names of protease K and endopeptidase K.</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.

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

<p>Endoproteinase Glu-C (Glutamyl endopeptidase, V8 protease, GluV8, EC 3.4.21.19) is a protease that hydrolyzes peptide bonds at the carboxylic side of either exclusively Glu, or Glu and Asp residues, depending on the buffer conditions. One unit of endoproteinase Glu-C will generate 1.0 μmole of p-nitroaniline from Z-Phe-Leu-Glu-pNA peptide mimic substrate per minute at pH 7.8 and 25 °C. Z-Phe-Leu-Glu-pNA substrate is available here.molecular weight ~ 27000.</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>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>Phosphodiesterase II from bovine spleen is an enzyme derived from the spleen of cattle, which serves as a crucial biological catalyst for the hydrolysis of phosphodiester bonds in nucleotide sequences. This enzyme's mode of action involves cleaving the phosphodiester linkages within nucleic acids, facilitating the breakdown of these macromolecules into smaller nucleotide units.</p>

<p>Glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the following reaction:  glycerol-3-phosphate + O2 ⇌ dihydroxyacetone phosphate + H2O2  One unit of Glycerol-3-phosphate oxidase will generate 1.0 μmole H2O2 per min at 37°C, under the presence of O2 and the optimal pH. If required, you can remove the build-up of hydrogen peroxide using catalase.</p>

Thioredoxin reductase (TR, TrxR) (EC 1.8.1.9) is an enzyme that reduce thioredoxin using NADPH as a co-factor, and also contains FAD. One unit of thioredoxin reductase will raise increase light absorbance by 1.0 per minute at 412nm in the presence of thioredoxin and Ellman's reagent at pH 7.0 and 25 °C.

<p>Glycerokinase (glycerol kinase, GP, ATP-glycerol 3-phosphotransferase; EC 2.7.1.30) is an enzyme that catalyzes the following reaction:  ATP + glycerol ⇌ ADP + glycerol 3-phosphate  One unit of Glycerokinase will convert 1.0 μmole of glycerol and ATP to glycerol 3-phosphate and ADP per min at pH 9.8 and 25 °C.</p>