Enzyme
Complement factor I is a serine protease that downregulates complement activity in the fluid phase and/or on cell surfaces in conjunction with one of its cofactors, factor H (FH), complement receptor 1 (CR1/CD35), C4 binding protein (C4BP) or membrane cofactor protein (MCP/CD46).
Protein-arginine deiminase is a unique family of enzymes that catalyzes the hydrolysis of peptidyl-arginine to form peptidyl-citrulline.
L-Lysine α-oxidase is a potent anticancer agent. L-Lysine α-oxidase also a L-amino acid oxidase, deaminates L-lysine with the yield of H2O2, ammonia, and α-keto-ε-aminocaproate. L-Lysine α-oxidase shows cytotoxicity and anticancer activity.
Polymyxin deacylase (Polymyxin acylase) is an N-myristoyl lyase. Polymyxin deacylase can deacylate polymyxin antibiotics and long-chain fatty acyl groups of proteins and peptides. Polymyxin deacylase exhibits antitumor activity against oral epithelial cancer cells. Polymyxin deacylase can be used in research on oral epithelial cancer and other cancers.
Phenylalanine ammonia-lyase is a non-mammalian enzyme converting phenylalanine into trans-cinnamic acid and ammonia. Phenylalanine ammonia-lyase can be used in the research of phenylketonuria.
DNA polymerase is a polymerase agent targeting DNA templates. DNA polymerase catalyzes the polymerization of deoxyribonucleotides (dNTPs) to extend DNA strands with high fidelity and processivity. DNA polymerase is promising for research of cancers.
Peptidylprolyl isomerase is an enzyme that catalyzes the cis-trans isomerization of peptidylprolyl amino groups. Peptidylprolyl isomerase may be involved in cellulase modification. Peptidylprolyl isomerase also functions as a chaperone protein.
Aeromonas proteolytica aminopeptidase is an aminopeptidase from Aeromonas proteolytica. Aeromonas proteolytica aminopeptidase can function as an esterase. Aeromonas proteolytica aminopeptidase can catalyze the hydrolysis of L-leucine ethyl ester (L-Leu-OEt) with a Km of 700 µM.
Protein disulfide isomerase is a prototypic thiol isomerase that catalyzes the formation and cleavage of thiol-disulfide bonds during protein folding in the endoplasmic reticulum (ER). Protein disulfide isomerase can be used for the study of cardiovascular diseases.
Formamidopyrimidine-DNA glycosylase is a selective DNA repair enzyme. Formamidopyrimidine-DNA glycosylase is promising for research of DNA damage repair and the and oxidative stress-related diseases (e.g., cancer, neurodegenerative diseases).
Thymidine phosphorylase is a nucleoside metabolism enzyme that plays an important role in the pyrimidine salvage pathway. Thymidine phosphorylase catalyzes the conversion of thymidine to thymine and 2-deoxy-α-D-ribose-1-phosphate (dRib-1-P). Thymidine phosphorylase plays an important role in platelet activation in vitro and thrombosis in vivo by participating in multiple signaling pathways. Thymidine phosphorylase can be used for the study of myocardial infarction, stroke, pulmonary embolism and cancer.
Fumarase catalyses the conversion of l-malic acid to fumaric acid. Fumarase participates in the tricarboxylic acid cycle in mitochondria. Fumarase participates in the cellular response to DNA double strand breaks.
Ribose-5-phosphate isomerase (Phosphoriboisomerase) exists widely in microorganisms, animals and plants. It is the first enzyme in the non-oxidative phase of the pentose phosphate pathway (PPP) and also a key enzyme in the Calvin cycle (photosynthetic carbon fixation). Ribose-5-phosphate isomerase catalyzes the reversible isomerization between D-ribulose-5-phosphate (Ru5P) and D-ribose-5-phosphate (R5P). Ribose-5-phosphate isomerase acts as a multifunctional biocatalyst for rare sugar production. Ribose-5-phosphate isomerase serves as a target for antitrypanosomal agents.
Thioglucosidase is a S-glycosidic bond hydrolase. Thioglucosidase is promising for research of plant defense metabolites (e.g., glucosinolates).
Phosphatidylinositol phosphodiesterase hydrolyzes phosphatidylinositol to diacylglycerols and a mixture of myoinositol 1- and 1, 2-cyclic phosphates.
Oxaloacetate decarboxylase catalyzes the irreversible decarboxylation of oxaloacetate to pyruvate and COIC2. Oxaloacetate decarboxylase is a member of the sodium ion transport decarboxylase (NaT-DC) enzyme family. Oxaloacetate decarboxylase converts the chemical energy of the decarboxylation reaction into an electrochemical gradient of Na+ ions across the membrane.
