Search results

Urokinase (UK) is a serine protease, which is one of biological plasminogen activators.
It is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing.
It can be obtained from human urine or kidney cell culture.

Matrix Metallopeptidase 23B (MMP23B) belongs to the matrix metalloproteinase (MMP) family, and it is section of a duplicated region of chromosome 1p36.3. MMP23B is a protease. MMP23B regulates the surface expression of some potassium channels by holding them in the endoplasmic reticulum. Members of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis.

Thiosulfate sulfurtransferase (glpE) is a mitochondrial matrix enzyme which is encoded by the nucleus. Escherichia coli glpE is a prototype for the single-domain rhodanese superfamily. glpE catalyzes the sulfur-transfer reaction in which a sulfur atom is transferred from thiosulfate to cyanide by a double-displacement mechanism.

ACADM enzyme is essential for the degradation a certain group of fats called medium-chain fatty acids. ACADM is essential for converting specific fatty acids to energy, mainly during fasting periods. ACADM functions in mitochondria, the energy-producing centers within cells. ACADM is localized in the mitochondria of numerous tissue types, predominantly the liver.

Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

Beta-Glucocerebrosidase, also known as GBA is amember of the glycosyl hydrolase 30 family. GBA is a lysosomal enzyme which requires a signal peptide for transport across the membrane of the rough endoplasmic reticulum as well as glycosylation for transport into lysosomes. Furthermore, Gaucher disease is caused by a deficiency in the activity of the enzyme glucocerebrosidase.

Acyl-coenzyme A thioesterase 13 (ACOT13) belongs to the thioesterase subfamily of esterase family. ACOT13 is highly expressed in the kidney with moderate expression in the brain, liver and intestines. ACOT13 contains a hotdog-fold and is thought to co-localize with microtubules, possibly having a role in cellular proliferation events. Deletion of a segment of the q arm of chromosome 6 is linked to early onset intestinal cancer, suggesting the presence of a cancer susceptibility locus.

Inorganic pyrophosphatase (ppa) is a member of the Ppase family. PPA is an enzyme which catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Since this is a highly exergonic reaction, it can therefore be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The role of the PPA enzyme is a critical one in the lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, DNA synthesis, as well as other biochemical transformations.

Phosphotransacetylase (PTA) is a metabolic enzyme (EC 2.3.1.8) that catalyzes the reversible conversion: acetyl-CoA + Pi ⇄ acetyl-phosphate + CoA. The reversible reaction of acetyl-CoA to acetate node and back, is useful in R&D and biotech assays such as Metabolic engineering, Synthetic biology, Production of biopolymers, Enzymatic synthesis of acetyl-phosphate, bacterial signaling
and Fermentation.  Phosphotransacetylase controls acetate formation and manipulates acetyl-CoA flux thus is widely used in protein expression, metabolic engineering, and synthetic pathways.

Scavenger mRNA-decapping enzyme (DCPS) is a member of the HIT family. DCPS is required for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It was shown that DCPS hydrolyzes the residual m7GpppN cap structure after the complete 3'–5' degradation of the mRNA by the exosome. Furthermore, DCPS releases m7GMP and is incapable of cleaving cap structures attached to a long RNA chain.

IMP2 Inner Mitochondrial Membrane Peptidase-Like (IMMP2L) is implicated in processing the signal peptide sequences, IMMP2L is used to direct mitochondrial proteins to the mitochondria. IMMP2L resides in the mitochondria and is one of the essential proteins for the catalytic activity of the mitochondrial inner membrane peptidase (IMP) complex. Two variants which encode the same protein have been found for IMMP2L.

Chitinase is a digestive enzyme which breaks down glycosidic bonds in chitin. Due to chitin being a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are usually found in organisms that either need to remake their own chitin or to dissolve and digest the chitin of fungi or animals. Chitinivorous organisms include many bacteria genuses such as Aeromonas, Bacillus, Vibrio, among others, which may be pathogenic or detritivorous. Chitinase expression is mediated by the NPR1 gene and the salicylic acid pathway, both of which are involved in resisting fungal and insect attack. Human chitinases appear in gastric juices. They are likely to be digestive chitinases, for catabolic activity. Chitinase activity is identified systemically in humans, in the blood, and possibly cartilage. Chitinase has been related to allergies, asthma in particular has been linked to enhanced chitinase expression levels, also dust mites and mold spores which are both chitin covered.

Amine Oxidase Copper Containing 3 , also referred to AOC3, a copper amine oxidase with a topaquinone cofactor.
AOC3 is a cell adhesion protein which participates in recirculation & extravasation of lymphocyte by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin independent fashion.
Amine Oxidase Copper Containing 3 acts in adipogenesis.
The protein catalyzes the oxidative deamination of small primary amines such as methylamine, benzylamine & aminoacetone in a reaction that produces an aldehyde, ammonia and H2O2.

ENO3 is one of three enolase isoenzymes in mammals. The homodimer ENO3 is located in skeletal muscle cells of adults and has a part in converting phosphoglyceric acid to phosphenolpyruvic acid in the glycolytic pathway. Mutations in ENO3 gene is linked to metabolic myopathies which is caused by low stability of the enzyme.

CBR1 is one of numerous monomeric, NADPH-dependent oxidoreductases having ubiquistly specificity for carbonyl compounds. CBR1 is broadly distributed in human tissues. CBR1 metabolizes toxic environmental quinones and pharmacological relevant substrates. CBR1 converts prostaglandin E2 to prostaglandin F2-alpha.

Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member of a new family of zinc-binding enzymes.

Arylsulfatase A (ARSA) hydrolyzes cerebrosidesulfate to cerebroside and sulfate. ARSA is inhibited by phosphate. The phosphate develops a covalent bond with the active site 3-oxoalanine. ARSA gene defects cause metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in various neurological symptoms and ultimately death.

Ribonuclease 7 (RNASE7) is one of the final RNase A superfamily ribonucleases. RNASE7 was isolated from skin-derived stratum corneum. RNASE7 protein demonstrated potent ribonuclease activity and hence may contribute to the well-known ribonuclease activity of human skin. RNASE7 has revealed a broad spectrum antimicrobial activity against many pathogenic microorganisms and extraordinarily potent activity.

Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso- PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.

PLA2G7 is a secreted enzyme which catalyzes the degradation of platelet-activating factor to biologically inactive products. The PLA2G7 enzyme is produced by inflammatory cells and hydrolyzes oxidised phospholipids in LDL. In the blood, PLA2G7 goes mainly with LDL and less than 20% is coupled with HDL.
PLA2G7 is implicated in the development of atherosclerosis and is also a marker for cardiac disease. PLA2G7 might have a major physiologic effect in the presence of inflammatory bodily responses.
PLA2G7 alters the action of PAF (platelet-activating factor) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. PLA2G7 has specificity for substrates with a short residue at the sn-2 position. PLA2G7 is inactive against long-chain phospholipids.
PLA2G7 gene defects are the source of platelet-activating factor acetylhydrolase deficiency, which is a trait that is present in 27% of the Japanese population.

Acetyl-COA Acyltransferase 2, (ACAA2) is a member of the thiolase family. ACAA2 catalyzes the final step of the mitochondrial fatty acid beta-oxidation spiral. Not like most mitochondrial matrix proteins, ACAA2 contains a non-cleavable amino-terminal targeting signal.

Dopa decarboxylase is a homodimeric, pyridoxal phosphate dependent enzyme.
Dopa decarboxylase is involved in 2 metabolic pathways, synthesizing 2 significant neurotransmitters the take part in numerous clinical disorders, including Parkinson’s disease. Dopa decarboxylase is located in different areas of the brain and is mostly found in basal ganglia. Dopa decarboxylase catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopa, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine. Defects in Dopa decarboxylase leads to aromatic L-amino-acid decarboxylase deficiency (AADCD). AADCD deficiency is an inborn error in neurotransmitter metabolism that causes combined serotonin and catecholamine deficiency.

Formylglutathione hydrolase (Esterase D) is a member of the esterase D family. Esterase D is a serine hydrolase involved in the detoxification of formaldehyde. Esterase D is active toward various substrates including O-acetylated sialic acids, and it may possibly be involved in the recycling of sialic acids. Esterase D is used as a genetic marker for retinoblastoma and Wilson's disease.