You searched for: Enzymes

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Peptidyl-prolyl cis-trans isomerase FKBP2(FKBP2 for short), also named 13 kDa FK506-binding protein, FK506-binding protein 2, Immunophilin FKBP13, Rotamase, is a endoplasmic reticulum peripheral membrane protein. It contains 1 PPIase FKBP-type domain and belongs to the FKBP-type PPIase family, FKBP2 subfamily which takes part in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP2 is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. FKBP2 functions as an ER chaperone and as a component of membrane cytoskeletal scaffolds.

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Sialate O-Acetylesterase (SIAE) belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. SIAE is widely expressed with high expression levels in the testis, prostate, and colon. SIAE catalyses N-acetyl-O-acetylneuraminate and H2O to N-acetylneuraminate and acetate. SIAE removes O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid. SIAE down-regulates B lymphocyte antigen receptor signaling (involving CD22), and is required for immunological tolerance. Loss of function mutations in SIAE are much more frequently found in humans with autoimmune diseases especially rheumatoid arthritis and type 1 diabetes.

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Aspartoacylase 3, also known as ACY3, N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming), Acylase III, Aminoacylase-3, Aspartoacylase-2, Aspartoacylase-2, HCV core-binding protein 1 and ASPA2, is a member of the Aspartoacylase subfamily. ACY3 plays an important role in deacetylating mercapturic acids in kidney proximal tubules and acts on N-acetyl-aromatic amino acids.ACY3 is located in the cytoplasm of S2 and S3 proximal tubules and the apical domain of S1 proximal tubules. ACY3 protein is also expressed at low levels in stomach, testis, heart, brain, lung and liver, and may function as an HCV (Hepatitis C virus) core binding protein.

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Peptidyl-Prolyl Cis-Trans Isomerase FKBP7 (FKBP7) is a member of the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. FKBP7 contains two EF-hand domains and one PPIase FKBP-type domain. FKBP7 exhibits PPIase activity and function as molecular chaperones. In addition, FKBP7 accelerates the folding of proteins during protein synthesis. It has been shown that Hsp90 complex to the nucleus bind its PPIase domain to cytoplasmic dynein, the motor protein responsible for retrograde movement along microtubules.

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Hog Acylase (from Kidney)

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Aldo-Keto Reductase Family 1 Member C2 (AKR1C2) plays a role in concert with the 5- alpha/5- beta -Steroid Reductases to convert Steroid hormones into the 3- alpha/5- alpha and 3- alpha/5- beta -Tetrahydrosteroids. AKR1C2 catalyses the inactivation of the most potent androgen 5- alpha-Dihydrotestosterone (5- alpha-DHT) to 5- alpha-Androstane-3- alpha, 17- beta -diol (3- alpha-diol).

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Thimet Oligopeptidase (THOP1) belongs to the peptidase M3 family which includes neurolysin and mitochondrial intermediate peptidase. THOP1 is located in Cytoplasm. THOP1 is widely expressed in human tissues and can detected in different subcellular locations. THOP1 is preferential cleavage for bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues. THOP1 is involved in the metabolism of neuropeptides under 20 amino acid residues and degradation of cytoplasmic peptide. In addition, THOP1 also can degrade the beta-amyloid precursor protein and generate amyloidogenic fragments.

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Carbonic Anhydrase 8 (CA8) belongs to the alpha-carbonic anhydrase family. Alpha-carbonic anhydrase is a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. Because CA8 has some sequence similarity with other known carbonic anhydrase genes, it was firstly called as CA-related protein. Nevertheless, CA8 does not have a carbonic anhydrase catalytic activity. Defects in CA8 are the cause of cerebellar ataxia mental retardation and dysequilibrium syndrome type 3 (CMARQ3), which is a congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and mild mental retardation.

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Inositol Monophosphatase 1 (IMPA1) belongs to the inositol monophosphatase family. IMPA1 is responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides, IMPA1 can use myo-inositol-1,3-diphosphate, myo-inositol-1,4-diphosphate, scyllo-inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2-AMP as substrates. IMPA1 has been implicated as the pharmacological target for lithium action in brain. IMPA1 shows magnesium-dependent phosphatase activity and is inhibited by therapeutic concentrations of lithium. In addition, IMPA1 plays a improtant role in intracellular signal transduction.

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Fig tree Ficin (from Latex)

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Recombinant Human Proprotein Convertase Subtilisin/Kexin Type 9/PCSK9 (D374Y) is a gain of function mutant of human PCSK9 protein. Human PCSK9 is a secretory subtilase belonging to the proteinase K subfamily. PCSK9 is synthesised as a soluble zymogen that undergoes autocatalytic intramolecular processing in the ER, the pro domain and mature chain are secreted together through noncovalent interactions. PCSK9 binds with low-density lipoprotein receptor (LDLR) and it plays a major regulatory role in cholesterol homeostasis. Inhibition of PCSK9 function by preventing PCSK9/LDLR interaction is currently being explored as a means of lowering cholesterol levels. PCSK9 also binds to apolipoprotein receptor 2 (ApoER2), and play a role in the neural development.

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0,25% Trypsin in HBSS (Hank’s Balanced Salt Solution) without calcium and magnesium.

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Brain-Specific Serine Protease 4 (BSSP-4) is a serine protease that preferentially cleaves the synthetic substrate H-D-Leu-Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. BSSP-4 is expressed abundantly in the epithelial cells of the airways, including trachea, esophagus and fetal lung, but scarce in adult lung and expressed at low levels in placenta, pancreas, prostate and thyroid gland. BSSP-4 belongs to the peptidase S1 family and related to trypsin, referentially hydrolyzing substrates after arginine and lysine residues. However, BSSP-4 is less susceptible to inhibition by common trypsin inhibitors such as aprotinin, alpha1-antitrypsin and secretory leukocyte protease inhibitor. BSSP-4 efficiently converts pro-urokinase- type plasminogen activator to its mature, active form.

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PGK1 is called phosphoglycerate kinase that involved in a critical energy-producing process known as glycolysis. Phosphoglycerate kinase helps carry out a chemical reaction that converts a molecule called 1,3-diphosphoglycerate, which is produced during the breakdown of glucose, to another molecule called 3-phosphoglycerate during glycolysis. PGK1 The encoded protein may also act as a cofactor for polymerase alpha.. The protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions.

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Carbonic Anhydrase X (CA10) belongs to CA family of zinc metalloenzymes, which catalyze the reversible hydration of carbon dioxide in various biological processes such as respiration, renal tubular acidification and bone resorption. While CA10 is a secreted protein without Carbonic Anhydrase activity (i.e., the reversible hydration of CO2) due to point mutations in the zinc binding site, it has esterase activity. The human and mouse CA10 are expressed in the brain, indicating that they may play a role in brain development.

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Glycine N-Methyltransferase (GNMT) is a tetrameric cytosolic protein. GNMT catalyses the synthesis of N-methylglycine from glycine using S-adenosylmethionine (AdoMet) as the methyl donor. It can affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine, playing an important role in maintaining normal AdoMet levels. GNMT is highly expressed in liver. As a major folate-binding protein, GNMT takes part in the detoxification pathway. Defects in GNMT are the cause of hypermethioninemia. the patients with this deficiency are mild hepatomegaly and chronic elevation of serum transaminases.

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Carboxypeptidase A2 (CPA) is a secreted pancreatic procarboxy-peptidase that cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan. CPA2 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. Three different forms of human pancreatic procarboxypeptidase A have been isolated, and the A1 and A2 forms are always secreted as monomeric proteins with different biochemical properties. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E, and is involved in zymogen inhibition.

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0,05% Trypsin/0,53 mM EDTA in HBSS (Hank’s Balanced Salt Solution) with sodium bicarbonate, without calcium and magnesium.

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Ubiquinone Biosynthesis Protein COQ7 Homolog (COQ7) is a mitochondrion inner membrane and peripheral membrane protein which belongs to the COQ7 family. It is expressed dominantly in heart and skeletal muscle. COQ7 is synthesised as a preprotein that is imported into the mitochondrial matrix, where the sequence is cleaved off and the mature protein becomes loosely associated with the inner membrane. COQ7 is involved in lifespan determination in ubiquinone-independent manner and also involved in ubiquinone biosynthesis. COQ7 is potential central metabolic regulator. Human COQ7 protein contains 179 amino acids, is mostly helical, and contains an alpha-helical membrane insertion. It has been shown that mutations in the gene are associated with increased life span. Defects of the gene slow down a variety of developmental and physiological processes, including the cell cycle, embryogenesis, post-embryonic growth, rhythmic behaviors and aging.

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Xaa-Pro aminopeptidase 2 (XPNPEP2) belongs to the peptidase M24B family of metalloproteases. Human XPNPEP2 is widely expressed in various tissues, such as kidney, lung, heart, placenta, liver, small intestine and colon. However, it doesn’t express in brain, skeletal muscle, pancreas, spleen, thymus, prostate, testis and ovary. XPNPEP2 is a Homotrimer which binds 2 manganese ions per subunit. The metalloprotease XPNPEP2 may play a role in the inflammatory process and other reactions produced in response to injury or infection and the metabolism of the vasodilator bradykinin.

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Uridinephosphorylase 1 (UPP1) is a member of the family of pentosyltransferase. UPP1 catalyses the reversible phosphorolysis of uridine to uracil. The expression levels and the enzymatic activity of UPP1 are higher in human solid tumors than in adjacent normal tissues. The high level of UPP1 expression in some tumors makes it a potential prognosticfactor for some cancers, such as oral squamous cell carcinoma. UPP1 is important for the homeostatic regulation of intracellular and plasma uridine concentratios. UPP1 plays an important role in the pyrimidine salvage pathway through its catalysis of the reversible phosphorolysis of uridine to uracil.

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Lon Protease, is a member of the Lon protease family. They are found in archaea, bacteria and eukaryotes. Lon protease is ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins, including some antitoxins. It required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. It degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long and binds to DNA in a double-stranded, site-specific manner. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, and UmuD. Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system.

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D-tyrosyl-tRNA(Tyr) deacylase 1(DTD1) belongs to the DTD family, and expressed in many adult and fetal tissues such as testis, ovary, spleen in adult and fetal brain. It is a nucleus and cytoplasm located protein, and is preferentially phosphorylated in cells arrested early in S phase. DTD1 is an ATPase involved in DNA replication, it may facilitate loading of CDC45 onto pre-replication complexes. The protein may hydrolyse D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr), a possible defense mechanism against a harmful effect of D-tyrosine.

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Selenophosphate synthetase 1 (SEPHS1) belongs to the selenophosphate synthase 1 family, Class II subfamily. It has four different isoforms by alternative splicing. Isoform 1 and isoform 2 are gradually expressed during the cell cycle until G2/M phase and then decreased, which Isoform 3 is gradually expressed during the cell cycle until S phase and then decreased. SEPHS1 can be activated by phosphate ions and by potassium ions. It can synthesise synthesises selenophosphate from selenide and ATP. Selenophosphate is the selenium donor used to synthesise selenocysteine, which is co-translationally incorporated into selenoproteins at in-frame UGA codons.

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Peptidyl-Prolyl Cis-Trans Isomerase-Like 1 (PPIase) belongs to the cyclophilin-type PPIase family. PPIases can accelerate the folding of proteins and catalyze the cis-trans isomerisaion of proline imidic peptide bonds in oligopeptides. PPIase is a ubiquitous protein and has highly expression in heart ,skeletal and muscle. PPIase contains a PPIase cyclophilin-type domain and four Cyclosporin A binding regions. PPIase might play an important role in proliferation of cancer cells through modulation of phosphorylation of stathmin. It is suggested that PPIase can act as as a novel molecular target for colon-cancer therapy.

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Peptidyl-Prolyl Cis-Trans Isomerase D (PPID) belongs to the cyclophilin-type PPIase family and PPIase D subfamily. PPID is widely expressed and it contains one PPIase cyclophilin-type domain and three TPR repeats. PPID catalyses the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides and accelerates the folding of proteins. PPID can bind to the immunosuppressant cyclosporine A and is known that its overexpression suppresses the apoptosis in cancer cells.

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Fructose-1,6-bisphosphatase 1(FBP1) is a homotetramer protein and belongs to the FBPase class 1 family. It involves in carbohydrate biosynthesis; gluconeogenesis pathway. FBP1 is a gluconeogenesis regulatory protein which catalyses the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.

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Protein Disulfide-Isomerase A4 (PDIA4) is an endoplasmic reticulum luminal protein that belongs to the protein disulfide isomerase family. Human PDIA4 is synthesised as a 625 amino acid precursor that contains a 20 amino acid signal sequence, and a 625 amino acid mature chain, including three thioredoxin domains. PDIA4 catalyses the rearrangement of -S-S- bonds in proteins and is thought to be a deoxycytidine kinase. In addition, PDIA4 serves as a proteases protein disulfide isomerase, phospholipase or an arrangement of these.

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Pancreatic Lipase-Related Protein 1 (PNLIPRP1) belongs to the Lipase family within the AB hydrolase superfamily. PNLIPRP1 is a secreted protein and contains one PLAT domain. PNLIPRP1 is involved in lipid metabolic process, acting as a negative regulator of pancreatic lipase activity by competing with pancreatic lipase for colipase occupancy. PNLIPRP1 may play a role in inhibiting dietary triglyceride digestion, but it lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters.

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Cyclin-dependent kinase 2 (CDK2) belongs to the cyclin-dependent kinase of Ser/Thr protein kinase. CDK2 acts as a catalytic subunit of the cyclin dependent kinase complex, whose activity is restricted to the G1-S phage of the cell cycle, it is essential for the G1/S transition. The kinase activity of CDK2 can be regulated by the association with a cyclin subunit, its phosphorylation state and CDK inhibitors. The activation of the CDK2/cyclin complex requires the phosphorylation of Thr160 and the dephosphorylation of Try14 and Tyr15. The inhibition of CDK2-cyclin complex can also be attributed to association with p27Kip1 and p21Waf1/Cip1. The activation of CDK2 has been shown to be necessary for apoptosis of quiescent cells, such as neurons, thymocytes and endothelial cells.