Search results

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.

Myeloperoxidase is an important enzyme used by granulocytes during phagocytic lysis of foreign particles engulfed. In normal tissues and in a variety of myeloproliferative disorders myeloid cells of both neutrophilic and eosinophilic types, at all stages of maturation, exhibit strong cytoplasmic reactivity for MPO. Erythroid precursors, megakaryocytes, lymphoid cells, mast cells, and plasma cells are nonreactive. MPO is not observed in the neoplastic cells of a wide variety of epithelial tumors and sarcomas. MPO is useful in differentiating between myeloid and lymphoid leukemias.

Isocitrate dehydrogenase [NAD] subunit gamma (IDH3G) mitochondrial is a member of the isocitrate and isopropylmalate dehydrogenases family. Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. The IDH3G is a gamma subunit of one isozyme of isocitrate dehydrogenase which belongs to a distinct subclass, which utilizes NAD(+) as the electron acceptor, and is restricted to the mitochondrial matrix.

Farnesyl-Diphosphate Farnesyltransferase 1, also known as FDFT1 is a membrane-associated enzyme sited at a branch point in the mevalonate pathway. FDFT1belongs to the phytoene/squalene synthase family. FDFT1 is the 1st specific enzyme in cholesterol biosynthesis, which catalyzes the dimerization of 2 molecules of farnesyl diphosphate in a two-step reaction to form squalene.

Ribonuclease 3 (RNASE3) is cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. RNASE3 possesses a broad diversity of biological activities. RNASE3 protein has shown antibacterial activity such as cytoplasmic membrane depolarization of preferentially Gram-negative and Gram-positive strains and promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.

Formiminotransferase cyclodeaminase is an enzyme which catalyzes the conversion of formiminoglutamateand tetrahydrofolateinto formiminotetrahydrofolateand glutamate.
Formiminotransferase cyclodeaminase, a bifunctional enzyme of tetrahydrofolate synthesis, is the target antigen of anti-LC1 (liver cytosol antigen type 1) autoantibodies. Presence of LC1 autoantibodies is a marker for type 2 autoimmune hepatitis (for which anti-LKM 1/cytochrome P450 2D6 autoantibodies are a further marker).
Serum LC1 autoantibody concentrations appear to fluctuate in parallel with aminotransferase levels, a particularly intriguing observation that suggests a possible role of LC1 autoreactivity in the pathogenic mechanism leading to hepatocyte injury.

Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.

PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.

IMPDH1 is a rate limiting enzyme in the de novo synthesis of guanine nucleotides and consequently participates in the regulation of cell growth. IMPDH1 takes part in the development of malignancy and the growth progression of some tumors. IMPDH1 performs as a homotetramer to regulate cell growth. IMPDH1 catalyzes the synthesis of xanthine monophosphate (XMP) from inosine-5''-monophosphate (IMP). Defects in this gene are a cause of retinitis pigmentosa type 10 (RP10).

Sepiapterin Reductase is an aldo-keto reductase that catalyzes the NADPH-dependent reduction of pteridine derivatives and is essential in the biosynthesis of BH4. Mutations in Sepiapterin Reductase gene result in DOPA-responsive dystonia due to sepiaterin reductase deficiency defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Sepiapterin reductase is part of the short-chain dehydrogenase/reductase family which reduces exogenous carbonyl compounds as well as phenylpropanedione. Sepiapterin reductase is an important enzyme for the biosynthesis of tetrahydrobiopterin, an necessary cofactor for aromatic amino acid hydrolases together with tyrosine hydroxylase, the rate-limiting enzyme in dopamine synthesis.

LPL is a lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue. LPL acts as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Type I hyperlipoproteinemia is a result of severe mutations which cause LPL deficiency, whereas less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. Lipoprotein lipase (LPL) is a fundamental enzyme in plasma triglyceride hydrolysis and is secreted by macrophages in the subendothelial space. LPL also promotes the development of atherosclerosis through facilitation of monocyte adhesion to endothelial cells, stimulation of tumor necrosis factor alpha (TNF) secretion and induction of vascular smooth muscle cell proliferation.

The SARS CoV-2 3CL protease (C30 Endopeptidase) derived from human SARS-CoV-2 is a C30-type cysteine protease situated in the NS3 segment. SARS CoV-2 3CL protease biological functionality is needed to process viral polyproteins to functional complete units. SARS CoV-2 3CL protease (main protease) is the core protease protein in CoV and corresponds to non-structural protein 5. SARS CoV-2 3CL cleaves the CoV polyprotein at 11 locations. SARS CoV-2 3CL protease has a cysteine-histidine catalytic dyad at its active site and cleaves a Gln–(Ser/Ala/Gly) peptide bond. SARS CoV-2 3CL protease at position P1 cleaves the bond between the glutamine and serine/alanine/glycine. SARS CoV-2 3CL protease is necessary in the processing of the CoV replicase polyprotein.

Branched-chain ?-keto acid dehydrogenase E1 component ? chain (BCKDHA) is a member of the BCKDHA family. The BCKD (branched-chain alpha-keto acid dehydrogenase) complex is an inner mitochondrial enzyme complex which catalyzes the second major step in the catabolism of the branched-chain amino acids leucine, isoleucine, and valine. This complex consists of 3 catalytic components: a heterotetrameric (alpha2-beta2) branched-chain alpha-keto acid decarboxylase (E1), a dihydrolipoyl transacylase (E2), and a dihydrolipoamide dehydrogenase (E3). Mutations in the BCKDHA gene result in maple syrup urine disease, type IA.

OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3 to the lesion.

Ubiquitin carboxyl-terminal hydrolase isozyme L3 belongs to a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to produce the ubiquitin monomer. UCHL3 takes part in the regulation of neuronal development and spermatogenesis and is associated to neurodegenerative diseases. UCHL3 has a 54% homology to UCHL1.

Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed.

Glycerol-3-phosphate dehydrogenase 1-like protein (GPD1L) converts sn-glycerol 3-phosphate to glycerone phosphate. GPD1L is found in the cytoplasm, associated with the plasma membrane, where it binds the sodium channel, voltage-gated, type V, alpha subunit (SCN5A). Mutations in the GPD1L gene are the cause of SIDS (sudden infant death syndrome) and Brugada syndrome type 2 (an autosomal dominant tachyarrhythmia).

Phospholipase A1 Member A (PLA1A) is a phospholipase which hydrolyzes fatty acids at the sn-1 position of phosphatidylserine and 1-acyl-2-lysophosphatidylserine. The secreted PLA1A protein hydrolyzes phosphatidylserine in liposomes. PLA1A hydrolyzes phosphatidylserine (PS) in the form of liposomes and 1-acyl-2 lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA) or phosphatidylinositol (PI). PLA1A isoform 2 hydrolyzes lyso-PS but not PS. The hydrolysis of lyso-PS in peritoneal mast cells activated by receptors for IgE leads to stimulation of histamine production.

PPA2 shares great imagination with members of the inorganic pyrophosphatase (PPase) family. PPA2 is localized to the mitochondrion and owns the signature sequence necessary for the catalytic activity of PPase. PPases catalyze the hydrolysis of pyrophosphate to inorganic phosphate, which is vital for the phosphate metabolism of cells.

GGCT is a member of the family of transferases, specifically the aminoacyltransferases. GGCT protein catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and takes an important part in glutathione homeostasis. GGCT induces release of cytochrome c from mitochondria with resultant induction of apoptosis.

Ribophorin 2 (RPN2) is a dolichyl-diphosphooligosaccharide protein glycosyltransferase subunit 2. The Ribophorin 2 protein is part of an N-oligosaccharyl transferase complex which links high mannose oligosaccharides to asparagine residues found in the Asn-X-Ser/Thr consensus motif of nascent polypeptide chains. RPN2 is analogous in sequence to the yeast oligosaccharyl transferase subunit SWP1.

Ribose-5-phosphate isomerase (RPIA) is a member of the ribose 5-phosphate isomerase family. RPIA is an enzyme which catalyzes the conversion between ribose-5-phosphate (R5P) and ribulose-5-phosphate (Ru5P). RPI occurs as 2 separate proteins forms, termed RPIA and RPIB. RPIA has a vital role in the metabolism of plants and animals, as it is involved in the Calvin cycle which takes place in plants, and the pentose phosphate pathway which occurs in plants as well as animals.

Acireductone dioxygenase 1 (ADI1) is a part of the acireductone dioxygenase family of metal-binding enzymes, which are involved in methionine salvage. ADI1 regulates mRNA processing in the nucleus, and carries out different functions depending on its localization. Related pseudogenes have been defined on chromosomes 8 and 20. ADI1 down-regulates cell migration arbitrated by MMP14.

PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.