Search results

Prolyl Endopeptidase , also known as PREP is a cytosolic prolyl endopeptidase which cleaves peptide bonds on the C-terminal side of prolyl residues within peptides which are up to about 30 a.a long. In addition, Prolyl endopeptidases have been shown to be implicated in the maturation and degradation of peptide hormones and neuropeptides.

GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.

HAGH is a part of the glyoxalase family and a thiolesterase which hydrolyses S-lactoyl-glutathione to reduced glutathione and D-lactate. HAGH protein is a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73 and serves as a pro-survival factor of the p53 family. HAGH appears only as a monomer and binds two zinc ions per subunit.

NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.

Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.

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.

Enoyl-CoA Delta Isomerase 1 (ECI1) is a main mitochondrial enzyme which takes part in beta-oxidation of unsaturated fatty acids. ECI1 is a member of the hydratase/isomerase superfamily. ECI1 catalyzes the transformation of 3-cis and 3-trans-enoyl-CoA esters to the 2-trans-enoylCoA intermediates.

GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 takes part in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and demonstrate close homology.

Lysozymeis an antimicrobial enzyme produced by animals that are part of the innate immune system. Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall.Lysozymes have primarily a bacteriolytic function - those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.

PRDX1 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX1 is an important protector of red blood cells against reactive oxygen species and in tumor prevention.
PRDX1 is antioxidant protective in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX1 has a proliferative effect and is involved in cancer development or progression.
Peroxiredoxin-1 is plays a role in redox regulation of the cell. Peroxiredoxin decreases peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. Peroxiredoxin is involved in eliminating peroxides generated during metabolism. Peroxiredoxin participates in the signaling cascades of growth factors and TNF-alpha by regulating the intracellular concentrations of h(2)o(2).

NAT6 is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to acrylamines. NAT6 is located mainly in the cytoplasm and its activity has been recognized by its feasibility to acetylate the N-terminus of proteins using a ping-pong-like mechanism and by its substrate specificity. Given that the NAT6 gene maps to the chromosomal region 3p21.3, which includes at least one tumor suppressor gene, the function of NAT6 plays an important role in cancer.