lysozyme C is a secreted protein and belongs to the glycosyl hydrolase 22 family. Lysozymes have primarily a bacteriolytic function, damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.
Lysozyme G-like 1 belongs to the glycosyl hydrolase 23 family. Glycoside hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. Lysozyme G-like 1 exhibits hydrolase activity, acting on glycosyl bonds (inferred); lysozyme activity (inferred). It is found in extracellular region and may functions in cell wall macromolecule catabolic process, metabolic process and peptidoglycan catabolic process. The lysozyme G gene structure has been largely conserved during vertebrate evolution, except at the 5' end of the gene, which varies in number of exons.
Lymphatic Vessel Endothelial Hyaluronic Acid Receptor 1 is a single-pass type I membrane protein. LYVE-1 is a CD44 homolog found primarily on lymphatic endothelial cells 1. LYVE-1 mainly expressed in endothelial cells lining lymphatic vessels. While LYVE-1 functions is a Ligand-specific transporter trafficking between intracellular organelles (TGN) and the plasma membrane. LYVE-1 plays a role in autocrine regulation of cell growth mediated by growth regulators containing cell surface retention sequence binding (CRS). It may act as an hyaluronan (HA) transporter, either mediating its uptake for catabolism within lymphatic endothelial cells themselves, or its transport into the lumen of afferent lymphatic vessels for subsequent re-uptake and degradation in lymph nodes.
Maleylacetoacetate Isomerase (MAAI) belongs to the Glutathione S-Transferase super-family. MAAI encodes multifunctional enzymes in the detoxification of electrophilic molecules by conjugation with glutathione, for example, mutagens, carcinogens and several therapeutic drugs. MAAI is a bifunctional protein with low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. MAAI can catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. But it has minimal glutathione-conjugating activity with 7-chloro-4-nitrobenz-2-oxa-1, ethacrynic acid 3-diazole and maleylacetoacetate isomerase activity.
Mitotic spindle assembly checkpoint protein MAD2A, also known as HsMAD2, Mitotic arrest deficient 2-like protein 1, MAD2-like protein 1, MAD2L1 and MAD2, is a nucleus and cytoplasm protein which belongs to theMAD2 family. MAD2L1 is a component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. MAD2L1 is required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate. MAD2L1 has two highly different native conformations, an inactive open conformation that cannot bind CDC20 and that predominates in cytosolic monomers, and an active closed conformation. MAD2L1 in the closed conformation preferentially dimerizes with another molecule in the open conformation, but can also form a dimer with a molecule in the closed conformation. Formation of a heterotetrameric core complex containing two molecules of MAD1L1 and of MAD2L1 in the closed conformation promotes binding of another molecule of MAD2L1 in the open conformation and the conversion of the open to the closed form, and thereby promotes interaction with CDC20.
c-Maf is an approximately 40 kDa transcriptional regulator that contains one bZIP domain. It can associate into homodimers and heterodimers with other basic leucine zipper transcription factors. c-Maf plays an important role in fetal erythropoiesis, lens development, mechanosensory neuron development, and the differentiation of chondrocytes and osteoblasts. In the pancreas, c-Maf promotes the transcription of glucagon in alpha cells and insulin in beta cells.
Drosophila that have mutations in their mago nashi (grandchildless) gene produce progeny with defects in germplasm assembly and germline development. This gene encodes the mammalian mago nashi homolog. In mammals, mRNA expression is not limited to the germ plasm, but is expressed ubiquitously in adult tissues and can be induced by serum stimulation of quiescent fibroblasts.
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