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L-Asparaginase is an enzyme that depletes L-Asparagine "an important nutrient for cancer cells" resulting in cancer/tumor cell starvation. L-asparaginase is an anti-tumor agent derived from E.coli.,which can inhibit the growth of malignant cells. It is used mainly for the induction of remission in acute lymphoblastic leukaemia. Because of the lymph node origin of malignant B cells in Multiple Myeloma, L-Asparagine is an essential amino acid for their cell metabolism, and, consequently, L-Asparaginase may be of value in managing the disease.
The rationale behind asparaginase is that it takes advantage of the fact that ALL cellsare unable to synthesize the non-essential amino acidasparaginewhereas normal cells are able to make their own asparagine. These leukemic cells depend on circulating asparagine. Asparaginase however catalyzes the conversion of L-asparagine to aspartic acidand ammonia. This deprives the leukemic cell of circulating asparagine.

Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.

AnsA is a cytoplasmic asparaginase from E.coli involved in intracellular asparagine utilization. E.coli has 2 L-asparaginases: the cytoplasmic type I form (ansA) and the periplasmic type II form (ansB). AnsA (Type L asparaginase) is constitutively expressed and is obligatory for the growth of the bacteria on asparagine as the sole nitrogen source.

Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.

ASRGL1 is a 308 amino acid protein which is a member of the Ntn-hydrolase family. ASRGL1 is an autoantigenic protein which is present in the mid-piece of sperm after obstruction of the male reproductive tract. ASRGL1 is expressed highly in the testis, but is also expressed in the brain, kidney and gastrointestinal tissues. High levels of ASRGL1 are also detected in ovarian, uterine and mammary tumors in comparison with normal tissues of the same origin.

Legumain, also known as LGMN is a lysosomal cysteine protease which is found in all mouse tissues, however it was mainly abundant in the kidney as well as placenta. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.

Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.

Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.

The AsnRS enzyme is a member of the ligases family, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. An asparagine-tRNA ligase is an enzyme which catalyzes the chemical reaction: ATP + L-asparagine + tRNAAsn AMP + diphosphate + L-asparaginyl-tRNAAsn. The three substrates of the AsnRS enzyme are ATP, L-asparagine, and tRNA(Asn), whereas its three products are AMP, diphosphate, and L-asparaginyl-tRNA(Asn).

Aspartoacylas or ASPA, is a protein, found in several tissues such as skeletal muscle, cerebral white matter, kidney, liver & lungs. ASPA is a homodimer that catalyses the deacetylation of Nacetylaspartic acid. In order to create L-aspartate & acetate.

Asparagine synthetase (ASNS) is a cytoplasmic enzyme that turns aspartate toasparagine and functions mostly in mammalian organs. ASNS is responsible for cell growthand its mRNA content is associated with changes in the cell cycle. ASNS may also play a role as a biomarker for ovarian cancer.

ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters and goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Further isoforms diverge mainly in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum.

Aspartoacylase is a homodimer which catalyzes the deacetylation of N-acetylaspartic acid (NAA) (a protein whose hydrolysis is crucial to maintenance of intact white matter) to generate acetate and L-aspartate. Aspartoacylase (ASPA) is expressed in the liver, lung and kidney tissue, as well as in the skeletal muscle and in cerebral white matter. NAA is ample in the brain where hydrolysis by aspartoacylase is believed to aid maintain white matter. In other tissues ASPA functions as a scavenger of NAA from body fluids. ASPA gene mutations cause Canavan disease (CAND or spongy degeneration of the brain).

HPSE also known as Heparanase-1 is an enzyme which cleaves heparan sulfate proteoglycans to allow cell movement through changing the extracellular matrix. In fact, the Heparan sulfate proteoglycans are major components of the basement membrane and extracellular matrix. In addition, this cleavage can release bioactive molecules from the extracellular matrix. HPSE is significant for the overall degradation of proteins in lysosomes.

Progastricsin-C (PGC) is an aspartic proteinase which is synthesized in the gastric mucosa as inactive precursors. PGC is a part of the peptidase family A1 and contains a prosegment which is responsible for stabilizing the inactive form and preventing the entrance of the substrate to the active site. PGC is used as a biomarker for various gastric diseases including Helicobacter pylori related gastritis. PGC is also hydrolyzes various proteins.

DARS uses a 2 step reaction to catalyze the specific attachment of an amino acid to its cognate tRNA: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.

Argininosuccinate lyase (ASL) is a member of the lyase 1 family. ASL is an enzyme which catalyzes the reversible breakdown of Argininosuccinate (ASA) yielding the amino acids arginine and fumarate. ASL which is located in the liver cytosol is the 4th enzyme of the urea cycle and involved in the biosynthesis of arginine in all species and the production of urea in ureotelic species. While Argininosuccinate synthetase (ASS) catalyzes the formation of argininosuccinate from citrulline and aspartate, ASL breaks down the newly formed argininosuccinate into L-arginine and fumarate. L-arginine continues within the urea cycle to form urea and orinthine, whereas fumarate can enter the citric acid cycle. ASL gene Mutations result in the autosomal recessive disorder argininosuccinic aciduria, or argininosuccinic acid lyase deficiency.

PCMT1 enzyme catalyses the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. PCMT1 is involved in the repair and/or degradation of damaged proteins.

Napsin A Aspartic Peptidase, also known as NAPSA is a member of the peptidase A1 family. NAPSA is involved in the processing of pneumocyte surfactant precursors. Furthermore the activation peptides of aspartic proteinases take part as inhibitors of the active site. These peptide segments/pro-parts are considered essential for correct folding, targeting, as well as control of the activation of aspartic proteinase zymogens. The pronapsin A gene is expressed mostly in lung and kidney. In addition, NAPSA translation product is expected to be a fully functional, glycosylated aspartic proteinase precursor which contains an RGD motif as well as an additional 18 residues at its C-terminus.

Arylsulfatase G (ARSG) is a member of the sulfatase enzyme family. Sulfatases are enzymes which hydrolyze sulfate esters from sulfated steroids, carbohydrates, proteoglycans, and glycolipids. Sulfatases are involved in hormone biosynthesis, modulation of cell signaling, and degradation of macromolecules. The ARSG protein exhibits arylsulfatase activity at acidic pH, as is characteristic of lysosomal sulfatases. The Arylsulfatase G enzyme localizes in the lysosomes. ARSG is inhibited by phosphate, which forms a covalent bond with the active site 3-oxoalanine. Arylsulfatase G is widely expressed, having very low expression in the brain, lung, heart and skeletal muscle.

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.

Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen(a zymogen) to trypsin, indirectly activating a number of pancreaticdigestive enzymes.
Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.

Arginase-1 is part of the urea cycle, it catalyzes the hydrolysis of arginine to ornithine and urea. There are two isoforms of mammalian arginase which differ in their tissue location, subcellular localization, immunologic crossreactivity & physiologic role. Arginase-1is a cytosolic enzyme and expressed primarily in the liver tissue. Inherited deficiency in this enzyme may lead toargininemia, which is an autosomal recessive disease in which hyperammonemia is detected.

ARG1 catalyzes the hydrolysis of arginine to ornithine and urea. 2 isoforms of mammalian arginase exist which vary in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic role. ARG1 is a cytosolic enzyme and expressed widely in the liver as part of the urea cycle. Inherited deficiency of this ARG1 causes argininemia, which is an autosomal recessive disorder characterized by hyperammonemia.