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N-acetylneuraminate lyase (NPL) is an enzyme which catalyzes the chemical reaction (N-acetylneuraminate ->N-acetyl-D-mannosamine + pyruvate). NPL is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NPL participates in amino sugars metabolism.

Chitodextrinase is a unique membrane-bound endoenzyme. The chitodextrinase enzyme cleaves soluble oligomers, but not chitin, to the di- and trisaccharides. Chitodextrinase is unable to solubilize chitin, but it can catalyze the hydrolysis of high to low molecular weight soluble chitin oligosaccharides.

GlsA1 is a member of the great superfamily of serine-dependent beta-lactamases and penicillin-binding proteins which exist almost in every bacteria and eukaryotes and catalyze the hydrolytic deamidation of l-glutamine to l-glutamate and free NH4+.

HDAC2 is a member of the histone deacetylase family that performs through the construction of large multiprotein complexes and are in charge of the deacetylation of lysine residues on the N-terminal region of the core histones. HDAC2 forms transcriptional repressor complexes by relating to a diversity of proteins, like YY1- a mammalian zinc-finger transcription factor.
In addition, HDAC2 has a vital part in transcriptional regulation, cell cycle progression and developmental procedures.

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.

Aldolase A (ALDOA) is a glycolytic enzyme, which catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. ALDOA is found in the developing embryo and is produced in even greater amounts in adult muscle. ALDOA expression is repressed in the adult liver, kidney and intestine and similar to ALDOC levels in the brain and other nervous tissue. ALDOA deficiency has been linked with myopathy and hemolytic anemia.

Pyroglutamyl-Peptidase I (PGPEP1) is an omega peptidase which detaches pyroglutamyl residues from the amino termini of peptides and proteins. PGPEP1 is a cytosolic cysteine peptidase which is expressed in most cell types. PGPEP1 enzyme has need of s a thiol-reducing agent for activity. PGPEP1 is possibly involved in the inactivation of biologically active peptides which have an amino terminal pyroglutamyl group, for instance peptides as neurotensin, luteinizing hormone releasing hormone, and thyrotropinreleasing hormone.

Acetylcholinesterase (ACHE) belongs to the type-B carboxylesterase/lipase family. ACHE catalyzes the breakdown of acetylcholine and other choline esters that play a role as neurotransmitters. During neurotransmission, ACH is released from the presynaptic neuron into the synaptic cleft and binds ACH receptors on the post-synaptic membrane, transmitting the signal from the nerve. ACHE is located on the post-synaptic membrane, terminates the signal transmission by hydrolyzing ACH.

HEXA is the alpha subunit of the lysosomal enzyme beta-hexosaminidase which, combined with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules having N-acetyl hexosamines terminus. The two subunits composing Beta-hexosaminidase, alpha and beta, belong to the glycosyl hydrolases family and are encoded by distinct genes. Alpha subunit gene mutations can cause Tay-Sachs disease (GM2-gangliosidosis type I).

Lipase Endothelial (LIPG) has extensive phospholipase activity and may be involved in lipoprotein metabolism and vascular biology. The LIPG protein is considered a member of the TG lipase family through its sequence and characteristic lid region which provides substrate specificity for enzymes of the TG lipase family. In addition, the LIPG has triglyceride lipase activities. LIPG hydrolyzes HDLs more efficiently than other lipoproteins.

Core 1 Beta3-Gal-T1 also known as,C1GALT1 creates the common core 1 O-glycan structure, Gal-beta-1-3GalNAc-R, by the transfer of Gal from UDP-Gal to GalNAc-alpha-1-R. Core 1 is a precursor for lots of extended mucin-type O-glycans on cell surface and secreted glycoproteins. Studies in mice have shown that this gene takes a main role in angiogenesis, thrombopoiesis and kidney homeostasis.

Urate oxidase catalyzes the enzymatic oxidation (degrades) of uric acid into allantoin, an inactive and soluble metabolite, which is 5 to 10 fold more soluble than uric acid . Urate oxidase is an enzyme of the purine breakdown pathway that catalyses the oxidation of uric acid to allantoin. Uricase is present in numerous diverse organisms, but not in higher primates including human. Hyperuricaemia is most commonly associated with gout and also occurs in mammalians with malignancy, especially those with lymphoid malignancies due to rapid cell turnover and an increased rate of purine metabolism. Uricase is effective in the prevention and treatment of hyperuricaemia in mammalians with malignancy and in those who have undergone transplantation. It appears to act rapidly, safely and induces a more dramatic decrease in plasma levels of uric acid.

Arylsulfatase A (ARSA) hydrolyzes cerebrosidesulfate to cerebroside and sulfate. ARSA is inhibited by phosphate. The phosphate develops a covalent bond with the active site 3-oxoalanine. ARSA gene defects cause metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in various neurological symptoms and ultimately death.

ADP-ribosylarginine hydrolase (ADPRH) is a member of the ADP-ribosylglycohydrolase family. ADPRH catalyzes the removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. The human ADPRH enzyme is DTT-independent as opposed to the rat and mouse enzymes, which require DTT for maximal activity.

AKR1B1 is part of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. AKR1B1 catalyzes the reduction several aldehydes, including the aldehyde form of glucose, and thus involved in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. AKR1B1 catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Transgenic mice over expressing human aldose reductase show that AKR1B1 is a key player in ischemic injury and impairment of functional and metabolic recovery after ischemia. Aldose Reductase is an obligatory mediator of TNF-alpha signaling leading to an increase in the expression of adhesion molecules and increased binding of monocytes to the endothelium. AKR1B1 is a critical regulator of TNF-alpha-induced apoptotic signaling in endothelial cells.

Peptidase D, also known as PEPD, Is a part of the peptidase family. PEPD is involved in collagen metabolism due to the high level of iminoacids in collagen. PEPD recycles proline, and sets the pace for the production of collagen. PEPD is also parts dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position.

Carboxymethylenebutenolidase homolog (CMBL) is a cysteine hydrolase of the dienelactone hydrolase family which is highly expressed in the liver cytosol. CMBL is the human homolog of Pseudomonas dienelactone hydrolase, which is a protein that participates in the bacterial halocatechol degradation pathway. CMBL which preferentially cleaves cyclic esters activates medoxomil-ester prodrugs in which the medoxomil moiety is coupled with an oxygen atom. CMBL is inhibited by PCMB (p-chloromercuribenzoate) and is encoded by a gene which maps to human chromosome 5p15.2. CMBL can also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin. CMBL is widely expressed, with the highest levels in the liver, followed by the kidney, small intestine and the colon.

Matrix metalloproteinase-2 (MMP-2) is involved in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP-2 contains a number of distinct domains: a prodomain that is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin like domain believed to have a role in substrate targeting; and a carboxyl terminal (hemopexin like) domain containing 2 N-linked glycosylation. The MMP-2 can degrade an extensive array of substrates including type IV, V, VII and X collagens as well as gelatin type I. In addition, MMP-2 interacts with THBS2, TIMP2, Thrombospondin 1, CCL7 and TIMP4. MMP-2 autocatalytic cleavage in the C-terminal generates the anti-angiogenic peptide, PEX. This process seems to be made possible by binding integrinv/beta3. Defects in the MMP-2 are the cause of Torg-Winchester syndrome (TWS), aka multicentric osteolysis nodulosis and arthropathy (MONA).

HPGD is the essential enzyme of prostaglandin degradation. 15-PGDH protein strongly decreases the biologic activity of these molecules by catalyzing the oxidation of the 15-hydroxyl group of prostaglandins to a keto group. GDH1 is involved in numerous physiologic and cellular processes, for instance inflammation.

ACAA1 is part of the thiolase family of enzymes and is takes part in lipid metabolism. ACAA1 enzyme is localized to the peroxisome and catalyzes the conversion of acyl-CoA and acetyl-CoA to 3-oxoacyl-CoA in the fatty acid oxidation pathway. ACAA1 shows high enzymatic activity in liver, kidney, intestine and white adipose tissue in rats. ACAA1 deficiency causes pseudo-Zellweger syndrome.

Carboxypeptidase-E (CPE ) is a carboxypeptidase that cleaves C-terminal amino acid residues and is involved in the biosynthesis of peptide hormones and neurotransmitters. CPE is a peripheral membrane protein. CPE specifically connects regulated secretory pathway proteins, including prohormones, but constitutively secreted proteins. Mutations in CPE are implicated in type II diabetes.

Carboxypeptidase B (EC 3.4.17.2) catalyzes hydrolysis of the basic amino acids lysine, arginine and ornithine from the C-terminal end of polypeptides. The Mw was found to be 34.5 kDa, optimun pH-7.9, and pI-6. Carboxypeptidase B is inhibited by arginine, lysine and ornithine. The enzyme is not inhibited by di-isopropylfluorophosphate (DFP), but it is inhibited by metal chelating agents, e.g., EDTA, 1,10-phenanthroline.

CBR1 is one of numerous monomeric, NADPH-dependent oxidoreductases having ubiquistly specificity for carbonyl compounds. CBR1 is broadly distributed in human tissues. CBR1 metabolizes toxic environmental quinones and pharmacological relevant substrates. CBR1 converts prostaglandin E2 to prostaglandin F2-alpha.

GSTZ1 is part of the glutathione S-transferase super-family which encodes multifunctional enzymes vital in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. GSTZ1 participates in the catabolism of phenylalanine and tyrosine. Thus defects in GSTZ1 cause harsh metabolic disorders including alkaptonuria, phenylketonuria and tyrosinaemia. GSTZ1 is a bifunctional protein which has minimal glutathione-conjugating activity with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. GSTZ1 has low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. GSTZ1 catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.