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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.

GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.

METTL21A, which is a part of the methyltransferase superfamily, is a Protein-lysine methyltransferase that in vitro methylates HSPA1, HSPA5 and HSPA8.

The enzyme Carbonic anhydrase II having an accession number of NP_414668 is also called carbonate dehydratase which is part of the enzyme family that catalyses rapid inter-conversion of carbon dioxide & water to bicarbonate, carbonic acid and protons (CO2 + H2O ? HCO3? + H+), a reaction that occurs rather slowly in the absence of a catalyst. The majority of carbonic anhydrases enclose a zinc ion in their active site and therefore is classified as metalloenzymes.
The most important function of Carbonic anhydrase is known to preserve acid-base balance in blood and other tissues, and to help transport carbon dioxide of tissues. Carbonic anhydrases have been found in all kingdoms of life. Carbonic anhydrase has 3 different classes: alpha, beta and gamma which share very little sequence or structural similarity, thus far they all perform the same function and require a zinc ion at the active site. Mammalian carbonic anhydrase is monomeric and belongs to the alpha class. Plant carbonic anhydrase is dimeric and belongs to the beta class.
Methane-producing bacteria carbonic anhydrase is trimeric and grows in hot springs which forms the gamma class.

Aldolase C Fructose-Bisphosphate (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain.

Tyrosine 3-monooxygenase (Th), is a rate-limiting enzyme in catecholamine synthesis. Th utilizes tetrahydrobiopterin as well as molecular oxygen to convert tyrosine to DOPA. Th regulates dopamine (DA) neurotransmission at the biosynthesis and reuptake steps. Th takes a vital part in the physiology of adrenergic neurons. Furthermore, Th effects overexpression in lymphocytes on the differentiation as well as function of T helper cells.

CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.

6PGD is the 2nd dehydrogenase in the pentose phosphate shift. Pentose is crucial for the biosynthesis of nucleic acid. The pentose phosphate cycle is a prominent source of NADPH. 6PGD deficiency is mostly asymptomatic, and the inheritance of this deasis is autosomal dominant. PGD deficiency elevate the erythrocyte pyruvate kinase levels of activity & decreases glutathione synthetase, which causes hemolysis.

Glycine-N-Acyltransferase-Like 2 (GLYATL2) is a part of the glycine N-acyltransferase family expressed mainly in salivary gland and trachea. GLYATL2 is a mitochondrial acyltransferase that transfers the acyl group to the N-terminus of glycine. GLYATL2 conjugates numerous substrates, like arachidonoyl-CoA and saturated medium and longchain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA, to form a variety of N-acylglycines. GLYATL2 also shows a preference for monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor.

OTC is a member of the ATCase/OTCase family. OTC has a key part in the urea cycle, catalyzing the second step in this pathway: the transformation of L-orthinine and carbamoyl phosphate to L-citrulline. In humans, the urea cycle is a vital pathway to detoxification of ammonia. Alterations in the gene encoding OTC are linked to the X-linked disorder OTCD (ornithine carbamoyltransferase deficiency). OTCD disorder of the urea cycle is characterized by hyperammonemia.

Fatty Acid Amide Hydrolase 2 (FAAH2) shares a conserved protein motif with the amidase signature family of enzymes. FAAH2 catalyzes the hydrolysis of a broad range of bioactive lipids, including those from the 3 main classes of fatty acid amides; N-acylethanolamines, fatty acid primary amides and N-acyl amino acids. FAAH2 is also degrades bioactive fatty acid amides to their corresponding acids, thus helping to end the signaling functions of these molecules. FAAH2 prefers monounsaturated acyl chains as a substrate.

GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.

Glutamic-Pyruvate Transaminase 2 (GPT2) catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids.

Lactate dehydrogenase (LDH) is an enzyme(EC1.1.1.27) present in a wide variety of organisms, including plants and animals.
A tetrameric enzyme that catalyses the interconversion of pyruvateand lactate with concomitant interconversion of NADH and NAD+. At high concentrations of pyruvate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.

MTHFS is a cytosolic protein which takes part in the formate metabolic process. MTHFS along with a magnesium cofactor catalyzes the ATP-dependent reaction which reduces 5-formyltetrahydrofolate (5-MTHF) to 5,10-methenyltetrahydrofolate(MTHF). MTHF is the substrate used by MTHFR (methylenetetrahydrofolate reductase) to generate 5-MTHF. In addition, MTHF is a coenzyme used in thymidine biosynthesis by thymidylate synthase (FAD).

Inorganic pyrophosphatase (ppa) is a member of the Ppase family. PPA is an enzyme which catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Since this is a highly exergonic reaction, it can therefore be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The role of the PPA enzyme is a critical one in the lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, DNA synthesis, as well as other biochemical transformations.

CA, also known as carbonic anhydrase is an enzyme. Its main function revolves around the CO2 + H2O HCO3- + H+ (conversion of carbon dioxide to bicarbonate & protons). CA has a zinc ion in its active site. The main function of CA is to keep acid-base balance in the blood stream and various tissues. This enzyme also assists Carbonic Anhydrase I to move CO2 to and from tissues.

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.

The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

HADH is part of the 3-hydroxyacyl-CoA dehydrogenase enzyme family. HADH is involved in mitochondrial matrix to catalyze the oxidation of straight-chain 3-hydroxyacyl-CoAs as part of the beta-oxidation pathway. HADH enzymatic activity is at its peak with medium-chain-length fatty acids. Mutations in HADH cause familial hyperinsulinemic hypoglycemia. HADH participates in fatty acid oxidation, where some enzymes work in a step-wise fashion to break metabolize fats and convert them to energy.

Glucose-6-phosphate isomerase (GPI) is a part of the GPI family whose members encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. GPI is a dimeric enzyme which catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. Mammalian GPI also functions as a tumor-secreted cytokine and an angiogenic factor (AMF) which stimulates endothelial cell motility. In addition, GPI is a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. GPI performs in different capacities inside and outside the cell. In the cytoplasm, GPI is involved in glycolysis and gluconeogenesis, while outside the cell it acts as a neurotrophic factor for spinal and sensory neurons.
Defects in the GPI gene cause the nonspherocytic hemolytic anemia and a severe enzyme deficiency can be linked to hydrops fetalis, immediate neonatal death and neurological impairment.

MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.

Aldolase C Fructose-Bisphosphate (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain.