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GLYAT is a mitochondrial acyltransferase that conjugates glycine with acyl-CoA substrates in the mitochondria. GLYAT is vital to the detoxification of endogenous and xenobiotic acyl-CoA's.

Cathepsin-E also known as CTSE is a gastric aspartyl protease which functions as a disulfide-linked homodimer. CTSE belongs to the peptidase C1 family; furthermore it has specificity similar to pepsin A and cathepsin D. CTSE is an intracellular proteinase which does not seem to be involved in the digestion of dietary protein and is found in the uppermost concentration in the surface of epithelial mucus-producing cells of the stomach. CTSE is the first aspartic proteinaseexpressed in the fetal stomach and is discovered in more than half of gastric cancers. For that reason CTSE is anoncofetal antigen. In addition, transcript variants utilizing alternative polyadenylation signals and two transcript variantsencoding different isoforms exist for this gene.

DPP4 also called adenosine deaminase complexing protein-2, and T-cell activation antigen CD26 is a serine exopeptidase and complex enzyme that is expressed on the surface of most cell types. DPPIV is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. DPP4 plays a role in t-cell activation. DPP4 is associated with intracellular signal transduction, apoptosis and involved in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and GLP-1.

DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.

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.

Carboxylesterase 1D, also known as CES1D is part of a big family of carboxylesterases which are responsible for the hydrolysis of ester in addition to amide bonds. CES1D is the principle lipase of white adipose tissue fat cake extracts. Partially purified white adipose tissue Ces1d had lipase activity in addition to lesser but detectable neutral cholesteryl ester hydrolase activity. CES1D demonstrates low catalytic efficiency for hydrolysis of CPT-11, a prodrugs for camptothecin used in cancer therapeutics.

UPP1 catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate which are used as carbon and energy sources or in the release of pyrimidine bases for nucleotide synthesis. UPP1 is part of the family of glycosyltransferases, specifically the pentosyltransferases. Pyrimidine nucleoside phosphorylases add ribose or deoxyribose to pyrimidine bases to form nucleosides that can be incorporated into RNA or DNA.

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.

4-Hydroxyphenylpyruvate Dioxygenase Isoform-1 is an Fe-containing enzyme, which catalyzes the second reaction in the catabolism of tyrosine the conversion of 4-hydroxyphenylpyruvate to homogentisate. Present as a homodimer, HPD uses zinc as a cofactor to catalyze the third step in the conversion of L-phenylalanine to fumarate and acetoacetic acid. Flaws in the gene encoding HPD result in tyrosinemia type 3 and hawkinsinuria, two inborn defects of metabolism which are related to a number of symptoms, like mental retardation and seizures and hair and urine abnormalities.

Malate dehydrogenase (EC1.1.1.37) is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of pyruvate using NADPH.
Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitochondrial membrane. Once in the cytosol, the malate is oxidized back to oxaloacetate by cytosolic malate dehydrogenase. Finally, phosphoenol-pyruvate carboxy kinase (PEPCK) converts oxaloacetate to phosphoenol pyruvate.

MGAT2 is an enzyme which takes part in the catalyzation of a crucial step in the reaction of oligomannose which converts to complex N-glycans. MGAT2 has three domains, classic to glycosyltransferase: short N-terminal cytoplasmic domain, a C-terminal catalytic domain and hydrophobic non-cleavable signal-anchor domain. The enzyme MGAT2 is encoded by the MGAT2 gene in humans. There are no introns in the DNA coding the gene, therefore mutations in the MGAT2 will result in carbohydrate-deficient glycoprotein syndrome, type II.

Beta-1,3-N-Acetylglucosaminyltransferase 2 (B3GNT2) is a part of the beta-1,3-N-acetylglucosaminyltransferase family which takes part in the synthesis of poly-N-acetyllactosamine. B3GNT2 is a type II transmembrane protein which prefers the substrate of lacto-N-neotetraose. B3GNT2 catalyzes the initiation and elongation of poly-N-acetyllactosamine chains and comprises the main polylactosamine synthase.

Glucuronidase Beta (GUSB) is a lysosomal hydrolase which is taking part in the stepwise degradation of glucuronic acid-containing glycosaminoglycans and plays a significant role in the degradation of dermatan and keratin sulfates. GUSB is comprised of heparin sulfate, chondroitin sulfate and hyaluronan.

Carboxyl ester lipase also known as CEL, formely called cholesterol esterase or bile salt-stimulated lipase, is an enzyme with lipolytic capablity of hydrolyzing cholesteryl esters, tri-, di-, and mono- phospholipids, acylglycerol, ceramide and lysophospholipids. The carboxyl terminus of the enzyme controls enzymatic activity by creating hydrogen bonds with the surface loop to partlyshield the active site. The active catalytic site triad of serine-histidine-aspartate is centrally located in the enzyme structure and is partly covered by a surface loop. Bile salt binding to the loop domain set free the active site for accessibility by water-insoluble substrates. CEL is produced mainly in the pancreas and lactating mammary gland, thus the protein is also expressed in liver, macrophages, and in the vessel wall.

SAT-1 is a member the acetyltransferase family, and is a rate-limiting enzyme in the catabolic pathway of polyamine metabolism. SAT1 catalyzes the acetylation of spermidine and spermine, and is involved in the regulation of the intracellular concentration of polyamines and their transport out of cells. Therefore, SAT-1’s role is essential in polyamine homoeostasis, given that acetylated products are either excreted from the cell or oxidized by acetylpolyamine oxidase. Increased SAT1 activity causes variety of other effects which include pancreatic cells death, obstruction of regenerative tissue growth, behavioral changes, keratosis follicularis spinulosa decalvans (KFSD), and hair loss.
Defects in the SAT1 gene are linked to KFSD (keratosis follicularis spinulosa decalvans), which is a rare X-linked disorder affecting the skin and the eye. The KFSD affected men show thickening of the skin of the neck, ears, and extremities, particularly the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration. Even though the majority of the affected families are compatible with an X-linked inheritance, KFSD are found to be clinically and genetically heterogeneous.

The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.

Glycerol-3-phosphate dehydrogenase 1-like protein (GPD1L) converts sn-glycerol 3-phosphate to glycerone phosphate. GPD1L is found in the cytoplasm, associated with the plasma membrane, where it binds the sodium channel, voltage-gated, type V, alpha subunit (SCN5A). Mutations in the GPD1L gene are the cause of SIDS (sudden infant death syndrome) and Brugada syndrome type 2 (an autosomal dominant tachyarrhythmia).

ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.

GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

Hyaluronidase-1 or HYAL1 is a protein, part of the endolytic glycoside hydrolase proteins group. Human hyaluronidases proteins, are 5 endo­β­N­acetyl­hexosaminidases (including HYAL1, HYAL2, HYAL3). Hyaluronidase-1 causes degradation to hyaluronic acid in the extracellular matrix of somatic tissues. HYAL1 needs an acidic environment and is the most common hyaluronidase in the plasma. Mutations in this protein can lead to mucopolysaccharidosis type IX and hyaluronidase deficiency.

Ribonuclease 7 (RNASE7) is one of the final RNase A superfamily ribonucleases. RNASE7 was isolated from skin-derived stratum corneum. RNASE7 protein demonstrated potent ribonuclease activity and hence may contribute to the well-known ribonuclease activity of human skin. RNASE7 has revealed a broad spectrum antimicrobial activity against many pathogenic microorganisms and extraordinarily potent activity.

Glutathione synthetase (GSS) is the second enzyme in the glutathione biosynthesis pathway. GSS catalyses the condensation of gamma-glutamylcysteine and glycine to form glutathione. Defects in the GSS are the cause of glutathione synthetase deficiency aka GSS deficiency or 5-oxoprolinuria or pyroglutamic aciduria, which is a severe form characterized by an increased rate of hemolysis and defective function of the central nervous system.

Adenosine deaminase-like protein (ADAL) is a putative nucleoside deaminase. ADAL catalyzes the hydrolytic deamination of adenosine or some similar substrate and has a role in purine metabolism.

Cytochrome b5 reductase 1 (CYB5R1) is a part of the flavoprotein pyridine nucleotide cytochrome reductase family. CYB5R1 is engaged in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin decrease.