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Methionine sulfoxide reductase A (MSRA) is a member of the MsrA Met sulfoxide reductase family. The MSRA enzyme has a vital function as a repair enzyme for proteins which have been inactivated by oxidation. MSRA catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. The three substrates of the MSRA enzyme are peptide-L-methionine, thioredoxin disulfide, and H2O, while its 2 products are peptide-L-methionine (R)-S-oxide and thioredoxin. The MSRA protein is ubiquitous and extremely conserved. Human and animal studies have shown the ultimate levels of expression in kidney and nervous tissue.

Histone deacetylase 8 (HDAC8) is a member of the class 1 of the histone deacetylase/acuc/apha family. HDAC8 is biologically involved in skull morphogenesis and metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex. Histones play a key role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation modifies chromosome structure and affects transcription factor access to DNA.

DUSP10 is a member of the protein-tyrosine phosphatase family. DUSPs inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residuesb and negatively regulate members of the MAPK superfamily which is linked with cellular proliferation and differentiation. DUSP10 interacts with MAPK14 and MAPK8. DUSP10 blocks in mammalian cells the enzymatic activation of MAP kinases with the selectivity p38 approximately JNK/SAPK >> ERK.

GZMB or Granzyme-B is a protein that mainly exist in granules of NK cells and T cells (cytotoxic), it is a serine protease. The protein is secreted by of NK cells and T cells together with the protein that creates pores (perforin) in order to lead to apoptosis in the target cell.

Ribonuclease H2 subunit A (RNASEH2A) is a member of the RNase HII family and eukaryotic subfamily. RNASEH2A Plays a part in DNA replication, probably by mediating the removal of lagging-strand Okazaki fragment RNA primers throughout DNA replication. RNASEH2A catalyzes the endonucleolytic cleavage of RNA to a 5’-phosphomonoester and is capable to bind magnesium or manganese as cofactors. Aicardi-Goutieres syndrome type 4 (AGS4) caused by defects in RNASEH2A.

TALDO1 is a important enzyme of the non-oxidative pentose phosphate pathway supplying ribose-5-phosphate for nucleic acid synthesis and NADPH for lipid biosynthesis. TALDO1 delivers a dihydroxyacetone group from donor compounds (fructose 6-phosphate or sedoheptulose 7-phosphate) to aldehyde acceptor compounds. TALDO1 is expressed at selectively great levels in oligodendrocytes of the brain. TALDO1 Deficiency results in accumulation of erythritol, D-arabitol, and ribitol.

GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.

Cathepsin B preproprotein (CTSB) is a papain-family cysteine protease which is normally located in lysosomes. CTSB is able to degrade several extracellular matrix components at both neutral and acidic pH and has been implicated in the progression of some human and rodent tumors progression and arthritis.

Obg-like ATPase 1 (OLA1) acts as a negative regulator of the cellular antioxidant response independent of transcriptional processes. OLA1 curbs the antioxidant response via nontranscriptional mechanisms. OLA1 hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. OLA1 is clearly down-regulated by DNA damage-inducing agents. OLA1 is expressed in all tissues; however it is more abundant in the testis, liver, lung, and brain. OLA1 is overexpressed in a number of malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.

Proteasome subunit alpha type-8 (PSMA8) is a member of the peptidase T1A family. PSMA8 is a multicatalytic proteinase complex which is distinguished by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. The PSMA8 subunit may be testis-specific.

DDT is an enzyme that catayzes the tautomerization of D-dopachrome to give 5,6-dihydroxyindole (DHI). DDT is part of the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. DDT shares a homologous amino acid sequence (33% identical) with MIF and has similar tautomerase activity. DDT functions a proinflammatory cytokine.

Dual Specificity Phosphatase 6, also known as DUSP6 belongs to the dual specificity protein phosphatase subfamily. DUSP6 is a Protein coding gene which inactivates MAP kinases. Various members of the family of dual specificity phosphatases show diverse tissue distribution, subcellular localization, and different modes of inducibility of their expression by extracellular stimuli.

PKLR is a pyruvate kinase which catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP. That is the rate-limiting step of glycolysis. PKLR gene encodes the L- and R-type isoenzymes through alternate splicing events controlled by different promoters. L-type isoform can also appear as a tetramer and is upregulated by glucose with implications in maturity-onset diabetes of the young.

Tyrosyl-DNA Phosphodiesterase 2 (TDP2), belongs to the CCR4/nocturin family of divalent cation-dependent phosphodiesterases.TDP2 associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor associated factors (TRAFs), and inhibits nuclear factor-kappa-B activation. TDP2 is characterized by similar sequence and structure as APE1 endonuclease, which participates in DNA repair and the activation of transcription factors.

The SARS CoV-2 3CL protease (C30 Endopeptidase) derived from human SARS-CoV-2 is a C30-type cysteine protease situated in the NS3 segment. SARS CoV-2 3CL protease biological functionality is needed to process viral polyproteins to functional complete units. SARS CoV-2 3CL protease (main protease) is the core protease protein in CoV and corresponds to non-structural protein 5. SARS CoV-2 3CL cleaves the CoV polyprotein at 11 locations. SARS CoV-2 3CL protease has a cysteine-histidine catalytic dyad at its active site and cleaves a Gln–(Ser/Ala/Gly) peptide bond. SARS CoV-2 3CL protease at position P1 cleaves the bond between the glutamine and serine/alanine/glycine. SARS CoV-2 3CL protease is necessary in the processing of the CoV replicase polyprotein.

CTSE or cathepsin E is an intracellular aspartic protease from the pepsin protein family. CTSE has a crucial part in protein degradation, creating bioactive proteins & processing antigens. The enzyme is responsible for cleaving at B site, Swedish mutant of amyloid precursor protein and the enzyme shows reactivity with the wild-type APP.

CDO1 (Cysteine dioxygenase) is a mammalian non-heme iron enzyme that initiates a number of significant metabolic pathways associated with pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. CDO1 catalyzes the conversion of L-cysteine to cysteine sulfinic acid (cysteine sulfinate) by incorporation of dioxygen. CDO1 is a vital regulator of cellular cysteine concentrations and has an essential role in maintaining the hepatic concentration of intracellular free cysteine within a proper narrow range. CDO1 is able to alter intracellular cysteine levels and glutathione levels. CDO1 is highly expressed in the liver and placenta. On the other hand CDO1 has a low expression in heart, brain and pancreas. CDO1 can also be detected in hepatoblastoma HepG2 cells.

DNA polymerase POLL is involved in base excision repair (BER). POLL is a low-fidelity polymerase that takes part in both spontaneous and DNA damage-induced mutagenesis. Furthermore, POLL takes part in the mutagenic bypass of T-T dimers. Pol lambda possesses terminal transferase and 5’-deoxyribose-5-phosphate lyase activity which is synchronized by PCNA and replication protein A.

Fumarylacetoacetate hydrolase domain-containing protein 1 (FAHD1) is a member of the FAH family. FAHD1 is considered to have hydrolase activity and it uses Magnesium and Calcium as cofactors. It seems quite likely that the metal binding sites are involved in an enzymatic activity connected to the catabolism of aromatic amino acids.

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.

Queuine TRNA-Ribosyltransferase Domain Containing 1, also known as QTRTD1 act together with QTRT1 to form an active queuine tRNA-ribosyltransferase. QTRTD1 exchanges queuine for the guanine at the wobble position of tRNAs along with GUN anticodons (tRNA-Asp,-Asn,-His and -Tyr), in that way forming the hypermodified nucleoside queuosine.

Ubiquitin-conjugating enzyme E2 H (UBE2H) is a member of the ubiquitin-conjugating enzyme family. Protein modification with ubiquitin is a vital cellular apparatus for directing abnormal or short-lived proteins for degradation. Ubiquitination requires at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2H receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2H protein sequence is 100% identical to the mouse homolog and 98% identical to the frog and zebrafish homologs.

Isocitrate dehydrogenase [NAD] subunit gamma (IDH3G) mitochondrial is a member of the isocitrate and isopropylmalate dehydrogenases family. Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. The IDH3G is a gamma subunit of one isozyme of isocitrate dehydrogenase which belongs to a distinct subclass, which utilizes NAD(+) as the electron acceptor, and is restricted to the mitochondrial matrix.