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Creatine Kinase, Mitochondrial 2 (CKMT2) is a member of the ATP:guanido phosphotransferase family. CKMT2 is responsible for the transfer of high energy phosphate from mitochondria to the cytosolic carrier, creatine. CKMT2 reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes have a principal role in energy transduction in tissues with large, variable energy demands, such as skeletal muscle, heart, brain and spermatozoa. Mitochondrial creatine kinase occurs in 2 different oligomeric forms: dimers and octamers, contrary to the exclusively dimeric cytosolic creatine kinase isoenzymes. The CKMT2 gene contains sequences homologous to a number of motifs which are shared among some nuclear genes encoding mitochondrial proteins and therefore may be crucial for the coordinated activation of these genes during mitochondrial biogenesis.

Ubiquitin-conjugating enzyme E2 F (UBE2F) is a member of the ubiquitin-conjugating enzyme family and UBE2F subfamily. Ubiquitin-conjugating enzymes or sometimes as ubiquitin-carrier enzymes, run the second step in the ubiquitination reaction which targets a protein for degradation using the proteasome. The UBE2F receives the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins.
RBX2-UBE2F complex neddylates specific target proteins, for example CUL5 as can be seen from the specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1.

Human Ubquitin-conjugating enzyme 7 (UbcH7) is a ubiquitin-conjugating enzyme (E2) mediating c-fos degradation, transcription factor NF-B maturation, and human papilloma virus-mediated p53 and Myc protein degradation, in vitro. The ubiquitin-conjugating enzymes (E2s) are essential components of the post-translational protein ubiquitination pathway, mediating the transfer of activated ubiquitin to substrate proteins. The human UBE2L1-UBE2L4 gene could potentially encode different isoforms of the UbcH7. UBE2L3 gene, located at chromosome 22q11.2, is the only identical family member with introns and encodes a polypeptide sequence identical to that of UbcH7.

Proteasome subunit alpha type 4 (PSMA4) belongs to the peptidase T1A family, which is a 20S core alpha subunit. The proteasome is a multicatalytic proteinase complex with an extremely ordered ring-shaped 20S core structure. The core structure is comprised of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. PSMA4 is dispersed throughout eukaryotic cells at a high concentration and cleaves peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway.

The proteasome is a multicatalytic proteinase complex with an extremely organized ring-shaped 20S core structure. The core structure consists of 4 rings of 28 non-identical subunits; 2 rings consist of 7 alpha subunits and 2 rings consist of 7 beta subunits. Proteasomes are spread all over the eukaryotic cells in large quantities and cleave peptides in an ATP/ubiquitin-dependent procedure in a non-lysosomal pathway. A vital role of a modified proteasome, the immunoproteasome, is the handling of class I MHC peptides.

T5 Exonuclease is an important enzyme that belongs to the family of exonucleases and plays a vital role in DNA metabolism and genetic engineering. This research paper aims to provide an overview of T5 Exonuclease, including its structure, function, and diverse applications in molecular biology.

T5 Exonuclease is derived from the bacteriophage T5, and it possesses a remarkable ability to selectively degrade single-stranded DNA in a 5' to 3' direction. It is a highly processive enzyme, meaning it can cleave multiple nucleotides consecutively without dissociating from the DNA substrate. The enzyme exhibits high specificity for single-stranded DNA, making it a valuable tool for various molecular biology applications.

The primary function of T5 Exonuclease is to remove nucleotides from the 5' ends of single-stranded DNA molecules. By digesting DNA in a processive manner, T5 Exonuclease is involved in DNA repair mechanisms, such as the removal of damaged or mismatched nucleotides. It is also widely utilized in molecular cloning techniques to generate DNA fragments with precise ends for subsequent DNA ligation reactions.

Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis. Kallikrein-11 (KLK11) which is a multifunctional protease is 1 of the 15 kallikrein subfamily members found in a cluster on chromosome 19. KLK11 cleaves synthetic peptides after arginine but not lysine residues.

Peroxisomal 2,4-dienoyl-CoA reductase (DECR2) is an supporting enzyme of beta-oxidation. DECR2 partakes in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. DECR2 catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.

Peptidyl-prolyl cis-trans isomerase-like 3 (PPIL3) belongs to the cyclophilin family which catalyzes the cis-trans isomerization of peptidylprolyl imide bonds in oligopeptides. PPIL3 acts either as catalyst or as molecular chaperone in protein-folding events.

Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

PDIA4 is an endoplasmic reticulum luminal protein that is a stress protein as well as a member of the protein disulfide isomerase family of proteins. PDIA4 participates in the catalysis of protein-S-S-bond rearrangement. PDIA4 and PDIA3 function as proteases, protein disulfide isomerases, phospholipases or an arrangement of these.

Neuron-specificenolase also caled NSE is a glycolytic isoenzyme which is situated in central and peripheral neurons and neuroendocrine cells. Enolase-2 is released into the CSF when neural tissue is injured. Neoplasms derived from neural or neuroendocrine tissue release Enolase-2 into the blood. Enolase-2 is a useful substance that has been detected in patients with certain tumors, such as neuroblastoma, small cell lung cancer, medullary thyroid cancer, carcinoid tumors, pancreatic endocrine tumors, and melanoma. ENO2 is 1 of the 3 enolase isoenzymes found in mammals. ENO2 isoenzyme, is found in mature neurons and cells of neuronal origin. An exchange from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates.

Pyruvate Dehydrogenase Complex, Component X, also known as PDHX, encodes the E3 binding protein subunit of the PDH complex which contains 3 catalytic subunits. PDHX tethers E3 dimers to the E2 core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is critical for a functional PDH complex.

AKR1A1 is part of the aldo/keto reductase superfamily, it catalyzes the NADPH-dependent reduction from a range of aromatic and aliphatic aldehydes to their related alcohols. AKR1A1 corresponds (65% identity) to aldose reductase, an enzyme that takes part in the pathogenesis of some diabetic and galactosemic complications. AKR1A1 is involved in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs.

TRXR is a ubiquitous enzyme which participates in various cellular processes such as cell growth, p53 activity, and protection against oxidation stress. The mammalian Thioredoxin reductase cleaves thioredoxins as well as non-disulfide substrates such as selenite, lipoic acids, lipid hydroperoxides, and hydrogen peroxidec.

Thymidine phosphorylase precursor (TYMP) is a platelet-derived endothelial cell growth factor that catalyzes the formation of thymine and 2-deoxy-D-ribose-1-phosphate from thymidine and orthophosphate. TYMP is an angiogenic inducer that potently stimulates the growth of endothelial cells and induces chemotaxis. TYMP has a highly restricted target cell specificity acting only on endothelial cells. An increased expression of TYMP is found in a broad array of different solid tumors and inflammatory diseases and is frequently associated with poor prognosis. Mutations in the TYMP gene are linked to mitochondrial neurogastrointestinal encephalomyopathy.

GPD1 enzyme catalyzes the reduction of dihydroxyacetone phosphate to sn-glycerol 3-phosphate. (sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH) previous names for glycerol-3-phosphate dehydrogenase include alpha glycerol-3-phosphate dehydrogenase and glycerolphosphate dehydrogenase. However, GPD1 differs from glyceraldehyde 3-phosphate dehydrogenase (GAPDH) whose substrate is an aldehyde not an alcohol.

AKR7A3, takes part in the detoxification of aldehydes and ketones. AKR7A3 reduces the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. AKR7A3 participates in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

DUSPs are distinguished by their ability to dephosphorylate both tyrosine and serine/threonine residues. DUSPs have been implicated as major modulators of critical signaling pathways. Dual specificity phosphatase 19 (DUSP19) belongs to the dual specificity protein phosphatase subfamily. DUSP19 is a protein phosphatase which functions as a stress-activated protein kinase pathway-regulating phosphatase. DUSP19 contains a variation of the consensus DUSP C-terminal catalytic domain, with the last serine residue replaced by alanine, and lacks the N-terminal CH2 domain found in the MKP class of DUSPs.

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.

ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial isozyme. ALDH2 has a low Km for acetaldehydes, and is localized in mitochondrial matrix.

Leucine Aminopeptidase 3 also known as LAP3 is a member of the peptidase M17 family. LAP3 is implicated in the processing as well as regular turnover of intracellular proteins. LAP3 catalyzes the removal of unsubstituted N-terminal amino acids from different peptides. LAP3 is responsible of releasing an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but could be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are as well readily hydrolyzed; however rates on arylamides are exceedingly low.

PTGES3 takes part as a cochaperone and is involved in signal transduction.
PTGES3 is a molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexess. PTGES3 is necessary for appropriate functioning of the glucocorticoid and other steroid receptors.
PTGES3 localizes to genomic response elements in a hormone-dependent method and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes.