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Thiosulfate sulfurtransferase like domain containing 1 (TSTD1) is a member of a family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. TSTD1 is localized around the nuclear membranes. TSTD1 is expressed in a number of human tissues, including the kidney, liver, skeletal muscle, heart, colon, thymus, spleen, placenta and lung. TSTD1 may participate in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes.

GSTM3 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The mu type of enzymes takes part in the detoxification of electrophilic compounds, including therapeutic drugs, carcinogens, environmental toxins and products of oxidative stress, by conjugation with glutathione.

NUDT10 belongs to the Nudix hydrolase family of pyrophosphatases. Nudix hydrolases contain a characteristic Nudix domain and are responsible for catalyzing the hydrolysis of nucleoside diphosphate derivatives. NUDT10 functions as a manganese-dependent polyphosphate phosphohydrolase with an optimum pH of 8.5. NUDT10 protein specifically metabolizes diadendosine-polyphosphates and, to a lesser extent, diphosphoinositol polyphosphates.

Placental alkaline phosphatase (PLAP) is a membrane-associated siaglycoprotein enzyme normally present at high concentration in syncytiotrophoblasts within the placenta during the third trimester of gestation. The expression of PLAP was originally thought to be restricted to term placenta but a human PLAP-like variant has been described which shares more than 85% homology with PLAP itself. PLAP is expressed only in normal term placenta, endocervix and fallopian tube and also in ovarian and proximal gastrointestinal tumors. It is also commonly expressed in germ cell tumors and more recently described in seminomas.

Epoxide Hydrolase 1 Microsomal (EPHX1) is a vital biotransformation enzyme which transfers epoxides from the degradation of aromatic compounds to trans-dihydrodiols that can be conjugated and excreted from the body. Epoxide hydrolase plays a role in both activation and detoxification of epoxides. Mutations in EPHX1 trigger preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity.

LYPLA1 is lysophospholipase which performs on biological membranes to regulate the multifunctional lysophospholipids. LYPLA1 protein hydrolyzes fatty acids from S-acylated cysteine residues in proteins like trimeric G alpha proteins or HRAS and in addition has depalmitoylating activity.

AK4 belongs to the adenylate kinase family of enzymes. AK4 protein is restricted to the mitochondrial matrix. Adenylate kinases regulate the adenine and guanine nucleotide structures in a cell by catalyzing the reversible transfer of phosphate group among these nucleotides. Hereditary mutations which cause AK4 deficiencies in erythrocytes have been associated to hemolytic anemia.

UBE2D2 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2D2 takes part in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. UBE2D2 catalyzes ubiquitination of IkB-alpha in a SCFB-TRCP and phosphorylation dependent method.

MMP10 (Matrix Metallopeptidase 10) which is a part of the matrix metalloproteinase (MMP) is activating procollagenase. MMP10 is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP10 takes part in the breakdown of extracellular matrix in normal physiological processes, like embryonic development, reproduction, and tissue remodeling, as also in disease processes, such as arthritis and metastasis. The majority MMP's are secreted as inactive proproteins that are activated when cleaved by extracellular proteinases. MMP10 encodes an enzyme which degrades proteoglycans and fibronectin.

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.

NEDD8-activating enzyme E1 catalytic subunit (UBA3) is the catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme, which belongs to the E1 ubiquitin-activating enzyme family. E1 activates NEDD8 by initially adenylating its C-terminal glycine residue with ATP, afterwards linking this residue to the side chain of the catalytic cysteine, generating a NEDD8-UBA3 thioester and free AMP. E1 at last transfers NEDD8 to the catalytic cysteine of UBE2M. The UBA3 enzyme connects with AppBp1, an amyloid beta precursor protein binding protein, to form a heterodimer, and at that point the enzyme complex activates NEDD8, a ubiquitin-like protein, which controls cell division, signaling and embryogenesis.

UCK1 is a uridine-cytidine kinase which catalyzes the phosphorylation of uridine and cytidine to uridine monophosphate and cytidine monophosphate. UCK1 does not phosphorylate deoxyribonucleosides or purine ribonucleosides. UCK1 is also phosphorylates uridine and cytidine analogs and uses ATP and GTP as a phosphate donor.

Glutamate Decarboxylase 1 Isoform-1, also known as GAD1 iso1 belongs to the group II decarboxylase family. GAD1 iso1 encodes one of several forms of glutamic acid decarboxylase, and is identified as a major autoantigen in insulin-dependent diabetes. GAD1 iso1 is in charge for catalyzing the production of gamma-aminobutyric acid from L-glutamic acid. In addition, a pathogenic function for GAD1 iso1 has been shown in the human pancreas while it has been identified as an autoantigen & an autoreactive T cell target in insulin-dependent diabetes. GAD1 iso1 play a role in the stiff man syndrome. It has been shown that deficiency in this enzyme has led to pyridoxine dependency with seizures.

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.

Akt1, also known as "Akt" or protein kinaseB (PKB) is an important molecule in mammaliancellular signaling.
In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. These enzymesare members of the serine/threonine-specific protein kinasefamily (EC2.7.11.1).
Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesispathways, and is therefore a key signaling protein in the cellular pathways that lead to skeletal muscle hypertrophy, and general tissue growth. Since it can block apoptosis, and thereby promote cell survival, Akt1 has been implicated as a major factor in many types of cancer. Akt (now also called Akt1) was originally identified as the oncogenein the transforming retrovirus, AKT8.

GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells.

Angiotensin Converting Enzyme (ACE) is a zinc metallopeptidase vital for blood pressure control and salt and water metabolism.ACE converts angiotensin I to angiotensin II by release of the terminal His-Leu which causes the vasoconstrictor activity of angiotensin to increase.ACE inactivates bradykinin, a potent vasodilator and has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.

Aldo-keto reductase family 1 member C4 or AKR1C4 is a part of the aldo/keto reductase superfamily that has more then 40 known proteins & enzymes. AKR1C4 catalyzes the conversion of aldehydes and ketones to their corresponding alcohols with NADH and/or NADPH as cofactors. AKR1C4 takes place in the bioreduction of chlordecone, a toxic organochlorine pesticide, to chlordecone alcohol in the liver tissue.

Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

PLA2G7 is a secreted enzyme which catalyzes the degradation of platelet-activating factor to biologically inactive products. The PLA2G7 enzyme is produced by inflammatory cells and hydrolyzes oxidised phospholipids in LDL. In the blood, PLA2G7 goes mainly with LDL and less than 20% is coupled with HDL.
PLA2G7 is implicated in the development of atherosclerosis and is also a marker for cardiac disease. PLA2G7 might have a major physiologic effect in the presence of inflammatory bodily responses.
PLA2G7 alters the action of PAF (platelet-activating factor) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. PLA2G7 has specificity for substrates with a short residue at the sn-2 position. PLA2G7 is inactive against long-chain phospholipids.
PLA2G7 gene defects are the source of platelet-activating factor acetylhydrolase deficiency, which is a trait that is present in 27% of the Japanese population.

PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
The PRMT1 protein functions as a histone methyltransferase specific for H4.
PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
CAF1 is a new regulator of PRMT1-dependent arginine methylation.
PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
PRMT1 plays a post-translationally part in regulating the transcriptional activity.
PRMT1is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells.