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Glutaminyl-Peptide Cyclotransferase, also known as QPCT is a member of the glutaminyl-peptide cyclotransferase family. QPCT is responsible for the biosynthesis of pyroglutamyl peptides. Furthermore, QPCT is partial against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length following the second residue. QPCT catalyzes N-terminal pyroglutamate formation, also in vitro, it catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid.

Cyclophilin-C belongs to the peptidyl-prolyl cis-trans isomerase (PPIase)) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Like other PPIases, the Cyclophilin-C protein can bind immunosuppressant cyclosporin A.

Cystathionine gamma-lyase or cystathionase (CTH) is a member of the trans-sulfuration enzymes family. CTH is an enzyme which breaks down cystathionine into cysteine and alpha-ketobutyrate. The CTH catalyzes the last step in the transsulfuration pathway from methionine to cysteine. Glutathione synthesis in the liver is dependent upon the availability of cysteine. Mutations in the CTH gene cause cystathioninuria.

AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.

Serpin Peptidase Inhibitor, Clade D Member 1 (SERPIND1) is a serine proteinase inhibitor which rapidly inhibits thrombin in the presence of dermatan sulfate. SERPIND1 gene is a member of the serpin gene superfamily. SERPIND1 protein contains 5 exons and 4 introns. SERPIND1 shares homology with antithrombin III and other members of the alpha 1-antitrypsin superfamily. SERPIND1 gene mutations are linked with cofactor II deficiency. SERPIND1 protein is activated by dermatan sulfate, and glycosaminoglycans. Allelic variations in the SERPIND1 gene are linked with cofactor II deficiency.

DTD2 is e member of the DTD family. DTD2 protein hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr) as a defense mechanism against a harmful effect of D-tyrosine.

ATPase Transporting, Lysosomal V1 Subunit F (ATP6V1F) is a component of vacuolar ATPase (V-ATPase); it is a multi-subunit enzyme, which mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is required for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is comprised of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain contains 3 A and 3 B subunits, 2 G subunits as well as the C, D, E, F, and H subunits. The V1 domain has the ATP catalytic site. The V0 domain consists of 5 different subunits: a, c, c', c', and d.

Peptidase D, also known as PEPD, Is a part of the peptidase family. PEPD is involved in collagen metabolism due to the high level of iminoacids in collagen. PEPD recycles proline, and sets the pace for the production of collagen. PEPD is also parts dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position.

KLK7 catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. KLK7 is involved in the activation of precursors to inflammatory cytokines.

PPIL1 belongs to the cyclophilin family of peptidylprolyl isomerases (PPIases).
The cyclophilins are a well conserved, ubiquitous family, members of which take an significant part in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL1 protein increases the folding of proteins and catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIL1 is involved in proliferation of cancer cells through modulation of phosphorylation of stathmin. PPIL1 is a novel molecular target for colon-cancer therapy.

Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.

Thyroid Hormone Receptor Interactor 10 (TRIP10) is a part of the F-BAR family of proteins which is expressed in a variety of tissues, including kidney, brain, liver, lung, heart and pancreas. The F-BAR family of proteins contains an N-terminal, alpha-helical, region which is hydrophobic and related to the Bin Amphiphysin Rvs (BAR) protein family. TRIP10 is vital for the coordination of membrane tubulation with Actin cytoskeletal reorganization during endocytosis.

GSTZ1 is part of the glutathione S-transferase super-family which encodes multifunctional enzymes vital in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. GSTZ1 participates in the catabolism of phenylalanine and tyrosine. Thus defects in GSTZ1 cause harsh metabolic disorders including alkaptonuria, phenylketonuria and tyrosinaemia. GSTZ1 is a bifunctional protein which has minimal glutathione-conjugating activity with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. GSTZ1 has low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. GSTZ1 catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.

Chitodextrinase is a unique membrane-bound endoenzyme. The chitodextrinase enzyme cleaves soluble oligomers, but not chitin, to the di- and trisaccharides. Chitodextrinase is unable to solubilize chitin, but it can catalyze the hydrolysis of high to low molecular weight soluble chitin oligosaccharides.

Serine/threonine/tyrosine-interacting protein (STYX) is a member of the protein-tyrosine phosphatase family. STYX contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which makes it catalytically inactive as a phosphatase. On the other hand, the binding pocket is adequately preserved to bind phosphorylated substrates, and may protect them from phosphatases. STYX may have a role in spermiogenesis. STYX is a possible pseudophosphatase.

PAPPA is a large zinc binding protein, which plays a role as a metalloprotease and specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. PAPP-A regulates IGF bioactivity in various biological systems, including the human ovary and cardiovascular systems. PAPP A levels were higher in patients with unstable angina or acute myocardial infarction. PAPPA is also involved in local proliferative processes such as wound healing and bone remodeling. Moreover, PAPP-A is produced in high concentrations during pregnancy and is released into the maternal circulation. In placenta, PAPP A is expressed in X cells in septa and anchoring villi, and in syncytiotrophoblasts in the chorionic villi.

ACAA1 is part of the thiolase family of enzymes and is takes part in lipid metabolism. ACAA1 enzyme is localized to the peroxisome and catalyzes the conversion of acyl-CoA and acetyl-CoA to 3-oxoacyl-CoA in the fatty acid oxidation pathway. ACAA1 shows high enzymatic activity in liver, kidney, intestine and white adipose tissue in rats. ACAA1 deficiency causes pseudo-Zellweger syndrome.

Haloacid dehalogenase-like hydrolase domain-containing protein 1A (HDHD1A) is a member of the adiponutrin family. HDHD1A is interesting because it is an X-linked gene that escapes X-inactivation. HDHD1A is particularly important in the perception of human X chromosome structural organization as well as the mechanism of X-inactivation.

DARS uses a 2 step reaction to catalyze the specific attachment of an amino acid to its cognate tRNA: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.

N-acetylneuraminate lyase (NanA) is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NanA catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine. NanA is inhibited by reduction with NaBH4 in the presence of the substrate, which indicates that it belongs to the Schiff-base-forming Class I aldolases. NanA is strongly inhibited by Cu2+ ions, p-chloromercuribenzoate and N-bromosuccinimide, it is also inhibited competitively by the reaction product, pyruvate, and its structurally related compounds, dihydroxyacetone and DL-glyceraldehyde.

Beta-secretase 1 or BACE1 or beta-site amyloid precursor protein cleaving enzyme 1, is a protein that is encoded by the BACE1 gene in humans. Expression of BACE1 is seen primarily in neurons as it is crucial for the creation of myelin sheats in the peripheric nervous system. Beta-secretase 1 is a proteas that is located in the cell membrane (transmembrane). The enzyme consists of 2 active sites (aspartate residues) in the extracellular domain that can act as a dimer.

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.

CA8 was first called CA-related protein since there is a sequence similarity to other identified carbonic anhydrase genes. Still, this protein has no carbonic anhydrase activity - the reversible hydration of carbon dioxide. CA8 still holds a carbonic anhydrase designation due to obvious sequence similarity to other members of the carbonic anhydrase gene family. Mutations in CA8 result in cerebellar ataxia mental retardation and dysequilibrium syndrome type 3 (CMARQ3).