Search results

HDAC2 is a member of the histone deacetylase family that performs through the construction of large multiprotein complexes and are in charge of the deacetylation of lysine residues on the N-terminal region of the core histones. HDAC2 forms transcriptional repressor complexes by relating to a diversity of proteins, like YY1- a mammalian zinc-finger transcription factor.
In addition, HDAC2 has a vital part in transcriptional regulation, cell cycle progression and developmental procedures.

GMP synthase (GMPS) is involved in purine biosynthesis. GMPS, which is a homodimer, catalyzes the last step in the GMP synthesis pathway, specifically the ATP-dependent amination of XMP to GMP. GMPS is comprised of one GMP-binding domain and one glutamine amidotransferase type-1 domain through which it communicates its catalytic activity. GMPS is engaged in the de novo synthesis of nucleotides which are not only vital for DNA and RNA synthesis, but also supply GTP, which is involved in sevral cellular processes important for cell division. GMPS gene chromosomal translocations are linked with acute myeloid leukemias, suggesting a possible role for GMPS in carcinogenesis.

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.

Uridine diphosphate glucose pyrophosphatase (NUDT14), is a part of the nudix hydrolase family. NUDT14 is a cytoplasmic protein which contains one nudix hydrolase domain and acts as the sugar donor in numerous glycosylation reactions, including those involved in the production of glycogen. NUDT14 hydrolyzes ADP-ribose into ribose 5-phosphate and AMP, and UDP-glucose to glucose 1-phosphate and UMP. NUDT14 is a homodimer which binds magnesium as a cofactor and is encoded by a gene located on human chromosome 14.

NUDT5 is part of the nudix hydrolase family which remove toxic nucleotide derivatives from the cell. NUDT5 hydrolyzes ADP-ribose and ADP-mannose in the presence of magnesium, and in addition hydrolyzes nucleotide sugars with decreasing activity such as ADP-glucose and diadenosine diphosphate. As a nudix hydrolase, NUDT5 holds a central nudix motif and functions to eliminate toxic nucleotide metabolites from the cell while maintaining the levels of signaling nucleotides.
NUDT5 is broadly expressed but is most abundant in liver as a homodimer.

Enolase-phosphatase E1 (ENOPH1) belongs to the MasA family of the HAD (halo-acid dehalogenase)-like hydrolase superfamily. ENOPH1 is a bifunctional enzyme which demonstrates both phosphatase and atypical enolase activities. ENOPH1 has a significant role in the ubiquitous methionine salvage pathway which is a biochemical pathway found in all organisms that regulate methionine levels in the cell.

THAP domain-containing protein 1 (THAP1) is a 213 amino acid protein which is restricted to the nucleoplasm and contains one THAPtype zinc finger, a conserved DNA-binding domain. THAP1 is a DNA-binding transcription regulator which regulates endothelial cell proliferation and G1/S cell-cycle progression. In addition, THAP1 has a pro-apoptopic activity by potentiating both serum-withdrawal and TNF-induced apoptosis. THAP1 protein colocalizes with the apoptosis response protein PAWR/PAR-4 in promyelocytic leukemia (PML) nuclear bodies, and serves as a proapoptotic factor which connects PAWR to PML nuclear bodies.

TPI1 is one of the triosephosphate isomerase family. TPI1 catalyzes the isomerization of glyceraldehydes 3-phosphate (G3P) and dihydroxy-acetone phosphate (DHAP) in glycolysis and gluconeogenesis. Mutations in TPI1 causes triosephosphate isomerase deficiency (TPI deficiency). TPI deficiency is an autosomal recessive disorder which is the most severe clinical disorder of glycolysis and is related to neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.

GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 is invloved in amino acid metabolism and the urea and tricarboxylic acid cycles. The 2 enzymes are homodimeric and demonstrate close homology.

Magnesium-dependent phosphatase 1 (MDP1) is a memeber of the HAD-like hydrolase superfamily. MDP1 is a magnesium-dependent phosphatase which may act as a tyrosine phosphatase. MDP1 is inhibited by vanadate and zinc, and slightly by calcium.

HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.

PAPSS1 is a bifunctional enzyme with APS kinase and ATP sulfurylase activity. PAPSS1 facilitates two stages in the sulfate activation pathway, yielding 3'-phosphoadenylylsulfate (PAPS). Additionally, PAPSS1 takes part in the biosynthesis of sulfated L-selectin ligands in endothelial cells.

Caspase 2 Apoptosis-Related Cysteine Peptidase (CASP2) is a part of the cysteine-aspartic acid protease (caspase) family. CASP2 takes part in the activation cascade of caspases responsible for apoptosis execution. CASP2 is also responsible for inactivating proteins essential for cell survival. The proteolytic cleavage of CASP2 is induced by a variety of apoptotic stimuli.

Inorganic pyrophosphatase (ppa) is a member of the Ppase family. PPA is an enzyme which catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Since this is a highly exergonic reaction, it can therefore be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The role of the PPA enzyme is a critical one in the lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, DNA synthesis, as well as other biochemical transformations.

MAT2B is part of the methionine adenosyltransferase family. MAT2B catalyzes the biosynthesis of S-adenosylmethionine from methionine and ATP. MAT2B is the regulatory beta subunit of MAT. MAT2B expression in hepatoma cell lines increases DNA synthesis and thus take part in cell proliferation.

ACP1 is part of the phosphotyrosine protein. ACP1 functions as an acid phosphatase and a protein tyrosine phosphatase (PTPase) existing in all human tissues, including adipocytes. ACP1 enzyme hydrolyzes protein tyrosine phosphate to protein tyrosine and orthophosphate, and also orthophosphoric monoesters to alcohol and orthophosphate. ACP1 is present in adipocytes, thus playing a specific role in the regulation of adipose tissue. High levels of the ACP1 negatively regulate cell proliferation and growth of leiomyomas during dephosphorylation of the PDGF receptor. High significant differences in birth weight-placental weight relationships were observed among acid phosphatase locus 1 phenotypes.

Membrane Metalloendopeptidase, also known as MME is a zinc metallopeptidase which is expressed at the cell surface of various cells. MME degrades the amyloid beta peptide whose abnormal misfolding as well as aggregation in neural tissue has been implicated as the cause for Alzheimer's disease. MME is expressed in an extended range of tissues and is especially plentiful in the kidney. MME is also a common acute lymphocytic leukemia antigen which is a significant cell surface marker in the diagnosis of human acute lymphocytic leukemia (ALL). MME is used in hematological diagnosis because it is expressed by early B, pro-B and pre-B lymphocytes, and also by lymph node germinal centers.

GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.

Nicotinamide Nucleotide Adenylyltransferase 2, also known as NMNAT2 is a member of the nicotinamide mononucleotide adenylyltransferase (NMNAT) enzyme family, members of which catalyze a vital step in NAD (NADP) biosynthetic pathway. Unlike the other human family member, which is localized to the nucleus, and is ubiquitously expressed; NMNAT2 is cytoplasmic, and is predominantly expressed in the brain. Two transcript variants encoding different isoforms have been found for NMNAT2. Among the diseases associated with NMNAT2 are tauopathy, and systemic lupus erythematosus.

Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.

Fumarase is an enzymatic factor of Krebs cycle, which catalyzes the formation of L-malate from fumarate. Fumarase exists in both a cytosolic form and an N-terminal extended form, differing only in the translation start site used. The N-terminal extended form is aimed to the mitochondrion, where the removal of the extension results in the same form as in the cytoplasm. Fumarase is similar to a number of thermostable Class-2 fumarases and functions as a homotetramer. Mutations in the Fumarase gene causes fumarase deficiency and leads to progressive encephalopathy, cerebral atrophy and developmental delay. Fumarase enzyme is also thought to act as a tumor suppressor. Leydig cell tumors are caused by Fumarase mutations and represents one of the first reports of germline mutations in any type of adult testicular tumor.

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.