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LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is localized primarily in muscle tissue and is part of the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. LDH1 is decreased in essential thrombocythemia. LDHA is induced through a non-genomic pathway of estrogen action. Reduction in LDH-A activity results in stimulation of mitochondrial respiration and decrease of mitochondrial membrane potential.

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.

Alkaline Phosphatase Liver/Bone/Kidney (Alpl) is a part of the alkaline phosphatases family which comprises 4 related alkaline phosphatases. Alpl is a membrane-bound glycosylated enzyme which is not expressed in any particular tissue. Alpl takes part in skeletal mineralization.

Lactate dehydrogenase (LDH) is an enzyme(EC1.1.1.27) present in a wide variety of organisms, including plants and animals.
A tetrameric enzyme that catalyses the interconversion of pyruvateand lactate with concomitant interconversion of NADH and NAD+. At high concentrations of pyruvate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.

Dehydrogenase/reductase SDR family member 4 (DHRS4) is a member of the short-chain dehydrogenases/reductases (SDR) family. DHRS4 reduces all trans retinal and 9-cis retinal. In addition, the DHRS4 protein can catalyze the oxidation of all trans retinol with NADP as cofactor, but with a much lower efficiency. Furthermore, DHRS4 reduces alkyl phenyl ketones and alpha dicarbonyl compounds with aromatic rings, such as pyrimidine 4 aldehyde, 3 benzoylpyridine, 4 benzoylpyridine, menadione and 4 hexanoylpyridine.

LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is localized primarily in muscle tissue and is part of the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. LDH1 is decreased in essential thrombocythemia. LDHA is induced through a non-genomic pathway of estrogen action. Reduction in LDH-A activity results in stimulation of mitochondrial respiration and decrease of mitochondrial membrane potential.

BAG1 binds to BCL2 and is also called BCL2-associated athanogene. BAG1 increases the anti-apoptotic effects of BCL2 and is characterizes as a link between growth factor receptors and anti-apoptotic mechanisms. BAG1 inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. BAG1 inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. BAG1 enhances the anti-cell death function of BCL2 induced by various stimuli.

SORD enzyme is part of of the zinc-containing alcohol dehydrogenase family that is broadly expressed in kidney and in the lens eye. SORD enzymatically catalyzes the zinc-dependent interconversion of polyols, such as sorbitol and xylitol, to their respective ketoses.

Akt1, also known as Akt or else protein kinase B (PKB) is an important molecule in mammaliancellular signaling. In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. Moreover, these enzymes are members of the serine/threonine-specific protein kinase family (EC2.7.11.1). Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesis pathways, and is therefore a key signaling protein in the cellular pathways which 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 most important factor in numerous types of cancer. Akt (now also called Akt1) was at first identified as the oncogenein the transforming retrovirus, AKT8.

BCAT1 catalyzes the leading reaction in the catabolism of the indispensable branched chain amino acids isoleucine, leucine and valine.

GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.

Immature Colon Carcinoma Transcript 1 (ICT1) functions as a codon-independent translation release factor that has lost all stop codon specificity and leads the termination of translation in mitochondrion in case of abortive elongation. The mature colon epithelium has 3 differentiated cell types which arise from a multipotent stem cell. ICT1 is involved in the hydrolysis of peptidyl-tRNAs which have been prematurely terminated and consequently in the recycling of stalled mitochondrial ribosomes. Digression from the normal maturation pathway by neoplastic transformation is assumed to originate in stem cells or their early descendants.

Polypeptide N-Acetylgalactosaminyltransferase 1 (Galnt1) , is part of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. The initial reaction in O-linked oligosaccharide biosynthesis is catalyzed by Glant1, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Moreover, Galnt1 is implicated in the glycosylation of proteins vital for bone formation for instance osteopontin and bone sialoprotein.

Pyruvate kinase is a key enzyme in the glycolytic pathway. The M2 isoenzyme of pyruvate kinase is specifically expressed at high levels in tumor cells, and can be measured in plasma of patients with advanced breast cancer. The marker is useful for measuring disease activity, sensitivity to chemotherapy and recurrence.

GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.

ST6GAL1 also known as ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, is part of the glycosyltransferase family 29. ST6GAL1 is a type II membrane protein which catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. Furthermore, ST6GAL1 is normally found in the Golgi however it can be proteolytically processed to a soluble form, ST6GAL1 is also involved in the generation of the cell-surface carbohydrate determinants as well differentiation antigens HB-6, CD75, and CD76.

Fructosamine 3 Kinase (FN3K) catalyzes the phosphorylation of fructosamines which may result in deglycation, the non-enzymatic reaction of glucose with primary amines followed by Amadori re-arrangement. Phosphorylation of fructosamines instigates metabolism of the modified amine and brings about the de-glycation of fructoselysine and of glycated proteins. A high concentration of glucose may affect non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). Fructosamines, the proteins altered in this way, are less active or functional.

Carboxylesterase 1D, also known as CES1D is part of a big family of carboxylesterases which are responsible for the hydrolysis of ester in addition to amide bonds. CES1D is the principle lipase of white adipose tissue fat cake extracts. Partially purified white adipose tissue Ces1d had lipase activity in addition to lesser but detectable neutral cholesteryl ester hydrolase activity. CES1D demonstrates low catalytic efficiency for hydrolysis of CPT-11, a prodrugs for camptothecin used in cancer therapeutics.

PRDX4 is an antioxidant enzyme that is part of the peroxiredoxin family. PRDX4 is localized to the cytoplasm. PRDX4 reduces hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. PRDX4 has a regulatory part in the activation of the transcription factor NF-kappaB. PRDX4 participates in redox regulation of the cell. PRDX4 regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.

NFATC1 is a component of the nuclear factor of activated T cells DNA-binding transcription complex. This complex consists of at least 2 components: a preexisting cytosolic component that translocates to the nucleus upon T cell receptor (TCR) stimulation, and an inducible nuclear component. Proteins belonging to this family of transcription factors play an essential role in inducible gene transcription during immune response. NFATC1 is an inducible nuclear component. NFATC1 functions as a major molecular target for the immunosuppressive drugs such as cyclosporin A. Different isoforms of NFATC1 may regulate inducible expression of different cytokine genes.

PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.

AKR1B1 is part of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. AKR1B1 catalyzes the reduction several aldehydes, including the aldehyde form of glucose, and thus involved in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. AKR1B1 catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Transgenic mice over expressing human aldose reductase show that AKR1B1 is a key player in ischemic injury and impairment of functional and metabolic recovery after ischemia. Aldose Reductase is an obligatory mediator of TNF-alpha signaling leading to an increase in the expression of adhesion molecules and increased binding of monocytes to the endothelium. AKR1B1 is a critical regulator of TNF-alpha-induced apoptotic signaling in endothelial cells.