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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.

Ketosamine-3-kinase (FN3KRP) catalyzes the phosphorylation of psicosamines and ribulosamines compared to the adjacent gene which encodes a highly analogous enzyme, fructosamine-3-kinase that has different substrate specificity. The activity of both enzymes may cause deglycation of proteins to reinstate their function. A high concentration of glucose can result in non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). The proteins altered in this way, are less active or functional.

PFKM is a regulatory glycolytic enzyme that converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. Mutations in PFKM gene have been related with glycogen storage disease type VII, also identified as Tarui disease.

NAGK is a member of the eukaryotic-type N-acetylglucosamine kinase family. NAGK converts endogenous N-acetylglucosamine (GlcNAc), a key component of complex carbohydrates, from lysosomal degradation or alimentary sources into GlcNAc 6-phosphate. NAGK is a prominent salvage enzyme of amino sugar metabolism in mammals. NAGK cooperates with STK16 and LNX1 and has ManNAc kinase activity.

PFKM is a regulatory glycolytic enzyme that converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. Mutations in PFKM gene have been related with glycogen storage disease type VII, also identified as Tarui disease.

Thermosensitive Gluconokinase, also known as IDNK is a 187 a.a protein which is a member of the gluconokinase gntK/gntV family. IDNK catalyzes theconversion of ATP and D-gluconate to ADP and 6-phospho-D-gluconate. In addition, IDNK is considered to take part in gender determination, deletion of the distal portion of 9p is able to lead to a development of male to female sex reversal, the phenotype of a female with a male X, Y genotype.

Glucokinase also known as GLK is a member of the bacterial glucokinase family. GLK is not highly significant in E.coli since glucoseis already transported into the cell through the PTS system as glucose 6-phosphate.

GSK3B is a serine-threonine kinase that belongs to the glycogen synthase kinase subfamily. GSK3B is involved in energy metabolism, neuronal cell development, and body pattern formation. Polymorphisms in the GSK3B gene have been implicated in modifying risk of Parkinson disease, and studies in mice show that overexpression of the GSK3B gene may be significant to the pathogenesis of Alzheimer disease.

Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. HK3 encodes hexokinase 3. Similar to hexokinases 1 and 2, this allosteric enzyme is inhibited by its product glucose-6-phosphate. Hexokinase3 lacks the hydrophobic N-terminal sequence critical for targeting to mitochondria. Hexpkinase3 may have anabolic functions, providing H6P for glycogen or lipid synthesis.

The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

Gastrokine 3 (GKN3P) is a Pseudogene, which May inhibit gastric epithelial cell proliferation.

Tribbles Pseudokinase 3, also known as TRIB3, is a putative protein kinase which is induced by the transcription factor NF-kappaB. In addition, TRIB3 is a negative regulator of NF-kappaB, and can as well sensitize cells to TNF- and TRAIL-induced apoptosis. Furthermore, TRIB3 is able to negatively regulate the cell survival serine-threonine kinase AKT1. One of the diseases which are associated with TRIB3 is anoxia.

The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

P85a functions as the regulatory subunit of the class IA PI3-kinase isoforms a, b, and d.
It contains two SH2 domains that bind to tyrosine-phosphorylated growth factor receptors or substrate adaptor proteins.
It also contains a BH (breakpoint cluster region homology) domain that shows GAP activity towards the small GTPases Rab4, Rab5, Cdc42, Rac1 and to a lesser extend towards Rab6 and Rab11.
It was shown that PI3Ka catalytic subunit mediated phosphorylation of the p85a adapter reduces the lipid kinase activity of the heterodimer and this gives hints for PI3K-dependent signaling events not requiring production of 3’-phosphorylated phosphoinositides.
PI3Ka protein kinase activity has been implicated in IRS-1 serine phosphorylation in insulin-treated adipocytes and in STAT3 and IRS-1 phosphorylation upon activation of the type 1 IFN receptor by IFN-a.

GlpK also known as glycerol kinase, is a member of the FGGY kinase family. GlpK catalyzes the transfer of a phosphate group from ATP to glycerol, thereby forming glycerol phosphate. Furthermore, this intermediate can then be converted to dihydroxyacetone phosphate (DHAP), which is utilized in either glycolysis or gluconeogenesis. The activity of GlpK is affected by numerous metabolites. The non-competitive allosteric inhibition by fructose 1,6-bisphosphate (FBP) triggers modifications in the quaternary structure of Glpk.

Serine/threonine-protein kinase 3 (), is a mammalian Ste20-related protein kinases most closely related to Drosophila Hippo, which is a major regulator of cell proliferation as well as survival in the course of development. STK3 is a serine/threonine kinase which functions early in a pheromone responsive signal transduction cascade in yeast. Furthermore, STK3 activates the human large tumor suppressor kinase Lats1. STK3 also modulates stress-induced cardiac hypertrophy.

MAP kinase-activated protein kinase 3 (MAPKAPK3) is involved in inflammatory Reaction by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally. MAPKAPK3 phosphorylates AU-rich elements (AREs)-binding proteins, like TTP/ZFP36, leading to control of stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36 (a major post-transcriptional regulator of TNF), promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity resulting in inhibition of dependent degradation of ARE-containing transcript. MAPKAPK3 is activated by growth inducers and stress stimulation of cells.

Serine/threonine-protein kinase 16 (STK16) is a membrane-associated protein kinase which phosphorylates on serine and threonine residues. STK16 is involved in secretory vesicle trafficking or intracellular signaling. Furthermore, the STK16 protein may have a role in regulating stromal-epithelial interactions which occur during ductal morphogenesis in the mammary gland. STK16 can autophosphorylate on Tyr residue; it is however unclear whether STK16 has tyrosine-protein kinase toward other proteins. STK16 may also be involved in TGF-beta signaling.

AK3L1 is an affiliate of the adenylate kinase family of enzymes. AK3L1 enzyme is restricted to the mitochondrial matrix. Adenylate kinases-3 regulates the adenine and guanine nucleotide compositions within a cell by means of catalyzing the reversible transfer of phosphate group among these nucleotides. 5 different isozymes of adenylate kinase have been identified in vertebrates. The enzyme expression of various adenylate kinase isozymes is growth regulated and tissue-specific.

GSK3B is a serine-threonine kinase that belongs to the glycogen synthase kinase subfamily. GSK3B is involved in energy metabolism, neuronal cell development, and body pattern formation. Polymorphisms in the GSK3B gene have been implicated in modifying risk of Parkinson disease, and studies in mice show that overexpression of the GSK3B gene may be significant to the pathogenesis of Alzheimer disease.

GSK3B is a serine-threonine kinase that belongs to the glycogen synthase kinase subfamily. GSK3B is involved in energy metabolism, neuronal cell development, and body pattern formation. Polymorphisms in the GSK3B gene have been implicated in modifying risk of Parkinson disease, and studies in mice show that overexpression of the GSK3B gene may be significant to the pathogenesis of Alzheimer disease.

VRK3 is a member of the protein kinase superfamily. The VRK3 gene has replacements at a number of residues within the ATP binding motifs which in other kinases were proved to be required for catalysis in both human and mouse. In vitro assays show that VRK3 has no phosphorylation activity but probably holds its substrate binding capability. VRK3 is universally expressed in human tissues and its protein is restricts to the nucleus.

PI3Ka plays a specific role in apoptosis in human colon cancer cells. Injection of neutralizing antibodies specific to PI3Ka into adenocarcinoma cells induced apoptosis, a response that was reverted by treating cells with caspase inhibitor. It was also shown that PI3Ka mediated phosphorylation of the p85a adapter reduces the lipid kinase activity of the heterodimer and this gives hints for PI3K-dependent signaling events not requiring production of 3’-phosphorylated phosphoinositides.
PI3Ka is a key regulator of the initiation of keratinocyte differentiation. A decrease in PI3Ka activity results in a loss of keratinocyte adhesion to the extracellular membrane and the initiation of early phase differentiation.

AKT Serine/Threonine Kinase 3 (Akt3) is a member of the Akt subfamily of serine/threonine protein kinases. Akt3is 1/3 closely related serine/threonine-protein kinases (Akt1, Akt2 and Akt3) called the Akt kinase and which regulate various processes including proliferation, metabolism, cell survival, growth and angiogenesis. The mentioned above is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Akt3 takes part in brain development and is critical for the viability of malignant glioma cells.