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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.

CKMT1A is in charge of the transfer of high energy phosphate from mitochondria to the cytosolic carrier, creatine. CKMT1A is a member of the creatine kinase isoenzyme family and exists as two isoenzymes, sarcomeric MtCK and ubiquitous MtCK, encoded by separate genes. Mitochondrial creatine kinase arises in two different oligomeric forms: dimers and octamers, unlike the exclusively dimeric cytosolic creatine kinase isoenzymes. Numerous malignant cancers with poor prognosis have displayed overexpression of ubiquitous mitochondrial creatine kinase which is linked to high energy turnover and inability to remove cancer cells through apoptosis.

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.

Nucleoside diphosphate kinase (Ndk) is an enzyme which catalyzes the exchange of phosphate groups between different nucleoside diphosphates. Ndk’s activity sustains equilibrium between the concentrations of various nucleoside triphosphates for example, when GTP is produced in the citric acid (Krebs) cycle is converted to ATP. Ndk has a key role in the synthesis of nucleoside triphosphates other than ATP.

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.

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.

GUK1 is part of the guanylate kinase family. GUK1 occurs as a monomer that catalyzes the ATP-dependent conversion of GMP to GDP, thus takes an important part in the recycling of GMP. Through its catalytic activity, GUK1 functions in regulation of the supply of guanine nucleotides to signal transduction pathways. GUK1 overexpression is related with pituitary adenocarcinomas, implicating that GUK1 is has a role in tumorigenesis.

PRKAB2 is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer contains an alpha catalytic subunit and non-catalytic beta and gamma subunits. AMPK is a significant energy-sensing enzyme that supervises cellular energy status. AMPK is activated as a reply to cellular metabolic stresses, therefore phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), vital enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. PRKAB2 is a positive regulator of AMPK activity and highly expressed in skeletal muscle.

DCK (Deoxycytidine kinase) is a key enzyme in the salvage of deoxyribonucleosides and in the activation of clinically relevant nucleoside analogues. DCK is responsible for the 5`-phosphorylation of purine and pyrimidine deoxynucleosides to the corresponding monophosphates using ATP or UTP as phosphate donors. Deficiency of the DCK enzyme activity is linked to resistance to antiviral and anticancer chemotherapeutic agents, whereas increased DCK enzyme activity is linked to increased activation of these compounds to cytotoxic nucleoside triphosphate derivatives.

Inositol-tetrakisphosphate 1-kinase (ITPK1) is a 414 amino acid monomer which is a member of the ITPK1 family and exists as 2 alternatively spliced isoforms. ITPK1 highest levels are found in the brain, followed by the heart, skeletal muscle, kidney, pancreas, liver, placenta and lung. ITPK1 is comprised of one ATP-grasp domain and has been shown to phosphorylate various inositol polyphosphates and modify TNFa induced apoptosis.

Protein Kinase, AMP-Activated, Alpha 1 (PRKAA1) is a protein coding gene which is the catalytic subunit of AMPK. AMPK is an energy sensor protein kinase which regulates cellular energy metabolism. AMPK adjusts the activity of various important metabolic enzymes by direct phosphorylation. Among its other features, AMPK protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways.

5'-AMP-activated protein kinase subunit beta-1 (PRKAB1) hinders protein, carbohydrate and lipid biosynthesis, in addition to cell growth and proliferation. AMPK is a heterotrimer comprised of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK acts via direct phosphorylation of metabolic enzymes, and longer-term effects by phosphorylation of transcription regulators. PRKAB1 is a regulator of cellular polarity by remodeling the actin cytoskeleton; most likely by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex compiles, through its C-terminus that joins alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

MAPK13 belongs to the MAP kinase family. MAP kinases perform as an incorporation point for various biochemical signals. MAP kinases take part in an extensive range of cellular courses like differentiation, development, transcription regulation and proliferation. MAPK13 is phosphorylated by MKK6 as a reaction to cytokines and cellular stresses.

PKLR is a pyruvate kinase which catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP. That is the rate-limiting step of glycolysis. PKLR gene encodes the L- and R-type isoenzymes through alternate splicing events controlled by different promoters. L-type isoform can also appear as a tetramer and is upregulated by glucose with implications in maturity-onset diabetes of the young.

STK17A belongs to the DAP kinase-associated apoptosis-inducing protein kinase family and encodes an autophosphorylated nuclear protein with a protein kinase domain. STK17A acts as a positive regulator of apoptosis. STK17A is greatly expressed in the placenta with lower levels in the heart, lung, skeletal muscle, kidney and pancreas.

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.

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.

PDXK converts vitamin B6 to Pyridoxal-5-phosphate (PLP), which is a vital cofactor in the intermediate metabolism of amino acids and neurotransmitters. PDXK is cytoplasmic and probably acts as a homodimer. The biological validity of the alternatively spliced transcript variants has not been determined.

Hydroxylysine Kinase, also known as HYKK, is a Protein Coding gene. HYKK which is a part of the aminoglycoside phosphotransferase family catalyzes the GTPdependent phosphorylation of 5-hydroxy-L-lysine.

PRKAG1 is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer comprised of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is a vital energy-sensing enzyme which supervises cellular energy status. PRKAG1 is one of the gamma regulatory subunits of AMPK. Alternatively spliced transcript variants encoding dissimilar isoforms were found.

UCK2 is a member of the uridinekinase family. UCK2 catalyzes the phosphorylation of uridine monophosphate to uridine diphosphate and cytidine monophosphate. UCK2 has a part in the production of pyrimidine nucleoside triphosphates essential for RNA and DNA synthesis. Furthermore, an allele of this gene is an important player in mediating nonhumoral immunity to Hemophilus influenzae type B.

Creatine Kinase, Mitochondrial 2 (CKMT2) is a member of the ATP:guanido phosphotransferase family. CKMT2 is responsible for the transfer of high energy phosphate from mitochondria to the cytosolic carrier, creatine. CKMT2 reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes have a principal role in energy transduction in tissues with large, variable energy demands, such as skeletal muscle, heart, brain and spermatozoa. Mitochondrial creatine kinase occurs in 2 different oligomeric forms: dimers and octamers, contrary to the exclusively dimeric cytosolic creatine kinase isoenzymes. The CKMT2 gene contains sequences homologous to a number of motifs which are shared among some nuclear genes encoding mitochondrial proteins and therefore may be crucial for the coordinated activation of these genes during mitochondrial biogenesis.

Mitogen-activated protein kinase 1 (MAPK1) is also known as "extracellular signal-regulated kinase 2" (ERK2). Two similar (85% sequence identity) protein kinases were originally called ERK1 and ERK2. They were found during a search for protein kinases that are rapidly phosphorylated after activation of cell surface tyrosine kinasessuch as the epidermal growth factor receptor. Phosphorylation of ERKs leads to the activation of their kinase activity.
The molecular events linking cell surface receptors to activation of ERKs are complex. It was found that RasGTP-binding proteins are involved in the activation of ERKs. Another protein kinase, Raf-1, was shown to phosphorylate a "MAPK kinase", thus qualifying as a "MAPK kinase kinase". The MAPK kinase was named "MAPK/ERK kinase" (MEK).
Receptor-linked tyrosine kinases, Ras, Raf, MEK and MAPK could be fitted into a signaling cascade linking an extracellular signal to MAPK activation.
Transgenic gene knockoutmice lacking MAPK1 have major defects in early development.

Thymidylate kinase (DTYMK) is involved in pyrimidine metabolism. Specifically, DTYMK catalyzes the ATP-dependent conversion of dTMP (deoxythymidine monophosphate) to dTDP (deoxythymidine diphosphate), which then acts as one of the 4 nucleotides in DNA. Through its role in the catalytic creation of dTDP, DTYMK has an imperative role in the pathway of DNA synthesis and is assumed to be involved in cell cycle progression and cell growth.