Glycerol Kinase
Glycerol
Dihydroxyacetone
Phosphotransferases
Glycerolphosphate Dehydrogenase
Phosphatidylinositol 3-Kinases
MAP Kinase Signaling System
Protein Kinases
Protein-Serine-Threonine Kinases
Chlorohydrins
Calcium-Calmodulin-Dependent Protein Kinases
Phosphoenolpyruvate Sugar Phosphotransferase System
Carbohydrate Metabolism, Inborn Errors
src-Family Kinases
Thermus
alpha-Chlorohydrin
Fructosediphosphates
Protein Kinase C
Phosphoenolpyruvate
Molecular Sequence Data
p38 Mitogen-Activated Protein Kinases
Cyclic AMP-Dependent Protein Kinases
Sugar Alcohol Dehydrogenases
Mutation
Mitogen-Activated Protein Kinase 1
Escherichia coli
Phosphorylation
Amino Acid Sequence
Aquaporins
Glucose
p21-Activated Kinases
Mitogen-Activated Protein Kinase Kinases
JNK Mitogen-Activated Protein Kinases
Mitogen-Activated Protein Kinase 3
Blood glycerol is an important precursor for intramuscular triacylglycerol synthesis. (1/178)
The utilization of blood glycerol and glucose as precursors for intramuscular triglyceride synthesis was examined in rats using an intravenous infusion of [2-(14)C]glycerol and [6-(3)H]glucose or [6-(14)C]glucose. In 24-h fasted rats, more glycerol than glucose was incorporated into intramuscular triglyceride glycerol in soleus (69 +/- 23 versus 4 +/- 1 nmol/micromol triglyceride/h, respectively, p = 0.02 glycerol versus glucose) and in gastrocnemius (25 +/- 5 versus 9 +/- 2 nmol/micromol triglyceride/h, respectively, p = 0.02). Blood glucose was utilized more than blood glycerol for triglyceride glycerol synthesis in quadriceps. In fed rats, the blood glycerol incorporation rates (4 +/- 2, 8 +/- 3, and 9 +/- 3 nmol/micromol triglyceride/h) were similar (p > 0.3) to those of glucose (5 +/- 2, 8 +/- 2, and 5 +/- 2 nmol/micromol triglyceride/h for quadriceps, gastrocnemius, and soleus muscle, respectively). Glucose incorporation into intramuscular triglycerides was less with [6-(3)H]glucose than with [6-(14)C]glucose, suggesting an indirect pathway for glucose carbon entry into muscle triglyceride. The isotopic equilibrium between plasma and intramuscular free glycerol ([U-(13)C]glycerol) was complete in quadriceps and gastrocnemius, but not soleus, within 2 h after beginning the tracer infusion. We conclude that blood glycerol is a direct and important precursor for muscle triglyceride synthesis in rats, confirming the presence of functionally important amounts of glycerol kinase in skeletal muscle. (+info)Expression of GUT1, which encodes glycerol kinase in Saccharomyces cerevisiae, is controlled by the positive regulators Adr1p, Ino2p and Ino4p and the negative regulator Opi1p in a carbon source-dependent fashion. (2/178)
In Saccharomyces cerevisiae glycerol utilization is mediated by two enzymes, glycerol kinase (Gut1p) and mitochondrial glycerol-3-phosphate dehydrogenase (Gut2p). The carbon source regulation of GUT1 was studied using promoter-reporter gene fusions. The promoter activity was lowest during growth on glucose and highest on the non-fermentable carbon sources, glycerol, ethanol, lactate, acetate and oleic acid. Mutational analysis of the GUT1 promoter region showed that two upstream activation sequences, UAS(INO) and UAS(ADR1), are responsible for approximately 90% of the expression during growth on glycerol. UAS(ADR1) is a presumed binding site for the zinc finger transcription factor Adr1p and UAS(INO) is a presumed binding site for the basic helix-loop-helix transcription factors Ino2p and Ino4p. In vitro experiments showed Adr1 and Ino2/Ino4 protein-dependent binding to UAS(ADR1) and UAS(INO). The negative regulator Opi1p mediates repression of the GUT1 promoter, whereas the effects of the glucose repressors Mig1p and Mig2p are minor. Together, the experiments show that GUT1 is carbon source regulated by different activation and repression systems. (+info)Glycerol transport and phosphoenolpyruvate-dependent enzyme I- and HPr-catalysed phosphorylation of glycerol kinase in Thermus flavus. (3/178)
The genes glpK and glpF, encoding glycerol kinase and the glycerol facilitator of Thermus flavus, a member of the Thermus/Deinococcus group, have recently been identified. The protein encoded by glpK exhibited an unusually high degree of sequence identity (80-6%) when compared to the sequence of glycerol kinase from Bacillus subtilis and a similar high degree of sequence identity (64.8%) was observed when the sequences of the glycerol facilitators of the two organisms were compared. The work presented in this paper demonstrates that T. flavus is capable of taking up glycerol, that glpF and glpK are expressed constitutively and that glucose exerts a repressive effect on the expression of these genes. T. flavus was found to possess the general components of the phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS) enzyme I and histidine-containing protein (HPr). These proteins catalyse the phosphorylation of T. flavus glycerol kinase, which contains a histidyl residue equivalent to His-232, the site of PEP-dependent, PTS-catalysed phosphorylation in glycerol kinase of Enterococcus casseliflavus. Purified glycerol kinase from T. flavus could also be phosphorylated with enzyme I and HPr from B. subtilis. Similar to enterococcal glycerol kinases, phosphorylated T. flavus glycerol kinase exhibited an electrophoretic mobility on denaturing and non-denaturing polyacrylamide gels that is different from the electrophoretic mobility of non-phosphorylated glycerol kinase. However, in contrast to PEP-dependent phosphorylation of enterococcal glycerol kinases, which stimulated glycerol kinase activity about 10-fold, phosphorylation of T. flavus glycerol kinase caused only a slight increase in enzyme activity. (+info)Changes in protein synthesis during the adaptation of Bacillus subtilis to anaerobic growth conditions. (4/178)
After a shift of Bacillus subtilis from aerobic to anaerobic growth conditions, nitrate ammonification and various fermentative processes replace oxygen-dependent respiration. Cell-free extracts prepared from wild-type B. subtilis and from mutants of the regulatory loci fnr and resDE grown under aerobic and various anaerobic conditions were compared by two-dimensional gel electrophoresis. Proteins involved in the adaptation process were identified by their N-terminal sequence. Induction of cytoplasmic lactate dehydrogenase (LctE) synthesis under anaerobic fermentative conditions was dependent on fnr and resDE. Anaerobic nitrate repression of LctE formation required fnr-mediated expression of narGHJI, encoding respiratory nitrate reductase. Anaerobic induction of the flavohaemoglobin Hmp required resDE and nitrite. The general anaerobic induction of ywfl, encoding a protein of unknown function, was modulated by resDE and fnr. The ywfl gene shares its upstream region with the pta gene, encoding the fermentative enzyme acetyl-CoA:orthophosphate acetyltransferase. Anaerobic repression of the synthesis of a potential membrane-associated NADH dehydrogenase (YjlD, Ndh), and anaerobic induction of fructose-1,6-bisphosphate aldolase (FbaA) and dehydrolipoamide dehydrogenase (PhdD, Lpd) formation, did not require fnr or resDE participation. Synthesis of glycerol kinase (GlpK) was decreased under anaerobic conditions. Finally, the effect of anaerobic stress induced by the immediate shift from aerobic to strictly anaerobic conditions was analysed. The induction of various systems for the utilization of alternative carbon sources such as inositol (IoIA, IoIG, IoIH, IoII), melibiose (MeIA) and 6-phospho-alpha-glucosides (GIvA) indicated a catabolite-response-like stress reaction. (+info)Glycerol as a correlate of impaired glucose tolerance: dissection of a complex system by use of a simple genetic trait. (5/178)
Glycerol kinase (GK) represents the primary entry of glycerol into glucose and triglyceride metabolism. Impaired glucose tolerance (IGT) and hypertriglyceridemia are associated with an increased risk of diabetes mellitus and cardiovascular disease. The relationship between glycerol and the risk of IGT, however, is poorly understood. We therefore undertook the study of fasting plasma glycerol levels in a cohort of 1,056 unrelated men and women of French-Canadian descent. Family screening in the initial cohort identified 18 men from five families with severe hyperglycerolemia (values above 2.0 mmol/liter) and demonstrated an X-linked pattern of inheritance. Linkage analysis of the data from 12 microsatellite markers surrounding the Xp21.3 GK gene resulted in a peak LOD score of 3.46, centered around marker DXS8039. In addition, since all of the families originated in a population with a proven founder effect-the Saguenay Lac-St.-Jean region of Quebec-a common disease haplotype was sought. Indeed, a six-marker haplotype extending over a region of 5.5 cM was observed in all families. Resequencing of the GK gene in family members led to the discovery of a N288D missense mutation in exon 10, which resulted in the substitution of a highly conserved asparagine residue by a negatively charged aspartic acid. Although patients with the N288D mutation suffered from severe hyperglycerolemia, they were apparently otherwise healthy. The phenotypic analysis of the family members, however, showed that glycerol levels correlated with impaired glucose metabolism and body-fat distribution. We subsequently noted a substantial variation in glycerolemia in subjects of the initial cohort with normal plasma glycerol levels and demonstrated that this variance showed significant family resemblance. These results suggest a potentially important genetic connection between fasting glycerolemia and glucose homeostasis, not only in this X-linked deficiency but, potentially, in individuals within the "normal" range of plasma glycerol concentrations. (+info)Glycerol kinase of Trypanosoma brucei. Cloning, molecular characterization and mutagenesis. (6/178)
Trypanosoma brucei contains two tandemly arranged genes for glycerol kinase. The downstream gene was analysed in detail. It contains an ORF for a polypeptide of 512 amino acids. The polypeptide has a calculated molecular mass of 56 363 Da and a pI of 8.6. Comparison of the T. brucei glycerol kinase amino-acid sequence with the glycerol kinase sequences available in databases revealed positional identities of 39.0-50.4%. The T. brucei glycerol kinase gene was overexpressed in Escherichia coli cells and the recombinant protein obtained was purified and characterized biochemically. Its kinetic properties with regard to both the forward and reverse reaction were measured. The values corresponded to those determined previously for the natural glycerol kinase purified from the parasite, and confirmed that the apparent Km values of the trypanosome enzyme for its substrates are relatively high compared with those of other glycerol kinases. Alignment of the amino-acid sequences of T. brucei glycerol kinase and other eukaryotic and prokaryotic glycerol kinases, as well as inspection of the available three-dimensional structure of E. coli glycerol kinase showed that most residues of the magnesium-, glycerol- and ADP-binding sites are well conserved in T. brucei glycerol kinase. However, a number of remarkable substitutions was identified, which could be responsible for the low affinity for the substrates. Most striking is amino-acid Ala137 in T. brucei glycerol kinase; in all other organisms a serine is present at the corresponding position. We mutated Ala137 of T. brucei glycerol kinase into a serine and this mutant glycerol kinase was over-expressed and purified. The affinity of the mutant enzyme for its substrates glycerol and glycerol 3-phosphate appeared to be 3. 1-fold to 3.6-fold higher than in the wild-type enzyme. Part of the glycerol kinase gene comprising this residue 137 was amplified in eight different kinetoplastid species and sequenced. Interestingly, an alanine occurs not only in T. brucei, but also in other trypanosomatids which can convert glucose into equimolar amounts of glycerol and pyruvate: T. gambiense, T. equiperdum and T. evansi. In trypanosomatids with no or only a limited capacity to produce glycerol, a hydroxy group-containing residue is found as in all other organisms: T. vivax and T. congolense possess a serine while Phytomonas sp., Leishmania brasiliensis and L. mexicana have a threonine. (+info)Glycerol dissimilation in Rhodopseudomonas sphaeroides. (7/178)
Rhodopseudomonas sphaeroides followed a diauxic growth curve when grown on a malate-glycerol medium, the first phase of growth being supported by malate and the second by glycerol. A soluble glycerokinase and a particulate, pyridine nucleotide-independent glycerophosphate dehydrogenase, were induced by the presence of glycerol in the medium, but neither was fully expressed nor functional until all malate had been consumed. (+info)Five cases of isolated glycerol kinase deficiency, including two families: failure to find genotype:phenotype correlation. (8/178)
Little is understood of the genotype/phenotype correlations in X linked glycerol kinase deficiency (GKD) where most cases are caused by extensive deletions of Xp21, which often include genes flanking the GK locus. Few cases of isolated GKD have been investigated where the phenotype is not influenced by neighbouring genes. In this paper, we present the mutation data from four confirmed and one suspected case of non-deletion, isolated, X linked GKD and therefore extend the base of patients that can allow an assessment of genotype/phenotype correlations for this disease. The mutations found were two terminations leading to premature truncation of the GK polypeptide chain, one insertion, and an amino acid substitution. Phenotypic variation was observed in two families, where there was more than one affected subject carrying the same mutation, confirming previous studies that suggest there is no correlation between disease severity and genotype. Furthermore, the nature of the mutation in different families does not appear to influence the spectrum of phenotypic variation. In addition, one coding polymorphism in exon 3 has been found. The characterisation of the gene structure has been completed and shows that instead of 19 there are 21 exons. (+info)Glycerol kinase is an enzyme that plays a crucial role in the metabolism of glycerol, which is a simple carbohydrate. The enzyme catalyzes the conversion of glycerol to glycerol-3-phosphate by transferring a phosphate group from ATP to glycerol. This reaction is an essential step in the metabolic pathway that leads to the formation of glucose or other energy-rich compounds in the body.
There are two main forms of glycerol kinase found in humans, designated as GK1 and GK2. GK1 is primarily expressed in the liver, while GK2 is found in various tissues, including the brain, heart, and muscles. Deficiencies in glycerol kinase can lead to metabolic disorders such as hyperglycerolemia, which is characterized by high levels of glycerol in the blood.
Glycerol, also known as glycerine or glycerin, is a simple polyol (a sugar alcohol) with a sweet taste and a thick, syrupy consistency. It is a colorless, odorless, viscous liquid that is slightly soluble in water and freely miscible with ethanol and ether.
In the medical field, glycerol is often used as a medication or supplement. It can be used as a laxative to treat constipation, as a source of calories and energy for people who cannot eat by mouth, and as a way to prevent dehydration in people with certain medical conditions.
Glycerol is also used in the production of various medical products, such as medications, skin care products, and vaccines. It acts as a humectant, which means it helps to keep things moist, and it can also be used as a solvent or preservative.
In addition to its medical uses, glycerol is also widely used in the food industry as a sweetener, thickening agent, and moisture-retaining agent. It is generally recognized as safe (GRAS) by the U.S. Food and Drug Administration (FDA).
Glycerophosphates are esters of glycerol and phosphoric acid. In the context of biochemistry and medicine, glycerophosphates often refer to glycerol 3-phosphate (also known as glyceraldehyde 3-phosphate or glycerone phosphate) and its derivatives.
Glycerol 3-phosphate plays a crucial role in cellular metabolism, particularly in the process of energy production and storage. It is an important intermediate in both glycolysis (the breakdown of glucose to produce energy) and gluconeogenesis (the synthesis of glucose from non-carbohydrate precursors).
In addition, glycerophosphates are also involved in the formation of phospholipids, a major component of cell membranes. The esterification of glycerol 3-phosphate with fatty acids leads to the synthesis of phosphatidic acid, which is a key intermediate in the biosynthesis of other phospholipids.
Abnormalities in glycerophosphate metabolism have been implicated in various diseases, including metabolic disorders and neurological conditions.
Dihydroxyacetone (DHA) is a simple sugar that is used as an ingredient in many self-tanning products. When applied to the skin, DHA reacts with amino acids in the dead layer of the skin to temporarily darken the skin color. This process is known as the Maillard reaction, which is a chemical reaction between an amino acid and a sugar. The effect of DHA is limited to the uppermost layer of the skin and it does not provide any protection against sunburn or UV radiation. The tanning effect produced by DHA usually lasts for about 5-7 days.
It's important to note that while DHA is considered safe for external use, it should not be inhaled or ingested, as it can cause irritation and other adverse effects. Additionally, some people may experience skin irritation or allergic reactions to products containing DHA, so it's always a good idea to do a patch test before using a new self-tanning product.
Phosphotransferases are a group of enzymes that catalyze the transfer of a phosphate group from a donor molecule to an acceptor molecule. This reaction is essential for various cellular processes, including energy metabolism, signal transduction, and biosynthesis.
The systematic name for this group of enzymes is phosphotransferase, which is derived from the general reaction they catalyze: D-donor + A-acceptor = D-donor minus phosphate + A-phosphate. The donor molecule can be a variety of compounds, such as ATP or a phosphorylated protein, while the acceptor molecule is typically a compound that becomes phosphorylated during the reaction.
Phosphotransferases are classified into several subgroups based on the type of donor and acceptor molecules they act upon. For example, kinases are a subgroup of phosphotransferases that transfer a phosphate group from ATP to a protein or other organic compound. Phosphatases, another subgroup, remove phosphate groups from molecules by transferring them to water.
Overall, phosphotransferases play a critical role in regulating many cellular functions and are important targets for drug development in various diseases, including cancer and neurological disorders.
Glycerol-3-phosphate dehydrogenase (GPD) is an enzyme that plays a crucial role in the metabolism of glucose and lipids. It catalyzes the conversion of dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate (G3P), which is a key intermediate in the synthesis of triglycerides, phospholipids, and other glycerophospholipids.
There are two main forms of GPD: a cytoplasmic form (GPD1) and a mitochondrial form (GPD2). The cytoplasmic form is involved in the production of NADH, which is used in various metabolic processes, while the mitochondrial form is involved in the production of ATP, the main energy currency of the cell.
Deficiencies or mutations in GPD can lead to a variety of metabolic disorders, including glycerol kinase deficiency and congenital muscular dystrophy. Elevated levels of GPD have been observed in certain types of cancer, suggesting that it may play a role in tumor growth and progression.
Phosphatidylinositol 3-Kinases (PI3Ks) are a family of enzymes that play a crucial role in intracellular signal transduction. They phosphorylate the 3-hydroxyl group of the inositol ring in phosphatidylinositol and its derivatives, which results in the production of second messengers that regulate various cellular processes such as cell growth, proliferation, differentiation, motility, and survival.
PI3Ks are divided into three classes based on their structure and substrate specificity. Class I PI3Ks are further subdivided into two categories: class IA and class IB. Class IA PI3Ks are heterodimers consisting of a catalytic subunit (p110α, p110β, or p110δ) and a regulatory subunit (p85α, p85β, p55γ, or p50γ). They are primarily activated by receptor tyrosine kinases and G protein-coupled receptors. Class IB PI3Ks consist of a catalytic subunit (p110γ) and a regulatory subunit (p101 or p84/87). They are mainly activated by G protein-coupled receptors.
Dysregulation of PI3K signaling has been implicated in various human diseases, including cancer, diabetes, and autoimmune disorders. Therefore, PI3Ks have emerged as important targets for drug development in these areas.
Mitogen-activated protein kinase (MAPK) signaling system is a crucial pathway for the transmission and regulation of various cellular responses in eukaryotic cells. It plays a significant role in several biological processes, including proliferation, differentiation, apoptosis, inflammation, and stress response. The MAPK cascade consists of three main components: MAP kinase kinase kinase (MAP3K or MEKK), MAP kinase kinase (MAP2K or MEK), and MAP kinase (MAPK).
The signaling system is activated by various extracellular stimuli, such as growth factors, cytokines, hormones, and stress signals. These stimuli initiate a phosphorylation cascade that ultimately leads to the activation of MAPKs. The activated MAPKs then translocate into the nucleus and regulate gene expression by phosphorylating various transcription factors and other regulatory proteins.
There are four major MAPK families: extracellular signal-regulated kinases (ERK1/2), c-Jun N-terminal kinases (JNK1/2/3), p38 MAPKs (p38α/β/γ/δ), and ERK5. Each family has distinct functions, substrates, and upstream activators. Dysregulation of the MAPK signaling system can lead to various diseases, including cancer, diabetes, cardiovascular diseases, and neurological disorders. Therefore, understanding the molecular mechanisms underlying this pathway is crucial for developing novel therapeutic strategies.
Protein kinases are a group of enzymes that play a crucial role in many cellular processes by adding phosphate groups to other proteins, a process known as phosphorylation. This modification can activate or deactivate the target protein's function, thereby regulating various signaling pathways within the cell. Protein kinases are essential for numerous biological functions, including metabolism, signal transduction, cell cycle progression, and apoptosis (programmed cell death). Abnormal regulation of protein kinases has been implicated in several diseases, such as cancer, diabetes, and neurological disorders.
Protein-Serine-Threonine Kinases (PSTKs) are a type of protein kinase that catalyzes the transfer of a phosphate group from ATP to the hydroxyl side chains of serine or threonine residues on target proteins. This phosphorylation process plays a crucial role in various cellular signaling pathways, including regulation of metabolism, gene expression, cell cycle progression, and apoptosis. PSTKs are involved in many physiological and pathological processes, and their dysregulation has been implicated in several diseases, such as cancer, diabetes, and neurodegenerative disorders.
Chlorohydrins are a class of chemical compounds that contain both chlorine and hydroxyl (-OH) groups. They are typically formed by the reaction of an aldehyde or ketone with a hypochlorous acid or chlorine in a process called halogenation. Chlorohydrins can be toxic and have been associated with various health effects, including irritation of the eyes, skin, and respiratory tract, and potential damage to the liver and kidneys. They are used in some industrial applications, such as the production of certain chemicals and pharmaceuticals, but their use is subject to regulations due to their potential hazards.
Protein kinase inhibitors (PKIs) are a class of drugs that work by interfering with the function of protein kinases. Protein kinases are enzymes that play a crucial role in many cellular processes by adding a phosphate group to specific proteins, thereby modifying their activity, localization, or interaction with other molecules. This process of adding a phosphate group is known as phosphorylation and is a key mechanism for regulating various cellular functions, including signal transduction, metabolism, and cell division.
In some diseases, such as cancer, protein kinases can become overactive or mutated, leading to uncontrolled cell growth and division. Protein kinase inhibitors are designed to block the activity of these dysregulated kinases, thereby preventing or slowing down the progression of the disease. These drugs can be highly specific, targeting individual protein kinases or families of kinases, making them valuable tools for targeted therapy in cancer and other diseases.
Protein kinase inhibitors can work in various ways to block the activity of protein kinases. Some bind directly to the active site of the enzyme, preventing it from interacting with its substrates. Others bind to allosteric sites, changing the conformation of the enzyme and making it inactive. Still, others target upstream regulators of protein kinases or interfere with their ability to form functional complexes.
Examples of protein kinase inhibitors include imatinib (Gleevec), which targets the BCR-ABL kinase in chronic myeloid leukemia, and gefitinib (Iressa), which inhibits the EGFR kinase in non-small cell lung cancer. These drugs have shown significant clinical benefits in treating these diseases and have become important components of modern cancer therapy.
Calcium-calmodulin-dependent protein kinases (CAMKs) are a family of enzymes that play a crucial role in intracellular signaling pathways. They are activated by the binding of calcium ions and calmodulin, a ubiquitous calcium-binding protein, to their regulatory domain.
Once activated, CAMKs phosphorylate specific serine or threonine residues on target proteins, thereby modulating their activity, localization, or stability. This post-translational modification is essential for various cellular processes, including synaptic plasticity, gene expression, metabolism, and cell cycle regulation.
There are several subfamilies of CAMKs, including CaMKI, CaMKII, CaMKIII (also known as CaMKIV), and CaMK kinase (CaMKK). Each subfamily has distinct structural features, substrate specificity, and regulatory mechanisms. Dysregulation of CAMK signaling has been implicated in various pathological conditions, such as neurodegenerative diseases, cancer, and cardiovascular disorders.
The Phosphoenolpyruvate (PEP) sugar phosphotransferase system (PTS) is not exactly a "sugar," but rather a complex molecular machinery used by certain bacteria for the transport and phosphorylation of sugars. The PTS system is a major carbohydrate transport system in many gram-positive and gram-negative bacteria, which allows them to take up and metabolize various sugars for energy and growth.
The PTS system consists of several protein components, including the enzyme I (EI), histidine phosphocarrier protein (HPr), and sugar-specific enzymes II (EII). The process begins when PEP transfers a phosphate group to EI, which then passes it on to HPr. The phosphorylated HPr then interacts with the sugar-specific EII complex, which is composed of two domains: the membrane-associated domain (EIIA) and the periplasmic domain (EIIC).
When a sugar molecule binds to the EIIC domain, it induces a conformational change that allows the phosphate group from HPr to be transferred to the sugar. This phosphorylation event facilitates the translocation of the sugar across the membrane and into the cytoplasm, where it undergoes further metabolic reactions.
In summary, the Phosphoenolpyruvate Sugar Phosphotransferase System (PEP-PTS) is a bacterial transport system that utilizes phosphoryl groups from phosphoenolpyruvate to facilitate the uptake and phosphorylation of sugars, allowing bacteria to efficiently metabolize and utilize various carbon sources for energy and growth.
Inborn errors of carbohydrate metabolism refer to genetic disorders that affect the body's ability to break down and process carbohydrates, which are sugars and starches that provide energy for the body. These disorders are caused by defects in enzymes or transport proteins that play a critical role in the metabolic pathways involved in carbohydrate metabolism.
There are several types of inborn errors of carbohydrate metabolism, including:
1. Galactosemia: This disorder affects the body's ability to metabolize the sugar galactose, which is found in milk and other dairy products. It is caused by a deficiency of the enzyme galactose-1-phosphate uridylyltransferase.
2. Glycogen storage diseases: These disorders affect the body's ability to store and break down glycogen, which is a complex carbohydrate that serves as a source of energy for the body. There are several types of glycogen storage diseases, each caused by a deficiency in a different enzyme involved in glycogen metabolism.
3. Hereditary fructose intolerance: This disorder affects the body's ability to metabolize the sugar fructose, which is found in fruits and sweeteners. It is caused by a deficiency of the enzyme aldolase B.
4. Pentose phosphate pathway disorders: These disorders affect the body's ability to metabolize certain sugars and generate energy through the pentose phosphate pathway. They are caused by defects in enzymes involved in this pathway.
Symptoms of inborn errors of carbohydrate metabolism can vary widely depending on the specific disorder and its severity. Treatment typically involves dietary restrictions, supplementation with necessary enzymes or cofactors, and management of complications. In some cases, enzyme replacement therapy or even organ transplantation may be considered.
SRC-family kinases (SFKs) are a group of non-receptor tyrosine kinases that play important roles in various cellular processes, including cell proliferation, differentiation, survival, and migration. They are named after the founding member, SRC, which was first identified as an oncogene in Rous sarcoma virus.
SFKs share a common structure, consisting of an N-terminal unique domain, a SH3 domain, a SH2 domain, a catalytic kinase domain, and a C-terminal regulatory tail with a negative regulatory tyrosine residue (Y527 in human SRC). In their inactive state, SFKs are maintained in a closed conformation through intramolecular interactions between the SH3 domain, SH2 domain, and the phosphorylated C-terminal tyrosine.
Upon activation by various signals, such as growth factors, cytokines, or integrin engagement, SFKs are activated through a series of events that involve dephosphorylation of the regulatory tyrosine residue, recruitment to membrane receptors via their SH2 and SH3 domains, and trans-autophosphorylation of the activation loop in the kinase domain.
Once activated, SFKs can phosphorylate a wide range of downstream substrates, including other protein kinases, adaptor proteins, and cytoskeletal components, thereby regulating various signaling pathways that control cell behavior. Dysregulation of SFK activity has been implicated in various diseases, including cancer, inflammation, and neurological disorders.
In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."
1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.
2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.
3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.
4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).
Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.
"Thermus" is not a medical term, but rather a genus of bacteria that are capable of growing in extreme temperatures. These bacteria are named after the Greek word "therme," which means heat. They are commonly found in hot springs and deep-sea hydrothermal vents, where the temperature can reach up to 70°C (158°F).
Some species of Thermus have been found to produce enzymes that remain active at high temperatures, making them useful in various industrial applications such as molecular biology and DNA amplification techniques like polymerase chain reaction (PCR). However, Thermus itself is not a medical term or concept.
Alpha-chlorohydrin is not typically referred to as a medical term, but it is a chemical compound with the formula HOCH2CHClNH2. It is primarily used in the production of other chemicals and has been used as a reagent in laboratory settings.
Ingestion or exposure to alpha-chlorohydrin can be harmful and may cause symptoms such as nausea, vomiting, abdominal pain, diarrhea, dizziness, and difficulty breathing. It is classified as a possible human carcinogen by the International Agency for Research on Cancer (IARC).
Medical professionals may encounter alpha-chlorohydrin in cases of accidental or intentional ingestion or exposure, or in the context of occupational health and safety for workers who may be exposed to it in industrial settings.
Dihydroxyacetone Phosphate (DHAP) is a 3-carbon organic compound that plays a crucial role in the metabolic pathway called glycolysis. It is an intermediate molecule formed during the conversion of glucose into pyruvate, which ultimately produces energy in the form of ATP.
In the glycolytic process, DHAP is produced from glyceraldehyde 3-phosphate (G3P) in a reaction catalyzed by the enzyme triose phosphate isomerase. Then, DHAP is converted back to G3P in a subsequent step, which prepares it for further processing in the glycolytic pathway. This reversible conversion of DHAP and G3P helps maintain the equilibrium of the glycolytic process.
Apart from its role in energy metabolism, DHAP is also involved in other biochemical processes, such as the synthesis of glucose during gluconeogenesis and the formation of lipids in the liver.
I'm sorry for any confusion, but "Fructosediphosphates" is not a recognized term in medicine or biochemistry. It's possible there may be a spelling mistake or misunderstanding in the term you're looking for.
If you meant "Fructose 1,6-bisphosphate," that is a key intermediate in carbohydrate metabolism. It's formed from fructose 6-phosphate in the process of glucose breakdown (glycolysis) and is then used in the generation of energy through the citric acid cycle.
If these terms are not what you were looking for, could you please provide more context or check the spelling? I'm here to help!
Protein Kinase C (PKC) is a family of serine-threonine kinases that play crucial roles in various cellular signaling pathways. These enzymes are activated by second messengers such as diacylglycerol (DAG) and calcium ions (Ca2+), which result from the activation of cell surface receptors like G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs).
Once activated, PKC proteins phosphorylate downstream target proteins, thereby modulating their activities. This regulation is involved in numerous cellular processes, including cell growth, differentiation, apoptosis, and membrane trafficking. There are at least 10 isoforms of PKC, classified into three subfamilies based on their second messenger requirements and structural features: conventional (cPKC; α, βI, βII, and γ), novel (nPKC; δ, ε, η, and θ), and atypical (aPKC; ζ and ι/λ). Dysregulation of PKC signaling has been implicated in several diseases, such as cancer, diabetes, and neurological disorders.
Phosphoenolpyruvate (PEP) is a key intermediate in the glycolysis pathway and other metabolic processes. It is a high-energy molecule that plays a crucial role in the transfer of energy during cellular respiration. Specifically, PEP is formed from the breakdown of fructose-1,6-bisphosphate and is then converted to pyruvate, releasing energy that is used to generate ATP, a major source of energy for cells.
Medically, abnormal levels of PEP may indicate issues with cellular metabolism or energy production, which can be associated with various medical conditions such as diabetes, mitochondrial disorders, and other metabolic diseases. However, direct measurement of PEP levels in clinical settings is not commonly performed due to technical challenges. Instead, clinicians typically assess overall metabolic function through a variety of other tests and measures.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
p38 Mitogen-Activated Protein Kinases (p38 MAPKs) are a family of conserved serine-threonine protein kinases that play crucial roles in various cellular processes, including inflammation, immune response, differentiation, apoptosis, and stress responses. They are activated by diverse stimuli such as cytokines, ultraviolet radiation, heat shock, osmotic stress, and lipopolysaccharides (LPS).
Once activated, p38 MAPKs phosphorylate and regulate several downstream targets, including transcription factors and other protein kinases. This regulation leads to the expression of genes involved in inflammation, cell cycle arrest, and apoptosis. Dysregulation of p38 MAPK signaling has been implicated in various diseases, such as cancer, neurodegenerative disorders, and autoimmune diseases. Therefore, p38 MAPKs are considered promising targets for developing new therapeutic strategies to treat these conditions.
Cyclic AMP (cAMP)-dependent protein kinases, also known as protein kinase A (PKA), are a family of enzymes that play a crucial role in intracellular signaling pathways. These enzymes are responsible for the regulation of various cellular processes, including metabolism, gene expression, and cell growth and differentiation.
PKA is composed of two regulatory subunits and two catalytic subunits. When cAMP binds to the regulatory subunits, it causes a conformational change that leads to the dissociation of the catalytic subunits. The freed catalytic subunits then phosphorylate specific serine and threonine residues on target proteins, thereby modulating their activity.
The cAMP-dependent protein kinases are activated in response to a variety of extracellular signals, such as hormones and neurotransmitters, that bind to G protein-coupled receptors (GPCRs) or receptor tyrosine kinases (RTKs). These signals lead to the activation of adenylyl cyclase, which catalyzes the conversion of ATP to cAMP. The resulting increase in intracellular cAMP levels triggers the activation of PKA and the downstream phosphorylation of target proteins.
Overall, cAMP-dependent protein kinases are essential regulators of many fundamental cellular processes and play a critical role in maintaining normal physiology and homeostasis. Dysregulation of these enzymes has been implicated in various diseases, including cancer, diabetes, and neurological disorders.
Sugar alcohol dehydrogenases (SADHs) are a group of enzymes that catalyze the interconversion between sugar alcohols and sugars, which involves the gain or loss of a pair of electrons, typically in the form of NAD(P)+/NAD(P)H. These enzymes play a crucial role in the metabolism of sugar alcohols, which are commonly found in various plants and some microorganisms.
Sugar alcohols, also known as polyols, are reduced forms of sugars that contain one or more hydroxyl groups instead of aldehyde or ketone groups. Examples of sugar alcohols include sorbitol, mannitol, xylitol, and erythritol. SADHs can interconvert these sugar alcohols to their corresponding sugars through a redox reaction that involves the transfer of hydrogen atoms.
The reaction catalyzed by SADHs is typically represented as follows:
R-CH(OH)-CH2OH + NAD(P)+ ↔ R-CO-CH2OH + NAD(P)H + H+
where R represents a carbon chain, and CH(OH)-CH2OH and CO-CH2OH represent the sugar alcohol and sugar forms, respectively.
SADHs are widely distributed in nature and have been found in various organisms, including bacteria, fungi, plants, and animals. These enzymes have attracted significant interest in biotechnology due to their potential applications in the production of sugar alcohols and other value-added products. Additionally, SADHs have been studied as targets for developing novel antimicrobial agents, as inhibiting these enzymes can disrupt the metabolism of certain pathogens that rely on sugar alcohols for growth and survival.
A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.
P-Chloromercuribenzoic acid (CMB) is not primarily considered a medical compound, but rather an organic chemical one. However, it has been used in some medical research and diagnostic procedures due to its ability to bind to proteins and enzymes. Here's the chemical definition:
P-Chloromercuribenzoic acid (CMB) is an organomercury compound with the formula C6H4ClHgO2. It is a white crystalline powder, soluble in water, and has a melting point of 208-210 °C. It is used as a reagent to study protein structure and function, as it can react with sulfhydryl groups (-SH) in proteins, forming a covalent bond and inhibiting their activity. This property has been exploited in various research and diagnostic applications. However, due to its toxicity and environmental concerns related to mercury, its use is now limited and regulated.
Mitogen-Activated Protein Kinase 1 (MAPK1), also known as Extracellular Signal-Regulated Kinase 2 (ERK2), is a protein kinase that plays a crucial role in intracellular signal transduction pathways. It is a member of the MAPK family, which regulates various cellular processes such as proliferation, differentiation, apoptosis, and stress response.
MAPK1 is activated by a cascade of phosphorylation events initiated by upstream activators like MAPKK (Mitogen-Activated Protein Kinase Kinase) in response to various extracellular signals such as growth factors, hormones, and mitogens. Once activated, MAPK1 phosphorylates downstream targets, including transcription factors and other protein kinases, thereby modulating their activities and ultimately influencing gene expression and cellular responses.
MAPK1 is widely expressed in various tissues and cells, and its dysregulation has been implicated in several pathological conditions, including cancer, inflammation, and neurodegenerative diseases. Therefore, understanding the regulation and function of MAPK1 signaling pathways has important implications for developing therapeutic strategies to treat these disorders.
'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.
While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.
E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.
Phosphorylation is the process of adding a phosphate group (a molecule consisting of one phosphorus atom and four oxygen atoms) to a protein or other organic molecule, which is usually done by enzymes called kinases. This post-translational modification can change the function, localization, or activity of the target molecule, playing a crucial role in various cellular processes such as signal transduction, metabolism, and regulation of gene expression. Phosphorylation is reversible, and the removal of the phosphate group is facilitated by enzymes called phosphatases.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Aquaporins are a type of membrane protein that function as water channels, allowing the selective and efficient transport of water molecules across biological membranes. They play crucial roles in maintaining fluid homeostasis, regulating cell volume, and supporting various physiological processes in the body. In humans, there are 13 different aquaporin subtypes (AQP0 to AQP12) that have been identified, each with distinct tissue expression patterns and functions. Some aquaporins also facilitate the transport of small solutes such as glycerol and urea. Dysfunction or misregulation of aquaporins has been implicated in several pathological conditions, including neurological disorders, cancer, and water balance-related diseases.
Glucose is a simple monosaccharide (or single sugar) that serves as the primary source of energy for living organisms. It's a fundamental molecule in biology, often referred to as "dextrose" or "grape sugar." Glucose has the molecular formula C6H12O6 and is vital to the functioning of cells, especially those in the brain and nervous system.
In the body, glucose is derived from the digestion of carbohydrates in food, and it's transported around the body via the bloodstream to cells where it can be used for energy. Cells convert glucose into a usable form through a process called cellular respiration, which involves a series of metabolic reactions that generate adenosine triphosphate (ATP)—the main currency of energy in cells.
Glucose is also stored in the liver and muscles as glycogen, a polysaccharide (multiple sugar) that can be broken down back into glucose when needed for energy between meals or during physical activity. Maintaining appropriate blood glucose levels is crucial for overall health, and imbalances can lead to conditions such as diabetes mellitus.
P21-activated kinases (PAKs) are a family of serine/threonine protein kinases that play crucial roles in various cellular processes, including cytoskeletal reorganization, cell motility, and gene transcription. They are activated by binding to small GTPases of the Rho family, such as Cdc42 and Rac, which become active upon stimulation of various extracellular signals. Once activated, PAKs phosphorylate a range of downstream targets, leading to changes in cell behavior and function. Aberrant regulation of PAKs has been implicated in several human diseases, including cancer and neurological disorders.
Mitogen-Activated Protein Kinase Kinases (MAP2K or MEK) are a group of protein kinases that play a crucial role in intracellular signal transduction pathways. They are so named because they are activated by mitogens, which are substances that stimulate cell division, and other extracellular signals.
MAP2Ks are positioned upstream of the Mitogen-Activated Protein Kinases (MAPK) in a three-tiered kinase cascade. Once activated, MAP2Ks phosphorylate and activate MAPKs, which then go on to regulate various cellular processes such as proliferation, differentiation, survival, and apoptosis.
There are several subfamilies of MAP2Ks, including MEK1/2, MEK3/6 (also known as MKK3/6), MEK4/7 (also known as MKK4/7), and MEK5. Each MAP2K is specific to activating a particular MAPK, and they are activated by different MAP3Ks (MAP kinase kinase kinases) in response to various extracellular signals.
Dysregulation of the MAPK/MAP2K signaling pathways has been implicated in numerous diseases, including cancer, cardiovascular disease, and neurological disorders. Therefore, targeting these pathways with therapeutic agents has emerged as a promising strategy for treating various diseases.
JNK (c-Jun N-terminal kinase) Mitogen-Activated Protein Kinases are a subgroup of the Ser/Thr protein kinases that are activated by stress stimuli and play important roles in various cellular processes, including inflammation, apoptosis, and differentiation. They are involved in the regulation of gene expression through phosphorylation of transcription factors such as c-Jun. JNKs are activated by a variety of upstream kinases, including MAP2Ks (MKK4/SEK1 and MKK7), which are in turn activated by MAP3Ks (such as ASK1, MEKK1, MLKs, and TAK1). JNK signaling pathways have been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory diseases.
Mitogen-Activated Protein Kinase 3 (MAPK3), also known as extracellular signal-regulated kinase 1 (ERK1), is a serine/threonine protein kinase that plays a crucial role in intracellular signal transduction pathways. It is involved in the regulation of various cellular processes, including proliferation, differentiation, and survival, in response to extracellular stimuli such as growth factors, hormones, and stress.
MAPK3 is activated through a phosphorylation cascade that involves the activation of upstream MAPK kinases (MKK or MEK). Once activated, MAPK3 can phosphorylate and activate various downstream targets, including transcription factors, to regulate gene expression. Dysregulation of MAPK3 signaling has been implicated in several diseases, including cancer and neurological disorders.
Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).
Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.
Substrate specificity can be categorized as:
1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.
Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.
Glycerol kinase
Glycerol kinase deficiency
List of OMIM disorder codes
Debbie C. Crans
Glycerol 3-phosphate
Glycerol
FGGY carbohydrate kinase family
Hyperglycerolemia
Colorimetric analysis
Choline kinase
1-Aminocyclopropane-1-carboxylate synthase
Morpheein
Protein moonlighting
Cold hardening
VDAC2
VDAC3
DAX1
Toxic Small RNA
Dipalmitoylphosphatidylcholine
IL1RAPL1
Glycerol-3-phosphate dehydrogenase
Fructolysis
PEP group translocation
Ether lipid
Voltage-dependent anion channel
Lipolysis
Lethal synthesis
Sterile alpha motif
Fructose
Adrenal insufficiency
Glycerol kinase - Wikipedia
Gk5 MGI Mouse Gene Detail - MGI:2443336 - glycerol kinase 5
Glycerol kinase (Haemophilus influenzae Rd KW20) | Protein Target - PubChem
Mechanistic and kinetics elucidation of Mg|sup|2+|/sup|/ATP molar ratio effect on glycerol kinase - Fingerprint - Welcome...
Glycerol Kinase Deficiency - Metabolic Support UK
Glycerol Kinase - Hzymes
The <i>Aspergillus fumigatus</i> Phosphoproteome Reveals Roles of High-Osmolarity Glycerol Mitogen-Activated Protein Kinases in...
Glycerol Kinase - Sekisui Diagnostics
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510(k) Premarket Notification
PharmacoSTORM nanoscale pharmacology reveals cariprazine binding on Islands of Calleja granule cells | Nature Communications
Recombinant Human PFKFB2 GST (N-Term) Protein (H00005208-Q01): Novus Biologicals
glycerol-3-phosphate metabolic process - Ontology Report - Rat Genome Database
NHANES 2007-2008: Cholesterol - LDL & Triglycerides Data Documentation, Codebook, and Frequencies
Chapter 22 Flashcards
RAB14 Antibody (NBP1-84720): Novus Biologicals
PDB 1r59
Human Metabolome Database: Showing metabocard for Glycerol 3-phosphate (HMDB0000126)
Adrenal Hypoplasia: Practice Essentials, Pathophysiology, Etiology
X-linked adrenal hypoplasia congenita: MedlinePlus Genetics
JCI - PPARγ regulates adipocyte cholesterol metabolism via oxidized LDL receptor 1
Feedback on Soma Side Effects and Usage, page 17 - AskDocWeb.com
The JAX Synteny Browser for mouse-human comparative genomics. - SyMAP - Synteny browser for plant genomes, including Medicago...
Peroxisomal compartmentalization of amino acid biosynthesis reactions imposes an upper limit on compartment size | bioRxiv
WikiGenes - Angioneurotic Edema
RCSB PDB - 1X3N: Crystal structure of AMPPNP bound Propionate kinase (TdcD) from Salmonella typhimurium
Publication : USDA ARS
Deficiency8
- Glycerol Kinase Deficiency occurs when the glycerol kinase gene which is found on the locus Xp21 of the X chromosome, is deleted or mutated (changed). (metabolicsupportuk.org)
- When someone suffers from glycerol kinase deficiency, many of the glycerol molecules that are released into the bloodstream do not get converted to DHAP (dihydroxyacetone phosphate) like they should be because there is not enough of the enzyme to catalyse (cause or accelerate a reaction) all the reactions that are meant to occur. (metabolicsupportuk.org)
- Glycerol Kinase Deficiency is an inherited condition. (metabolicsupportuk.org)
- Rarely, the entire NR0B1 gene is deleted along with other neighboring genes, resulting in the development of X-linked adrenal hypoplasia with hypoplasia congenita and other diseases, such as Duchenne and Becker muscular dystrophy and glycerol kinase deficiency. (medlineplus.gov)
- Mutations in this gene are associated with glycerol kinase deficiency (GKD). (platcovid.com)
- many patients with this deficiency also have a chromosomal deletion that extends beyond the glycerol kinase gene into the contiguous gene region, which contains the genes for congenital adrenal hypoplasia and Duchenne muscular dystrophy. (msdmanuals.com)
- Thus, patients with glycerol kinase deficiency may have one or more of these disease entities. (msdmanuals.com)
- Glycerol kinase deficiency, if present, does not result in morbidity but results in hyperglycerolemia. (medscape.com)
GlpK5
- The genes encoding the glycerol facilitator, glpF, and glycerol kinase, glpK, were isolated on a 4.5 kb EcoRl fragment from a chromosomal mini-library by functional complementation of an Escherichia coli glpK mutant after establishing a map of the chromosomal glpFK region with the help of a PCR-amplified glpK segment. (nau.edu)
- Schweizer, HP , Jump, R & Po, C 1997, ' Structure and gene-polypeptide relationships of the region encoding glycerol diffusion facilitator (glpF) and glycerol kinase (glpK) of Pseudomonas aeruginosa ', Microbiology , vol. 143, no. 4, pp. 1287-1297. (nau.edu)
- In the study, glycerol uptake facilitator or aquaglyceroporin gene (glpF) and glycerol kinase (glpK) gene were PCR-cloned from E. coli, inserted into a shuttle vector pBS29P2gfp, and expressed in P. chlororaphis by a Pseudomonas promoter P2. (usda.gov)
- The simultaneous expression of glpF and glpK resulted in an increased rate of glycerol metabolism for cell growth of P. chlororaphis. (usda.gov)
- 1.9 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with glycerol. (edu.pl)
Dehydrogenase2
- Converted from glycerol 3-phosphate to dihydroxyacetone phosphate (DHAP) via glycerol 3-phosphate dehydrogenase. (wikipedia.org)
- Glycerol 3-phospate may then be converted by dehydrogenation to dihydroxyacetone phosphate (DHAP) by the enzyme glycerol-3-phosphate dehydrogenase. (hmdb.ca)
Metabolism8
- A second protein, glycerol kinase, is involved in entry of external glycerol into cellular metabolism by trapping glycerol in the cytoplasm as sn-glycerol 3-phosphate. (nau.edu)
- The P. chlororaphis recombinants were then tested for cell growth and glycerol metabolism in chemically defined medium containing 0.5 and 1.0 % glycerol. (usda.gov)
- This protein is a key enzyme in the regulation of glycerol uptake and metabolism. (platcovid.com)
- Overview of Fatty Acid and Glycerol Metabolism Disorders Fatty acids are the preferred energy source for the heart and an important energy source for skeletal muscle during prolonged exertion. (msdmanuals.com)
- Symptoms of glycerol metabolism disorders begin at any age and are usually accompanied by acidosis, hypoglycemia, and elevated blood and urine levels of glycerol. (msdmanuals.com)
- Diagnosis of glycerol metabolism disorders is by detecting an elevated level of glycerol in serum and urine and is confirmed by DNA analysis. (msdmanuals.com)
- Glycerol metabolism disorder treatment is with a low-fat diet, but glucocorticoid replacement is critical for patients with adrenal hypoplasia. (msdmanuals.com)
- Accumulating evidence suggests that dysregulated glycerol metabolism contributes to the pathophysiology of obesity and type 2 diabetes. (lu.se)
Enzyme glycerol kinase1
- Glycerol 3-phosphate is produced from glycerol, the triose sugar backbone of triglycerides and glycerophospholipids, by the enzyme glycerol kinase. (hmdb.ca)
Triglycerides and glycerophospholipids1
- Glycerol kinase, encoded by the gene GK, is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. (wikipedia.org)
Acetate2
- Propionate kinase, like acetate kinase, contains a fold with the topology betabetabetaalphabetaalphabetaalpha, identical with that of glycerol kinase, hexokinase, heat shock cognaten 70 (Hsc70) and actin, the superfamily of phosphotransferases. (rcsb.org)
- Comparison of TdcD complex structures with those of acetate and sugar kinase/Hsc70/actin obtained with different ligands has permitted the identification of catalytically essential residues involved in substrate binding and catalysis, and points to both structural and mechanistic similarities. (rcsb.org)
High-osmolarity glycerol2
- fumigatus and high-osmolarity glycerol (HOG) pathway MAPK mutants upon cell wall damage. (bath.ac.uk)
- In addition, we are currently analysing the role of the MAPK of the High Osmolarity Glycerol (HOG) pathway, CgHog1. (boku.ac.at)
Dihydroxyacetone1
- G3P is acted upon by glycerol phosphate oxidase to produce dihydroxyacetone phosphate and hydrogen peroxide. (cdc.gov)
Protein kinase3
- The mitogen-activated protein kinase (MAPK) signaling pathways are essential to the adaptation to the human host. (bath.ac.uk)
- Checkpoint kinase 1 (Chk1, CHEK1) is a Ser/Thr protein kinase that plays a key role in mediating the cellular response to DNA-damage. (rcsb.org)
- Here, we propose a molecular mechanism where the AQP7 mobility in adipocytes is dependent on perilipin 1 and protein kinase A. Biochemical analyses combined with ex vivo studies in human primary adipocytes, demonstrate that perilipin 1 binds to AQP7, and that catecholamine activated protein kinase A phosphorylates the N-terminus of AQP7, thereby reducing complex formation. (lu.se)
Uptake1
- Aquaporin-9 Protein Is the Primary Route of Hepatocyte Glycerol Uptake for Glycerol Gluconeogenesis in Mice. (lu.se)
Adipocytes4
- ADP + sn-glycerol 3-phosphate Adipocytes lack glycerol kinase so they cannot metabolize the glycerol produced during triacyl glycerol degradation. (wikipedia.org)
- Glycerol efflux from adipocytes is regulated by the aquaglyceroporin AQP7, which is translocated upon hormone stimulation. (lu.se)
- Together, these findings are indicative of how glycerol release is controlled in adipocytes, and may pave the. (lu.se)
- Regulation of glycerol efflux in adipocytes. (lu.se)
Glycerokinase1
- Glycerol Kinase (alternative name, ATP:glycerol 3-phosphotransferase or Glycerokinase) adopts a ribonuclease H-like fold consisting of an alpha-beta 2-layer sandwich of CATH family 3.30.420.40. (wikipedia.org)
FGGY1
- The protein encoded by this gene belongs to the FGGY kinase family. (platcovid.com)
Sodium Azide1
- Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. (fishersci.com)
Lipase1
- The second reaction is driven by the reagents from bottle 1, with lipase added in reagent 2 to convert triglycerides to glycerol, and 4-aminophenzone added to react with the hydrogen peroxide produced in the last reaction. (cdc.gov)
Glycolysis1
- Glycerol 3-phosphate is a chemical intermediate in the glycolysis metabolic pathway. (hmdb.ca)
Cytoplasmic2
- The glycerol facilitator is one of the few known examples of bacterial solute transport proteins that catalyse facilitated diffusion across the cytoplasmic membrane. (nau.edu)
- Focal Adhesion Kinase (FAK) is a cytoplasmic tyrosine kinase that colocalizes with integrins in focal adhesions. (fishersci.com)
Carbohydrate1
- Two ORFs, orfX and orfY, encoding a putative regulatory protein and a carbohydrate kinase of unknown function, were located upstream of the glpFK operon. (nau.edu)
Metabolic1
- The objective of this study is to improve by genetic engineering the glycerol metabolic capability of Pseudomonas chlororaphis which is capable of producing commercially valuable biodegradable poly(hydroxyalkanoate) (PHA) and biosurfactant rhamnolipids (RLs). (usda.gov)
Facilitator1
- The glycerol facilitator and glycerol kinase were identified in a T7 expression system as proteins with apparent molecular masses of 25 and 56 kDa, respectively. (nau.edu)
Enzymes1
- The aim of this study was to develop a platform of Mycobacterium tuberculosis (Mtb) kinase enzymes that may be used for the identification of therapeutically relevant ethnobotanical extracts that will allow drug target identification, as well as the subsequent isolation of the active compounds. (biomedcentral.com)
Pseudomonas2
- Evidence is presented that glycerol transport in Pseudomonas aeruginosa is mediated by a similar transport system. (nau.edu)
- This study reports the successful genetic engineering (GE) of the Pseudomonas chlororaphis to result in improved strain capable of consuming the glycerol substrate at a faster rate, thus cutting down on the production time and therefore making the bioprocess more cost-friendly. (usda.gov)
Phosphorylation3
- It catalyzes the phosphorylation of glycerol by ATP, yielding ADP and glycerol-3-phosphate. (platcovid.com)
- The binding of extracellular matrix ligands to integrins triggers autophosphorylation at Tyr-397, and activation of FAK through phosphorylation of Tyr residues (Tyr-576 and Tyr577) in the kinase domain activation loop. (fishersci.com)
- In addition, phosphorylation of other Tyr residues (Tyr-925, and Tyr-861) creates binding sites for SH2 domains of intracellular signaling molecules such as Src, PI3 kinase, and Grb2. (fishersci.com)
Blood and urine1
- GKD is diagnosed through specialised blood and urine tests to find the amount of glycerol present. (metabolicsupportuk.org)
Fatty1
- Triglycerides are fatty acid esters of glycerol that have three hydroxyl groups. (cdc.gov)
MAPK1
- Our global phosphoproteome network analysis showed an enrichment for protein kinases, RNA recognition motif domains, and the MAPK signaling pathway. (bath.ac.uk)
Aquaporin2
Phosphoric1
- The chemical reactions and pathways involving glycerol-3-phosphate, a phosphoric monoester of glycerol. (mcw.edu)
Catalyzes1
- An enzyme that catalyzes the formation of glycerol 3-phosphate from ATP and glycerol. (nih.gov)
Genetics1
- This showed the involvement of the HOG pathway and identified novel protein kinases and transcription factors, which were confirmed by fungal genetics to be involved in promoting tolerance of cell wall damage. (bath.ac.uk)
Aqueous1
- The 50% inhibitory concentration (IC 50 ) of an aqueous root extract of P. sidoides against the kinases indicated SK has an IC 50 of 1.2 μg/ml and GK 1.4 μg/ml. (biomedcentral.com)
Molecules1
- This results in the extra molecules of glycerol left floating around in the cell which can cause serious damage when left untreated. (metabolicsupportuk.org)
Identification1
- This study suggests P. sidoides is potentially a source of anti-tubercular compounds and the Mtb kinase platform has significant potential as a tool for the subsequent screening of P. sidoides extracts and plant extracts in general, for compound identification and elaboration by selected extract target inhibitor profiling. (biomedcentral.com)
Type1
- In contrast to the wild-type strain, there is an overall decrease of differentially phosphorylated kinases and phosphatases in ΔsakA, ΔmpkC, and ΔsakA ΔmpkC mutants. (bath.ac.uk)
Source1
- This mutant no longer transported glycerol and could no longer utilize it as sole carbon and energy source. (nau.edu)
Liver1
- This glycerol is instead shuttled to the liver via the blood where it is: Phosphorylated by glycerol kinase to glycerol 3-phosphate. (wikipedia.org)