An enzyme that catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP. It is important in the glycolysis process. EC 2.7.2.1.
An enzyme that catalyzes the synthesis of acetylphosphate from acetyl-CoA and inorganic phosphate. Acetylphosphate serves as a high-energy phosphate compound. EC 2.3.1.8.
Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.
A genus of anaerobic, irregular spheroid-shaped METHANOSARCINALES whose organisms are nonmotile. Endospores are not formed. These archaea derive energy via formation of methane from acetate, methanol, mono-, di-, and trimethylamine, and possibly, carbon monoxide. Organisms are isolated from freshwater and marine environments.
Carbon-containing phosphoric acid derivatives. Included under this heading are compounds that have CARBON atoms bound to one or more OXYGEN atoms of the P(=O)(O)3 structure. Note that several specific classes of endogenous phosphorus-containing compounds such as NUCLEOTIDES; PHOSPHOLIPIDS; and PHOSPHOPROTEINS are listed elsewhere.
A class of enzymes that transfers phosphate groups and has a carboxyl group as an acceptor. EC 2.7.2.
A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.
A genus of gram-negative, anaerobic cocci parasitic in the mouth and in the intestinal and respiratory tracts of man and other animals.
An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.
Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.
Product of the oxidation of ethanol and of the destructive distillation of wood. It is used locally, occasionally internally, as a counterirritant and also as a reagent. (Stedman, 26th ed)
An intracellular signaling system involving the MAP kinase cascades (three-membered protein kinase cascades). Various upstream activators, which act in response to extracellular stimuli, trigger the cascades by activating the first member of a cascade, MAP KINASE KINASE KINASES; (MAPKKKs). Activated MAPKKKs phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES which in turn phosphorylate the MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs). The MAPKs then act on various downstream targets to affect gene expression. In mammals, there are several distinct MAP kinase pathways including the ERK (extracellular signal-regulated kinase) pathway, the SAPK/JNK (stress-activated protein kinase/c-jun kinase) pathway, and the p38 kinase pathway. There is some sharing of components among the pathways depending on which stimulus originates activation of the cascade.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
A phorbol ester found in CROTON OIL with very effective tumor promoting activity. It stimulates the synthesis of both DNA and RNA.
Agents that inhibit PROTEIN KINASES.
A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)
The rate dynamics in chemical or physical systems.
An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.
A PROTEIN-TYROSINE KINASE family that was originally identified by homology to the Rous sarcoma virus ONCOGENE PROTEIN PP60(V-SRC). They interact with a variety of cell-surface receptors and participate in intracellular signal transduction pathways. Oncogenic forms of src-family kinases can occur through altered regulation or expression of the endogenous protein and by virally encoded src (v-src) genes.
Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A mitogen-activated protein kinase subfamily that regulates a variety of cellular processes including CELL GROWTH PROCESSES; CELL DIFFERENTIATION; APOPTOSIS; and cellular responses to INFLAMMATION. The P38 MAP kinases are regulated by CYTOKINE RECEPTORS and can be activated in response to bacterial pathogens.
Derivatives of BUTYRIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxypropane structure.
A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A rod-shaped bacterium surrounded by a sheath-like structure which protrudes balloon-like beyond the ends of the cell. It is thermophilic, with growth occurring at temperatures as high as 90 degrees C. It is isolated from geothermally heated marine sediments or hot springs. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
A proline-directed serine/threonine protein kinase which mediates signal transduction from the cell surface to the nucleus. Activation of the enzyme by phosphorylation leads to its translocation into the nucleus where it acts upon specific transcription factors. p40 MAPK and p41 MAPK are isoforms.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
A group of enzymes that catalyzes the transfer of a phosphate group onto a nitrogenous group acceptor. EC 2.7.3.
Enzymes that catalyze the cleavage of a carbon-carbon bond by means other than hydrolysis or oxidation. This subclass contains the DECARBOXYLASES, the ALDEHYDE-LYASES, and the OXO-ACID-LYASES. EC 4.1.
A family of gram-negative bacteria in the order Rhodocyclales, class BETAPROTEOBACTERIA. It includes many genera previously assigned to the family PSEUDOMONADACEAE.
Release of oil into the environment usually due to human activity.
A class in the phylum PROTEOBACTERIA comprised of chemoheterotrophs and chemoautotrophs which derive nutrients from decomposition of organic material.
The fern plant family of the order Polypodiales, class Filicopsida, division Pteridophyta, subkingdom Tracheobionta.
Organic compounds containing carbon and hydrogen in the form of an unsaturated, usually hexagonal ring structure. The compounds can be single ring, or double, triple, or multiple fused rings.

Purification and characterization of two extremely thermostable enzymes, phosphate acetyltransferase and acetate kinase, from the hyperthermophilic eubacterium Thermotoga maritima. (1/86)

Phosphate acetyltransferase (PTA) and acetate kinase (AK) of the hyperthermophilic eubacterium Thermotoga maritima have been purified 1,500- and 250-fold, respectively, to apparent homogeneity. PTA had an apparent molecular mass of 170 kDa and was composed of one subunit with a molecular mass of 34 kDa, suggesting a homotetramer (alpha4) structure. The N-terminal amino acid sequence showed significant identity to that of phosphate butyryltransferases from Clostridium acetobutylicum rather than to those of known phosphate acetyltransferases. The kinetic constants of the reversible enzyme reaction (acetyl-CoA + Pi -->/<-- acetyl phosphate + CoA) were determined at the pH optimum of pH 6.5. The apparent Km values for acetyl-CoA, Pi, acetyl phosphate, and coenzyme A (CoA) were 23, 110, 24, and 30 microM, respectively; the apparent Vmax values (at 55 degrees C) were 260 U/mg (acetyl phosphate formation) and 570 U/mg (acetyl-CoA formation). In addition to acetyl-CoA (100%), the enzyme accepted propionyl-CoA (60%) and butyryl-CoA (30%). The enzyme had a temperature optimum at 90 degrees C and was not inactivated by heat upon incubation at 80 degrees C for more than 2 h. AK had an apparent molecular mass of 90 kDa and consisted of one 44-kDa subunit, indicating a homodimer (alpha2) structure. The N-terminal amino acid sequence showed significant similarity to those of all known acetate kinases from eubacteria as well that of the archaeon Methanosarcina thermophila. The kinetic constants of the reversible enzyme reaction (acetyl phosphate + ADP -->/<-- acetate + ATP) were determined at the pH optimum of pH 7.0. The apparent Km values for acetyl phosphate, ADP, acetate, and ATP were 0.44, 3, 40, and 0.7 mM, respectively; the apparent Vmax values (at 50 degrees C) were 2,600 U/mg (acetate formation) and 1,800 U/mg (acetyl phosphate formation). AK phosphorylated propionate (54%) in addition to acetate (100%) and used GTP (100%), ITP (163%), UTP (56%), and CTP (21%) as phosphoryl donors in addition to ATP (100%). Divalent cations were required for activity, with Mn2+ and Mg2+ being most effective. The enzyme had a temperature optimum at 90 degrees C and was stabilized against heat inactivation by salts. In the presence of (NH4)2SO4 (1 M), which was most effective, the enzyme did not lose activity upon incubation at 100 degrees C for 3 h. The temperature optimum at 90 degrees C and the high thermostability of both PTA and AK are in accordance with their physiological function under hyperthermophilic conditions.  (+info)

Cloning, sequence analysis, expression and inactivation of the Corynebacterium glutamicum pta-ack operon encoding phosphotransacetylase and acetate kinase. (2/86)

The Corynebacterium glutamicum ack and pta genes encoding the acetate-activating enzymes acetate kinase and phosphotransacetylase were isolated, subcloned on a plasmid and re-introduced into Corynebacterium glutamicum. Relative to the wild-type, the recombinant strains showed about tenfold higher specific activities of both enzymes. Sequence analysis of a 3657 bp DNA fragment revealed that the ack and pta genes are contiguous in the corynebacterial chromosome, with pta upstream and the last nucleotide of the pta stop codon (TAA) overlapping the first of the ack start codon (ATG). The predicted gene product of pta consists of 329 amino acids (Mr 35242), that of ack consists of 397 amino acids (Mr 43098) and the amino acid sequences of the two polypeptides show up to 60 % (phosphotransacetylase) and 53% (acetate kinase) identity in comparison with respective enzymes from other organisms. Northern (RNA) blot hybridizations using pta- and ack-specific probes and transcriptional cat fusion experiments revealed that the two genes are transcribed as a 2.5 kb bicistronic mRNA and that the expression of this operon is induced when Corynebacterium glutamicum grows on acetate instead of glucose as a carbon source. Directed inactivation of the chromosomal pta and ack genes led to the absence of detectable phosphotransacetylase and acetate kinase activity in the respective mutants and to their inability to grow on acetate. These data indicate that no isoenzymes of acetate kinase and phosphotransacetylase are present in Corynebacterium glutamicum and that a functional acetate kinase/phosphotransacetylase pathway is essential for growth of this organism on acetate.  (+info)

Genes coding for phosphotransacetylase and acetate kinase in Sinorhizobium meliloti are in an operon that is inducible by phosphate stress and controlled by phoB. (3/86)

Recent work in this laboratory has shown that the gene coding for acetate kinase (ackA) in Sinorhizobium meliloti is up-regulated in response to phosphate limitation. Characterization of the region surrounding ackA revealed that it is adjacent to pta, which codes for phosphotransacetylase, and that these two genes are part of an operon composed of at least two additional genes in the following order: an open reading frame (orfA), pta, ackA, and the partial sequence of a gene with an inferred peptide that has a high degree of homology to enoyl-ACP reductase (fabI). Experiments combining enzyme assays, a chromosomal lacZ::ackA transcriptional fusion, complementation analysis with cosmid subclones, and the creation of mutations in pta and ackA all indicated that the orfA-pta-ackA-fabI genes are cotranscribed in response to phosphate starvation. Primer extension was used to map the position of the phosphate starvation-inducible transcriptional start sites upstream of orfA. The start sites were found to be preceded by a sequence having similarity to PHO boxes from other phosphate-regulated genes in S. meliloti and to the consensus PHO box in Escherichia coli. Introduction of a phoB mutation in the wild-type strain eliminated elevated levels of acetate kinase and phosphotransacetylase activities in response to phosphate limitation and also eliminated the phosphate stress-induced up-regulation of the ackA::lacZ fusion. Mutations in either ackA alone or both pta and ackA did not affect the nodulation or nitrogen fixation phenotype of S. meliloti.  (+info)

Homofermentative production of D- or L-lactate in metabolically engineered Escherichia coli RR1. (4/86)

We investigated metabolic engineering of fermentation pathways in Escherichia coli for production of optically pure D- or L-lactate. Several pta mutant strains were examined, and a pta mutant of E. coli RR1 which was deficient in the phosphotransacetylase of the Pta-AckA pathway was found to metabolize glucose to D-lactate and to produce a small amount of succinate by-product under anaerobic conditions. An additional mutation in ppc made the mutant produce D-lactate like a homofermentative lactic acid bacterium. When the pta ppc double mutant was grown to higher biomass concentrations under aerobic conditions before it shifted to the anaerobic phase of D-lactate production, more than 62.2 g of D-lactate per liter was produced in 60 h, and the volumetric productivity was 1.04 g/liter/h. To examine whether the blocked acetate flux could be reoriented to a nonindigenous L-lactate pathway, an L-lactate dehydrogenase gene from Lactobacillus casei was introduced into a pta ldhA strain which lacked phosphotransacetylase and D-lactate dehydrogenase. This recombinant strain was able to metabolize glucose to L-lactate as the major fermentation product, and up to 45 g of L-lactate per liter was produced in 67 h. These results demonstrate that the central fermentation metabolism of E. coli can be reoriented to the production of D-lactate, an indigenous fermentation product, or to the production of L-lactate, a nonindigenous fermentation product.  (+info)

Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium. (5/86)

We have previously reported the isolation of a group of anaerobically regulated, fnr-dependent lac fusions in Salmonella typhimurium and have grouped these oxd genes into classes based on map position. In order to identify these genes, we have replaced the original Mud-lac fusion in a member of each oxd class with the much smaller Mud-cam element, cloned the fusion, and determined DNA sequence sufficient to define the oxd gene. Several of the fusions correspond to previously known genes from S. typhimurium or Escherichia coli: oxd-4 = cbiA and oxd-11 = cbiK, oxd-5 = hybB, oxd-7 = dcuB, oxd-8 = moaB, oxd-12 = dmsA, and oxd-14 = napB (aeg-46. 5). Two other fusions correspond to previously unknown loci: oxd-2 encodes an acetate/propionate kinase, and oxd-6 encodes a putative ABC transporter present in S. typhimurium but not in E. coli.  (+info)

Catabolite regulation of the pta gene as part of carbon flow pathways in Bacillus subtilis. (6/86)

In Bacillus subtilis, the products of the pta and ackA genes, phosphotransacetylase and acetate kinase, play a crucial role in the production of acetate, one of the most abundant by-products of carbon metabolism in this gram-positive bacterium. Although these two enzymes are part of the same pathway, only mutants with inactivated ackA did not grow in the presence of glucose. Inactivation of pta had only a weak inhibitory effect on growth. In contrast to pta and ackA in Escherichia coli, the corresponding B. subtilis genes are not cotranscribed. Expression of the pta gene was increased in the presence of glucose, as has been reported for ackA. The effects of the predicted cis-acting catabolite response element (CRE) located upstream from the promoter and of the trans-acting proteins CcpA, HPr, Crh, and HPr kinase on the catabolite regulation of pta were investigated. As for ackA, glucose activation was abolished in ccpA and hprK mutants and in the ptsH1 crh double mutant. Footprinting experiments demonstrated an interaction between CcpA and the pta CRE sequence, which is almost identical to the proposed CRE consensus sequence. This interaction occurs only in the presence of Ser-46-phosphorylated HPr (HPrSer-P) or Ser-46-phosphorylated Crh (CrhSer-P) and fructose-1,6-bisphosphate (FBP). In addition to CcpA, carbon catabolite activation of the pta gene therefore requires at least two other cofactors, FBP and either HPr or Crh, phosphorylated at Ser-46 by the ATP-dependent Hpr kinase.  (+info)

The role of histidines in the acetate kinase from Methanosarcina thermophila. (7/86)

The role of histidine in the catalytic mechanism of acetate kinase from Methanosarcina thermophila was investigated by diethylpyrocarbonate inactivation and site-directed mutagenesis. Inactivation was accompanied by an increase in absorbance at 240 nm with no change in absorbance at 280 nm, and treatment of the inactivated enzyme with hydroxylamine restored 95% activity, results that indicated diethylpyrocarbonate inactivates the enzyme by the specific modification of histidine. The substrates ATP, ADP, acetate, and acetyl phosphate protected against inactivation suggesting at least one active site where histidine is modified. Correlation of residual activity with the number of histidines modified, as determined by absorbance at 240 nm, indicated that a maximum of three histidines are modified per subunit, two of which are essential for full inactivation. Comparison of the M. thermophila acetate kinase sequence with 56 putative acetate kinase sequences revealed eight highly conserved histidines, three of which (His-123, His-180, and His-208) are perfectly conserved. Diethylpyrocarbonate inactivation of the eight histidine --> alanine variants indicated that His-180 and His-123 are in the active site and that the modification of both is necessary for full inactivation. Kinetic analyses of the eight variants showed that no other histidines are important for activity. Analysis of additional His-180 variants indicated that phosphorylation of His-180 is not essential for catalysis. Possible functions of His-180 are discussed.  (+info)

Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases. (8/86)

Acetate kinase, an enzyme widely distributed in the Bacteria and Archaea domains, catalyzes the phosphorylation of acetate. We have determined the three-dimensional structure of Methanosarcina thermophila acetate kinase bound to ADP through crystallography. As we previously predicted, acetate kinase contains a core fold that is topologically identical to that of the ADP-binding domains of glycerol kinase, hexokinase, the 70-kDa heat shock cognate (Hsc70), and actin. Numerous charged active-site residues are conserved within acetate kinases, but few are conserved within the phosphotransferase superfamily. The identity of the points of insertion of polypeptide segments into the core fold of the superfamily members indicates that the insertions existed in the common ancestor of the phosphotransferases. Another remarkable shared feature is the unusual, epsilon conformation of the residue that directly precedes a conserved glycine residue (Gly-331 in acetate kinase) that binds the alpha-phosphate of ADP. Structural, biochemical, and geochemical considerations indicate that an acetate kinase may be the ancestral enzyme of the ASKHA (acetate and sugar kinases/Hsc70/actin) superfamily of phosphotransferases.  (+info)

Acetate kinase is an enzyme that catalyzes the reversible phosphorylation of acetate to form acetyl phosphate and ADP (adenosine diphosphate) from ATP (adenosine triphosphate). The reaction is as follows:

Acetate + ATP -> Acetyl phosphate + ADP

This enzyme plays a role in the metabolism of certain bacteria and archaea, where it helps to generate energy in the form of ATP. It is not typically found in humans or other mammals.

Phosphate Acetyltransferase (PAT) is an enzyme involved in the metabolism of certain amino acids. It catalyzes the transfer of a phosphate group from acetyl phosphate to a variety of acceptor molecules, including carbon, nitrogen, and sulfur nucleophiles. This reaction plays a crucial role in several biochemical pathways, such as the biosynthesis of certain amino acids, vitamins, and cofactors.

The systematic name for this enzyme is acetylphosphate-protein phosphotransferase. It belongs to the family of transferases, specifically those transferring phosphorus-containing groups. The gene that encodes this enzyme in humans is called PAT1 or CABYR. Defects in this gene have been associated with certain neurological disorders.

Acetates, in a medical context, most commonly refer to compounds that contain the acetate group, which is an functional group consisting of a carbon atom bonded to two hydrogen atoms and an oxygen atom (-COO-). An example of an acetate is sodium acetate (CH3COONa), which is a salt formed from acetic acid (CH3COOH) and is often used as a buffering agent in medical solutions.

Acetates can also refer to a group of medications that contain acetate as an active ingredient, such as magnesium acetate, which is used as a laxative, or calcium acetate, which is used to treat high levels of phosphate in the blood.

In addition, acetates can also refer to a process called acetylation, which is the addition of an acetyl group (-COCH3) to a molecule. This process can be important in the metabolism and regulation of various substances within the body.

Methanosarcina is a genus of archaea, which are single-celled microorganisms that lack a nucleus and other membrane-bound organelles. These archaea are characterized by their ability to produce methane as a metabolic byproduct during the process of anaerobic respiration or fermentation. Methanosarcina species are found in various environments, including freshwater and marine sediments, waste treatment facilities, and the digestive tracts of animals. They are capable of degrading a wide range of organic compounds, such as acetate, methanol, and methylamines, to produce methane. It's important to note that while Methanosarcina species can be beneficial in certain environments, they may also contribute to the release of greenhouse gases, particularly methane, which is a potent contributor to climate change.

Organophosphates are a group of chemicals that include insecticides, herbicides, and nerve gases. They work by inhibiting an enzyme called acetylcholinesterase, which normally breaks down the neurotransmitter acetylcholine in the synapse between nerves. This leads to an overaccumulation of acetylcholine, causing overstimulation of the nervous system and resulting in a wide range of symptoms such as muscle twitching, nausea, vomiting, diarrhea, sweating, confusion, and potentially death due to respiratory failure. Organophosphates are highly toxic and their use is regulated due to the risks they pose to human health and the environment.

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.

Veillonella is a genus of Gram-negative, anaerobic, non-spore-forming, coccoid or rod-shaped bacteria. These bacteria are commonly found as normal flora in the human mouth, intestines, and female genital tract. They are known to be obligate parasites, meaning they rely on other organisms for nutrients and energy. Veillonella species are often associated with dental caries and have been implicated in various infections such as bacteremia, endocarditis, pneumonia, and wound infections, particularly in immunocompromised individuals or those with underlying medical conditions. Proper identification of Veillonella species is important for the diagnosis and treatment of these infections.

Acetate-CoA ligase is an enzyme that plays a role in the metabolism of acetate in cells. The enzyme catalyzes the conversion of acetate and coenzyme A (CoA) to acetyl-CoA, which is a key molecule in various metabolic pathways, including the citric acid cycle (also known as the Krebs cycle).

The reaction catalyzed by Acetate-CoA ligase can be summarized as follows:

acetate + ATP + CoA → acetyl-CoA + AMP + PPi

In this reaction, acetate is activated by combining it with ATP to form acetyl-AMP, which then reacts with CoA to produce acetyl-CoA. The reaction also produces AMP and pyrophosphate (PPi) as byproducts.

There are two main types of Acetate-CoA ligases: the short-chain fatty acid-CoA ligase, which is responsible for activating acetate and other short-chain fatty acids, and the acyl-CoA synthetase, which activates long-chain fatty acids. Both types of enzymes play important roles in energy metabolism and the synthesis of various biological molecules.

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.

Acetic acid is an organic compound with the chemical formula CH3COOH. It is a colorless liquid with a pungent, vinegar-like smell and is the main component of vinegar. In medical terms, acetic acid is used as a topical antiseptic and antibacterial agent, particularly for the treatment of ear infections, external genital warts, and nail fungus. It can also be used as a preservative and solvent in some pharmaceutical preparations.

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.

Tetradecanoylphorbol acetate (TPA) is defined as a pharmacological agent that is a derivative of the phorbol ester family. It is a potent tumor promoter and activator of protein kinase C (PKC), a group of enzymes that play a role in various cellular processes such as signal transduction, proliferation, and differentiation. TPA has been widely used in research to study PKC-mediated signaling pathways and its role in cancer development and progression. It is also used in topical treatments for skin conditions such as psoriasis.

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.

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.

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.

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.

Fermentation is a metabolic process in which an organism converts carbohydrates into alcohol or organic acids using enzymes. In the absence of oxygen, certain bacteria, yeasts, and fungi convert sugars into carbon dioxide, hydrogen, and various end products, such as alcohol, lactic acid, or acetic acid. This process is commonly used in food production, such as in making bread, wine, and beer, as well as in industrial applications for the production of biofuels and chemicals.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

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.

Butyrates are a type of fatty acid, specifically called short-chain fatty acids (SCFAs), that are produced in the gut through the fermentation of dietary fiber by gut bacteria. The name "butyrate" comes from the Latin word for butter, "butyrum," as butyrate was first isolated from butter.

Butyrates have several important functions in the body. They serve as a primary energy source for colonic cells and play a role in maintaining the health and integrity of the intestinal lining. Additionally, butyrates have been shown to have anti-inflammatory effects, regulate gene expression, and may even help prevent certain types of cancer.

In medical contexts, butyrate supplements are sometimes used to treat conditions such as ulcerative colitis, a type of inflammatory bowel disease (IBD), due to their anti-inflammatory properties and ability to promote gut health. However, more research is needed to fully understand the potential therapeutic uses of butyrates and their long-term effects on human health.

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.

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.

"Thermotoga maritima" is not a medical term, but rather a scientific name for a specific type of bacterium. It belongs to the domain Archaea and is commonly found in marine environments with high temperatures, such as hydrothermal vents. The bacterium is known for its ability to survive in extreme conditions and has been studied for its potential industrial applications, including the production of biofuels and enzymes.

In a medical context, "Thermotoga maritima" may be relevant in research related to the development of new drugs or therapies, particularly those that involve extremophile organisms or their enzymes. However, it is not a term used to describe a specific medical condition or treatment.

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.

Adenosine diphosphate (ADP) is a chemical compound that plays a crucial role in energy transfer within cells. It is a nucleotide, which consists of a adenosine molecule (a sugar molecule called ribose attached to a nitrogenous base called adenine) and two phosphate groups.

In the cell, ADP functions as an intermediate in the conversion of energy from one form to another. When a high-energy phosphate bond in ADP is broken, energy is released and ADP is converted to adenosine triphosphate (ATP), which serves as the main energy currency of the cell. Conversely, when ATP donates a phosphate group to another molecule, it is converted back to ADP, releasing energy for the cell to use.

ADP also plays a role in blood clotting and other physiological processes. In the coagulation cascade, ADP released from damaged red blood cells can help activate platelets and initiate the formation of a blood clot.

Carbon-carbon lyases are a class of enzymes that catalyze the breaking of carbon-carbon bonds in a substrate, resulting in the formation of two molecules with a double bond between them. This reaction is typically accompanied by the release or addition of a cofactor such as water or a coenzyme.

These enzymes play important roles in various metabolic pathways, including the breakdown of carbohydrates, lipids, and amino acids. They are also involved in the biosynthesis of secondary metabolites, such as terpenoids and alkaloids.

Carbon-carbon lyases are classified under EC number 4.1.2. in the Enzyme Commission (EC) system. This classification includes a wide range of enzymes with different substrate specificities and reaction mechanisms. Examples of carbon-carbon lyases include decarboxylases, aldolases, and dehydratases.

It's worth noting that the term "lyase" refers to any enzyme that catalyzes the removal of a group of atoms from a molecule, leaving a double bond or a cycle, and it does not necessarily imply the formation of carbon-carbon bonds.

Rhodocyclaceae is a family of gram-negative, facultatively anaerobic bacteria that are commonly found in various environments such as soil, water, and the gastrointestinal tracts of animals. These bacteria are known for their ability to perform anaerobic respiration using various electron acceptors, including nitrate, sulfur compounds, and metals.

The family Rhodocyclaceae includes several genera of bacteria that have been reclassified from other families in the past few decades. Some notable genera within this family include:

* Rhodocyclus: These are aerobic, non-motile bacteria that form thick-walled cysts and are capable of using a variety of organic compounds as electron donors and acceptors for respiration.
* Dechloromonas: These are motile, gram-negative bacteria that can use chlorinated compounds as electron donors and reduce them to less harmful forms.
* Azonexus: These are aerobic, non-motile bacteria that can oxidize ammonia to nitrite and are often found in wastewater treatment plants.
* Aromatoleum: These are anaerobic, motile bacteria that can degrade aromatic compounds such as benzene and toluene.

Overall, the family Rhodocyclaceae is a diverse group of bacteria that play important roles in various biogeochemical cycles and have potential applications in bioremediation and other environmental technologies.

Petroleum pollution is not a medical term per se, but it is an environmental and public health issue. It refers to the contamination of the environment, particularly water bodies, soil, and air, by petroleum products or hydrocarbons. These pollutants can originate from various sources, including oil spills, leaks from underground storage tanks, runoff from roads, and improper disposal of industrial waste.

The health effects of petroleum pollution can vary depending on the type and amount of exposure. Short-term exposure to high levels of hydrocarbons can cause irritation to the eyes, skin, and respiratory tract, while long-term exposure has been linked to more severe health problems such as neurological damage, cancer, and reproductive issues. Therefore, it is crucial to prevent and mitigate petroleum pollution to protect both the environment and public health.

Betaproteobacteria is a class of proteobacteria, a group of gram-negative bacteria. This class includes several genera of bacteria that are widely distributed in the environment, and can be found in soil, water, and various organisms including humans. Some members of Betaproteobacteria are important pathogens, causing diseases such as meningitis, pneumonia, and urinary tract infections. Other members of this class are capable of breaking down environmental pollutants, making them useful in bioremediation applications.

I apologize for any confusion, but "Polypodiaceae" is not a medical term. It is a taxonomic category in botany, specifically a family of ferns known as the "Polypody Family." This family includes various species of leafy ferns that are commonly found growing on trees, rocks, and soil in many parts of the world. If you have any questions about a medical term or concept, I'd be happy to help clarify those for you.

Aromatic hydrocarbons, also known as aromatic compounds or arenes, are a class of organic compounds characterized by a planar ring structure with delocalized electrons that give them unique chemical properties. The term "aromatic" was originally used to describe their distinctive odors, but it now refers to their characteristic molecular structure and stability.

Aromatic hydrocarbons contain one or more benzene rings, which are cyclic structures consisting of six carbon atoms arranged in a planar hexagonal shape. Each carbon atom in the benzene ring is bonded to two other carbon atoms and one hydrogen atom, forming alternating double and single bonds between the carbon atoms. However, the delocalized electrons in the benzene ring are evenly distributed around the ring, leading to a unique electronic structure that imparts stability and distinctive chemical properties to aromatic hydrocarbons.

Examples of aromatic hydrocarbons include benzene, toluene, xylene, and naphthalene. These compounds have important uses in industry, but they can also pose health risks if not handled properly. Exposure to high levels of aromatic hydrocarbons has been linked to various health effects, including cancer, neurological damage, and respiratory problems.

In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production ... The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme ... Grundy FJ, Waters DA, Allen SH, Henkin TM (November 1993). "Regulation of the Bacillus subtilis acetate kinase gene by CcpA". J ... Salmonella typhimurium propionate kinase (StTdcD) catalyzes reversible transfer of the γ-phosphate of ATP to propionate during ...
Reeves RE, Guthrie JD (1975). "Acetate kinase (pyrophosphate). A fourth pyrophosphate-dependent kinase from Entamoeba ... an acetate kinase (diphosphate) (EC 2.7.2.12) is an enzyme that catalyzes the chemical reaction diphosphate + acetate ⇌ {\ ... The systematic name of this enzyme class is diphosphate:acetate phosphotransferase. This enzyme is also called pyrophosphate- ... the two substrates of this enzyme are diphosphate and acetate, whereas its two products are phosphate and acetyl phosphate. ...
... or Mn2+-dependent formation of acetyl-CoA from acetate and ATP catalyzed by acetate kinase, an essential reaction for priming ... Rose, Irwin A. (1955). "Acetate kinase of bacteria (acetokinase)". Methods Enzymol. 1: 591-595. doi:10.1016/0076-6879(55)01102- ... Rose, I.A. (1968). "State of magnesium in cells as estimated from adenylate kinase equilibrium". Proc. Natl. Acad. Sci. USA. 61 ... Rose, I.A. (1970). "Stereochemistry of pyruvate kinase, pyruvate carboxylase, and malate enzyme reactions". J. Biol. Chem. 245 ...
DPNH kinase, reduced diphosphopyridine nucleotide kinase, and NADH kinase. This enzyme has at least one activator, acetate. EC ... In enzymology, a NADH kinase (EC 2.7.1.86) is an enzyme that catalyzes a chemical reaction. ATP + NADH ⇌ {\displaystyle \ ... Other names in common use include reduced nicotinamide adenine dinucleotide kinase (phosphorylating), ... 2.7.1.86 Griffiths MM, Bernofsky C (1972). "Purification and properties of reduced diphosphopyridine nucleotide kinase from ...
... formation requires two enzymes: phosphate acetyltransferase and acetate kinase. acetyl-CoA + phosphate → acetyl- ... Many industrial solvents are acetates, including methyl acetate, ethyl acetate, isopropyl acetate, ethylhexyl acetate. Butyl ... acetate and basic zinc acetate. Commercially important acetate salts are aluminium acetate, used in dyeing, ammonium acetate, a ... "acetates" (hence, acetate of lead, acetate of aluminium, etc.). The simplest of these is hydrogen acetate (called acetic acid) ...
Ballongue, Jean; Amine, Jamel; Gay, Peptitdemange; Gay, Robert (July 1986). "Regulation of acetate kinase and butyrate kinase ... Butyrate kinase is active within the human colon. To form butyrate, two molecules of acetyl-CoA are combined and reduced to ... One study has previously found that butyrate kinase is not regulated by its end-products or other acids such as acetic acid, ... Butyryl-phosphate is then converted into butyrate by using butyrate kinase and in the process, releases ATP. Butyrate plays an ...
... (EC 2.7.2.15, PduW, TdcD, propionate/acetate kinase) is an enzyme with systematic name ATP:propanoate ... "Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase". Journal of Bacteriology. 187 ... comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily". Journal of Molecular Biology. 352 ... Propionate+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 2.7.2). ...
... the team concluded that the microbe likely acquired the ability to efficiently consume acetate using acetate kinase and ... Scientists hypothesize acetate kinase could be the urokinase in a major protein superfamily that includes actin. Evidence ... Recently researchers have proposed an evolution hypothesis for acetate kinase and phosphoacetyl transferase with genomic ... structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases". Journal of Bacteriology. 183 (2): 680- ...
Extracellular release of sphingosine-1-phosphate induced by phorbol 12-myristate 13-acetate (PMA)". The Journal of Biological ... Sphingosine kinase 1 is an enzyme that in humans is encoded by the SPHK1 gene. Sphingosine kinase 1 phosphorylates sphingosine ... Xia P, Wang L, Moretti PA, Albanese N, Chai F, Pitson SM, D'Andrea RJ, Gamble JR, Vadas MA (Mar 2002). "Sphingosine kinase ... Xia P, Wang L, Moretti PA, Albanese N, Chai F, Pitson SM, D'Andrea RJ, Gamble JR, Vadas MA (Mar 2002). "Sphingosine kinase ...
Saxena A, Scaini G, Bavaresco DV, Leite C, Valvassori SS, Carvalho AF, Quevedo J (November 2017). "Role of Protein Kinase C in ... Medroxyprogesterone acetate (MPA), also known as depot medroxyprogesterone acetate (DMPA) in injectable form and sold under the ... A differential effect of megestrol acetate and medroxyprogesterone acetate on serum estrone sulfate and sex hormone binding ... "The plasma concentration of medroxyprogesterone acetate and ovarian function during treatment with medroxyprogesterone acetate ...
Harwood CS, Canale-Parola E (1982). "Properties of acetate kinase isozymes and a branched-chain fatty acid kinase from a ... In enzymology, a branched-chain-fatty-acid kinase (EC 2.7.2.14) is an enzyme that catalyzes the chemical reaction ATP + 2- ... This enzyme is also called isobutyrate kinase. ...
González MI, Bannerman PG, Robinson MB (July 2003). "Phorbol myristate acetate-dependent interaction of protein kinase Calpha ...
Acetate formation requires two enzymes: phosphate acetyltransferase and acetate kinase. acetyl-CoA + phosphate → acetyl- ... The E. coli strain W3110 was genetically engineered to generate 2 moles of acetate for every 1 mole of glucose that undergoes ... For instance, strains for the increased production of ethanol, lactate, succinate and acetate have been developed due to the ... The mixture of end products produced by mixed acid fermentation includes lactate, acetate, succinate, formate, ethanol and the ...
12-O-Tetradecanoylphorbol-13-acetate (PMA or TPA) is a diacylglycerol mimic that can activate the classical PKCs. It is often ... In cell biology, Protein kinase C, commonly abbreviated to PKC (EC 2.7.11.13), is a family of protein kinase enzymes that are ... The consensus sequence of protein kinase C enzymes is similar to that of protein kinase A, since it contains basic amino acids ... Aug 2016 Wikimedia Commons has media related to Protein kinase C and PKC activators. protein+kinase+c at the U.S. National ...
It acts by inhibiting enzymes involved in the microbial metabolism, e.g. acetate kinase and L-glutamic acid decarboxylase. It ...
Protein kinase C (PKC) is a phorbol ester receptor. Phorbol esters can stimulate PKC in a similar way to diglycerides. Phorbol ... In particular, 12-O-tetradecanoylphorbol-13-acetate (TPA) is used as a biomedical research tool in models of carcinogenesis. ... "Tumour promoter phorbol-12-myristate-13-acetate induces chromosomal damage via indirect action". Nature. 293 (5828): 144-6. ...
As an activator of protein kinase C, it is a weak tumor promoter compared to 12-O-tetradecanoylphorbol-13-acetate. PDBu is ...
Bacterial proteins involved are ferredoxin-NADP reductase, acetate kinase, and NADH-quinone oxidoreductase found in the ... it was discovered that several microbial proteins were altered such as butyrate kinase, enoyl coenzyme A (enoyl-CoA) hydratase ... "Genital injury signatures and microbiome alterations associated with depot medroxyprogesterone acetate usage and intravaginal ...
Höller, Ulrich; König, Gabriele M.; Wright, Anthony D. (November 1999). "A New Tyrosine Kinase Inhibitor from a Marine Isolate ... was found in ethyl acetate extract from U. botrytis. Ulocladium botrytis also synthesizes extracellular keratinases and can ... Additionally, a new tyrosine kinase (p56tck) inhibitor called ulocladol, with the molecular formula C16H14O7, ...
... interacts with RACK1 and is a substrate for the phosphorylation by phorbol 12-myristate 13-acetate-activated protein kinase C ... The protein kinase Ki-1/57 occurs in the nucleus". Am. J. Pathol. 140 (2): 473-82. PMC 1886443. PMID 1310832. Strausberg RL, ...
... of the related adhesion focal tyrosine kinase in megakaryocytes upon stem cell factor and phorbol myristate acetate stimulation ... "Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions". Nature. 376 (6543 ... Protein tyrosine kinase 2 beta is an enzyme that in humans is encoded by the PTK2B gene. This gene encodes a cytoplasmic ... "Entrez Gene: PTK2B PTK2B protein tyrosine kinase 2 beta". Soni D, Regmi SC, Wang DM, DebRoy A, Zhao YY, Vogel SM, Malik AB, ...
... of the related adhesion focal tyrosine kinase in megakaryocytes upon stem cell factor and phorbol myristate acetate stimulation ... The proteins that bind to paxillin are diverse and include protein tyrosine kinases, such as Src and focal adhesion kinase (FAK ... "Activation of pyk2/related focal adhesion tyrosine kinase and focal adhesion kinase in cardiac remodeling". The Journal of ... We also know that the binding of paxillin to focal adhesion kinase (FAK) is critical for directing paxillin function. The ...
The Rubottom group found that lead(IV) acetate in DCM or benzene gave good yields of acyclic and cyclic α-hydroxy esters after ... synthesized various derivatives of phosphatidyl-D-myo-inositol to aid in the study of the various phosphatidylinositol 3-kinase ... In order to synthesize α-hydroxy esters, different oxidants are needed such as NaOCl (see above), lead(IV) acetate, or a ... acetate or hypofluorous acid-acetonitrile (HOF-ACN). However, these α-hydroxylations do not proceed via silyl enol ether ...
Creatine conversion to phosphocreatine is catalyzed by creatine kinase; spontaneous formation of creatinine occurs during the ... guanidino acetate, synthesized in the kidney from the amino acids arginine and glycine) by S-adenosyl methionine. It is then ...
... acetate and sugar kinases, Hsp70, actin). In A. aeolicus, the active site of the enzyme exists in a cleft between the two ... This can be accomplished via inhibition of polyphosphate kinase, enhancement of exopolyphosphatase activity, or both. ... which includes polyphosphate kinase [PPK] and PPX) and develop a wide variety of assays and techniques for quantification of ... by the lab of Nobel laureate Arthur Kornberg in 1993 and is part of the polyphosphate operon along with polyphosphate kinase, ...
... acetate, carbon dioxide and ATP by the combined actions of pyruvate:ferredoxin oxido-reductase, hydrogenase, acetate:succinate ... Superoxide dismutase, malate dehydrogenase (decarboxylating), ferredoxin, adenylate kinase and NADH:ferredoxin oxido-reductase ...
... that are exclusively shared by all members of this genus in the proteins acetate kinase and O-methyltransferase. These CSIs ...
An example is the teratogen and carcinogen phorbol 12-myristate 13-acetate, which is a plant terpene that activates protein ... kinase C, which promotes cancer, making it a useful investigative tool. There is also interest in creating small molecule ...
"Both acetate kinase and acetyl Coenzyme A synthetase are involved in acetate-stimulated change in the direction of flagellar ...
It is used to produce cellulose acetate butyrate (CAB), which is used in a wide variety of tools, paints, and coatings, and is ... whereas carnivores have butyrate-producing bacterial communities dominated by the butyrate kinase pathway. Butyrate's effects ... MCT1 and MCT4 have also been associated with the transport of short chain fatty acids such as acetate and formate which are ... Short-chain fatty acids (SCFAs) such as acetate, butyrate, and propionate, which are produced by gut microbial fermentation of ...
... associated with the activation of protein kinase C. PROG still has no effect on calcium channels of hypothalamic neurons from ... chlormadinone acetate, cyproterone acetate, hydroxyprogesterone caproate, medroxyprogesterone acetate, and nomegestrol acetate ... "Megestrol acetate NCD oral suspension -- Par Pharmaceutical: megestrol acetate nanocrystal dispersion oral suspension, PAR ... Estradiol/megestrol acetate Ethinylestradiol/megestrol acetate Kuhl H (August 2005). "Pharmacology of estrogens and ...
Mitogen-activated protein kinase kinase, VEGF, or Akt. Phorbol myristate acetate Tumor initiation Tumor progression Compton C ( ...
In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production ... The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme ... Grundy FJ, Waters DA, Allen SH, Henkin TM (November 1993). "Regulation of the Bacillus subtilis acetate kinase gene by CcpA". J ... Salmonella typhimurium propionate kinase (StTdcD) catalyzes reversible transfer of the γ-phosphate of ATP to propionate during ...
Crystal structure of acetate kinase from Mycobacterium avium ... Acetate kinase. A, B. 392. Mycobacterium avium. Mutation(s): 0 ... Crystal structure of acetate kinase from Mycobacterium avium. *PDB DOI: https://doi.org/10.2210/pdb3P4I/pdb ... Mtb cytidylate kinase, is described. The homolog-rescue strategy evaluated here for TB is also generalizable to drug targets ...
Can Acetic Acid Assay Kit (Acetate Kinase Manual Format) (K-ACETRM) be use to test Sodium Acetate concentration? ...
Home Analytical Solutions Food constituents, Enzymes Enzymatic Assay Kits Acetic acid - Enzymatic assay kit (Acetate Kinase - ... Acetic acid - Enzymatic assay kit (Acetate Kinase - Quick - Manual format) Reference : K-ACETRM ...
... kinases extracellular signal-regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) via a protein kinase C-dependent ... MAP kinase-dependent autophagy controls phorbol myristate acetate-induced macrophage differentiation of HL-60 leukemia cells.. ... MAP kinase-dependent autophagy controls phorbol myristate acetate-induced macrophage differentiation of HL-60 leukemia cells.. ... 2022). MAP kinase-dependent autophagy controls phorbol myristate acetate-induced macrophage differentiation of HL-60 leukemia ...
Tetradecanoylphorbol Acetate Grants and funding * EY 13421/EY/NEI NIH HHS/United States ... Protein kinase Cgamma regulation of gap junction activity through caveolin-1-containing lipid rafts Invest Ophthalmol Vis Sci. ...
The role of protein kinase C (PKC) isoforms in GnRH-stimulated MAPK [ERK and Jun N-terminal kinase (JNK)] was examined in the ... The role of protein kinase C (PKC) isoforms in GnRH-stimulated MAPK [ERK and Jun N-terminal kinase (JNK)] was examined in the ... The role of protein kinase C (PKC) isoforms in GnRH-stimulated MAPK [ERK and Jun N-terminal kinase (JNK)] was examined in the ... The role of protein kinase C (PKC) isoforms in GnRH-stimulated MAPK [ERK and Jun N-terminal kinase (JNK)] was examined in the ...
Bryostatin 1 and phorbol 12-myristate 13-acetate (PMA) are both potent activators of protein kinase C (PKC), although in many ... Differential regulation of protein kinase C isozymes by bryostatin 1 and phorbol 12-myristate 13-acetate in NIH 3T3 fibroblasts ... Differential regulation of protein kinase C isozymes by bryostatin 1 and phorbol 12-myristate 13-acetate in NIH 3T3 fibroblasts ... N2 - Bryostatin 1 and phorbol 12-myristate 13-acetate (PMA) are both potent activators of protein kinase C (PKC), although in ...
Glucocorticoids synergize with IL-1beta to induce TLR2 expression via MAP Kinase Phosphatase-1-dependent dual Inhibition of ... 17), activation of metalloproteinases by 4-aminophenylmercuric acetate (APMA) resulted in enhanced sTLR2 shedding (Figure 6B). ... Phorbol 12-myristate 13-acetate (PMA, # 524400) was from Cayman Chemical. Dexamethasone (#D8893) was obtained from Sigma- ... 4-aminophenylmercuric acetate (APMA, 10 μM) was added to the indicated samples 5 h before supernatants were harvested. Soluble ...
Elevation of creatinine kinase may occur. Clinical improvement or recovery after stopping corticosteroids may require weeks to ... Betamethasone Acetate (UNII: TI05AO53L7) (Betamethasone - UNII:9842X06Q6M) Betamethasone Acetate. 3 mg in 1 mL. ... BETAMETHASONE SODIUM PHOSPHATE AND BETAMETHASONE ACETATE betamethasone sodium phosphate and betamethasone acetate injection, ... Betamethasone acetate is a white to creamy white, odorless powder that sinters and resolidifies at about 165°C, and remelts at ...
... κB kinase; KEAP, Kelch-like ECH-associated protein 1; NOX, NADPH oxidase; NQ01, NAD(P)H:quinone acceptor oxidoreductase 1; NRF2 ... deoxycorticosterone acetate. ELISA. enzyme-linked immunosorbent assay. GFR. glomerular filtratin rate. MCP-1. monocyte ... CXA-10, a Nitrated Fatty Acid, Is Renoprotective in Deoxycorticosterone Acetate-Salt Nephropathy. Cynthia M. Arbeeny, Hong Ling ... CXA-10, a Nitrated Fatty Acid, Is Renoprotective in Deoxycorticosterone Acetate-Salt Nephropathy ...
M00579 Phosphate acetyltransferase-acetate kinase pathway, acetyl-CoA => acetate [PATH:eclc00430 eclc00620 eclc01200 eclc01100 ...
The neurons were lysed using a hypotonic lysis buffer (Tris-acetate buffer, pH 7.75). Fifty microliters of the sample and 50 μl ... 2005) Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase. Cell ... 2005) Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells. ... 2007) S6 kinase deletion suppresses muscle growth adaptations to nutrient availability by activating AMP kinase. Cell Metab 5: ...
... ethyl acetate; HPLC, high-performance liquid chromatography; DMSO, dimethyl sulfoxide; LC/MS, liquid chromatography/mass ... spectrometry; PKC, protein kinase C.. **Received January 22, 2008.. *Accepted May 12, 2008. ...
protein kinase C. K-H. Krebs-Henseleit bicarbonate buffer. PMA. phorbol 12-myristate 13-acetate. Grb2. growth factor receptor ... extracellular signal-regulated kinase. JNK. c-Jun N-terminal kinase. MAP. mitogen-activated protein. quercetin. 3,3′,4′,5,7- ... Quercetin Inhibits Shc- and Phosphatidylinositol 3-Kinase-Mediated c-Jun N-Terminal Kinase Activation by Angiotensin II in ... Quercetin Inhibits Shc- and Phosphatidylinositol 3-Kinase-Mediated c-Jun N-Terminal Kinase Activation by Angiotensin II in ...
This study is being done to see how safe and effective abemaciclib is when given together with abiraterone acetate plus ... Prior treatment with abemaciclib or any cyclin-dependent kinase (CDK) 4 & 6. inhibitors. ... with abiraterone acetate plus prednisone in participants with metastatic castration resistant. prostate cancer. Prednisolone ... A Phase 2, Randomized, Double-Blind, Placebo-Controlled Study of Abiraterone Acetate plus Prednisone with or without ...
protein kinase A. PKC. protein kinase C. PMA. phorbol-12-myristate-13-acetate. 4αPMA. 4α-phorbol-12-myristate-13-acetate. WT. ... though they display different sensitivities to signaling via cAMP/protein kinase A (PKA) and protein kinase C (PKC). We ... 2007) Protein kinase A modulates PLC-dependent regulation and PIP2-sensitivity of K+ channels. Channels (Austin) 1:124-134. ... 2014) Differential protein kinase C-dependent modulation of Kv7.4 and Kv7.5 subunits of vascular Kv7 channels. J Biol Chem 289: ...
... belong to the CMGC kinase family and are closely related to dual-specificity tyrosine phosphorylation-regulated kinases (DYRKs ... Here the authors demonstrate that members of the Homeodomain-interacting protein kinases (HIPKs) HIPK3 and DYRK1A are also ... showing a similar binding mode to the hinge region of the kinase as observed for Cdk6. Remarkably, DYRK1A is inhibited by ... Kinases were diluted 1:5 in acetate buffer (pH 5.5 for DYRK1A, Cdk4/CycD3, and pH 5.0 for HIPK2 and HIPK3). To obtain high ...
... and tocopherol acetate (TA) are widely used ingredients in cosmetics. The present study was carried out to evaluate the content ... alpha-tocopherol via protein kinase C inhibition. Free Radic. Biol. Med. 1999; 27: 729-737. ... Abstract: Tocopherol (T) and tocopherol acetate (TA) are widely used ingredients in cosmetics. The present ... In summary, we have determined that alpha-tocopherol acetate is not metabolized to the free form of alpha-tocopherol in plasma ...
Taurine and hypotaurine metabolism - Oryza sativa japonica (Japanese rice) (RefSeq ...
M00579 Phosphate acetyltransferase-acetate kinase pathway * M00620 Incomplete reductive citrate cycle * Methane metabolism * ...
Equal amounts of protein were resolved by SDS-PAGE (4% to 12% tri-acetate mini gel; Invitrogen) and transferred to ... kinases (i.e., c-Jun N-terminal kinase [JNK]) [20,21], p38 mitogen-actiated protein kinase (p38MAPK) [22,23], phosphatase 2A [ ... Activation of the hematopoietic progenitor kinase-1 (HPK1)-dependent, stress-activated c-Jun N-terminal kinase (JNK) pathway by ... which is a serine/threonin protein kinase that contains an NH2-terminal catalytic kinase domain and plays an important role in ...
Crystal structure of AMPPNP bound Propionate kinase (TdcD) from Salmonella typhimurium ... by molecular replacement using Methanosarcina thermophila acetate kinase (MAK; EC 2.7.2.1). Propionate kinase, like acetate ... than for acetate (26.9 mM). Comparison of TdcD complex structures with those of acetate and sugar kinase/Hsc70/actin obtained ... Comparison with Members of Acetate and Sugar Kinase/Heat Shock Cognate 70/Actin Superfamily.. Simanshu, D.K., Savithri, H.S., ...
DNA-dependent protein kinase; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; PMA, phorbol 12-myristate 13-acetate; CREB, cAMP ... trans-signalling complex but not protein kinase C activator phorbol 12-myristate 13-acetate. The inhibitory effects of cAMP on ... Janus kinase; MEK, mitogen-activated protein/ERK kinase; SHP-2, SH2 domain-containing tyrosine phosphatase-2; PKA, cAMP- ... Selective inhibition of cytokine-activated extracellular signal-regulated kinase by cyclic amp via Epac1-dependent induction of ...
E. addisoniae acts by decreasing the ERK kinase activation (Watjen et al., 2007). The ethyl acetate extract inhibited PTP1B ( ... Ethyl acetate extract of E. milbraedii stem bark inhibited PTP1B (Na et al., 2007; Jang et al., 2008). Dichloromethane extract ... The roots ethyl acetate extract of E. addisoniae exhibited an antiviral activity against H1N1 and H9N2 neuraminidases (Nguyen ... E. mildbraedii ethyl acetate extract showed anti-inflammatory activity and radical scavenging activity in 1, 1-Diphenyl-2- ...
Isolation and characterization of acetate kinase and phosphotransacetylase mutants of Escherichia coli and Salmonella ...
... myristate-13-acetate-induced tumor cell invasion by apigenin via the inhibition of p38 mitogen-activated protein kinase- ... myristate-13-acetate-induced tumor cell invasion by apigenin via the inhibition of p38 mitogen-activated protein kinase- ... myristate-13-acetate-induced tumor cell invasion by apigenin via the inhibition of p38 mitogen-activated protein kinase- ... myristate-13-acetate-induced tumor cell invasion by apigenin via the inhibition of p38 mitogen-activated protein kinase- ...
Acetate kinase 2. 5. NGO1521 Primosomal replication protein. 3. NGO0582 DNA Helicase. 3, 5. NGO1196 ...
  • Interestingly, PKCα, PKCβII, and PKCε translocation to the plasma membrane was more pronounced and more prolonged in phorbol-12-myristate-13-acetate (PMA) than in GnRH-treated cells. (biu.ac.il)
  • Bryostatin 1 and phorbol 12-myristate 13-acetate (PMA) are both potent activators of protein kinase C (PKC), although in many systems bryostatin 1 induces only a subset of the responses to PMA and blocks those which it does not induce. (elsevierpure.com)
  • Forskolin treatment reduced the sensitivity of Kv7.5 channels to Ciona intestinalis voltage-sensing phosphatase (Ci-VSP)-induced PIP 2 depletion, whereas activation of PKC with phorbol-12-myristate-13-acetate potentiated the Ci-VSP-induced decline in Kv7.5 current amplitude. (aspetjournals.org)
  • Here we demonstrate that elevation of cyclic AMP (cAMP) levels in human umbilical vein endothelial cells (HUVECs) specifically attenuates ERK1,2 activation in response to either leptin or a soluble interleukin IL-6 receptor-α/IL-6 (sIL-6R-α/IL-6) trans-signalling complex but not protein kinase C activator phorbol 12-myristate 13-acetate. (gla.ac.uk)
  • We found that apigenin markedly inhibits the phorbol-12-myristate-13-acetate (PMA)-induced increase in MMP-9 expression and activity in several cancer cell lines. (spandidos-publications.com)
  • Stimulation of cardiomyocytes with 4 beta-phorbol 12-myristate 13-acetate (PMA) led to a rapid increase in particulate-bound PKC activity, a response attributed to the activation of alpha-, delta- and zeta- type PKCs but not beta-type PKC. (unige.ch)
  • On the other hand, it readily stimulated the phosphorylation of mitogen-activated protein (MAP) kinases extracellular signal-regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) via a protein kinase C-dependent mechanism. (ac.rs)
  • Our findings showed that Ang II stimulated rapid and significant activation of extracellular signal-regulated kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38 in RASMC. (aspetjournals.org)
  • Woolson, H. D. , Thomson, V. S. , Rutherford, C. , Yarwood, S. J. and Palmer, T. M. (2009) Selective inhibition of cytokine-activated extracellular signal-regulated kinase by cyclic amp via Epac1-dependent induction of suppressor of cytokine signalling-3. (gla.ac.uk)
  • Quercetin also inhibited Ang II-induced Shc·p85 association and subsequent activation of phosphatidylinositol 3-kinase (PI3-K)/Akt pathway in RASMC. (aspetjournals.org)
  • Phosphatidylinositol 3-kinase type 2α (PI3KC2α) is an essential member of the structurally unresolved class II PI3K family with crucial functions in lipid signaling, endocytosis, angiogenesis, viral replication, platelet formation and a role in mitosis. (nature.com)
  • Specifically this another hormone system in the effects can be dangerous, and telomerase, and by blocking phosphatidylinositol 3-kinase pathway inhibitors. (ncfy.com)
  • Activation of the phosphatidylinositol 3-kinase/mechanistic target of rapamycin pathway plays a role in the pathogenesis of non-Hodgkin lymphoma. (haematologica.org)
  • This multicenter, open-label phase 2 study evaluated buparlisib (BKM120), a pan-class I phosphatidylinositol 3-kinase inhibitor, in patients with relapsed or refractory non-Hodgkin lymphoma. (haematologica.org)
  • Phosphatidylinositol 3-kinase (PI3K)/mechanistic target of rapamycin (mTOR) signaling regulates many cellular activities, including proliferation, survival, angiogenesis, and glucose metabolism. (haematologica.org)
  • The phosphatidyl inositol 3-kinase (PI3K)/Akt pathway was involved in this ubiquitin-proteasome-mediated degradation of PDCD4. (plos.org)
  • Notably, inhibition of the CaMKK (calmodulin-dependent protein kinase kinase) had little affect on GLUT translocation, whereas the inhibition or knockdown of AMPK (compound C, siRNA) activity prevented GLUT3 translocation to the cell surface after glutamate excitation. (jneurosci.org)
  • The inhibitory effect of cAMP could not be reversed by inhibition of cAMP-dependent protein kinase (PKA) but was blocked by depletion of the alternative intracellular cAMP sensor exchange protein activated by cAMP 1 (Epac1), which is also required to observe SOCS-3 accumulation in response to cAMP. (gla.ac.uk)
  • Morphological rescue is possible following Rho kinase inhibition in an oligodendrocyte subset. (jneurosci.org)
  • Pretreatment of JB6 P(+) mouse epidermal cells with lingonberry extracts produced a dose-dependent inhibition on the activation of activator protein-1 (AP-1) and nuclear factor-kappaB (NF-kappaB) induced by either 12-O-tetradecanoylphorbol-13-acetate (TPA) or ultraviolet-B (UVB). (cdc.gov)
  • We found that apigenin could inhibit PMA-induced phosphorylation of p38 mitogen-activated protein kinase (p38 MAPK), which was involved in the down-regulation of the expression of matrix metalloproteinase-9 (MMP-9) at mRNA levels. (spandidos-publications.com)
  • Lingonberry extract blocked UVB-induced phosphorylation of the mitogen-activated protein kinase (MAPK) signaling members ERK1, ERK2, p38, and MEK1/2 but not JNK. (cdc.gov)
  • Salmonella typhimurium propionate kinase (StTdcD) catalyzes reversible transfer of the γ-phosphate of ATP to propionate during l-threonine degradation to propionate. (wikipedia.org)
  • A related enzyme, butyrate kinase, facilitates the formation of butyryl-CoA by phosphorylating butyrate in the presence of ATP to form butyryl phosphate. (wikipedia.org)
  • Betamethasone Sodium Phosphate and Betamethasone Acetate Injectable Suspension is a sterile aqueous suspension containing 3 mg per milliliter betamethasone (equivalent to 3.95 mg betamethasone sodium phosphate USP) and 3 mg per milliliter betamethasone acetate. (nih.gov)
  • Betamethasone sodium phosphate, a soluble ester, provides prompt activity, while betamethasone acetate is only slightly soluble and affords sustained activity. (nih.gov)
  • Complexes of Vps34, the sole class III PI3K member, produce PI 3-phosphate (PI(3)P) in the endolysosomal system and during autophagy to regulate vesicle-mediated sorting en route to lysosomes 1 . (nature.com)
  • We investigated the mechanisms and the role of autophagy in the differentiation of HL-60 human acute myeloid leukemia cells induced by protein kinase C (PKC) activator phorbol myristate acetate (PMA). (ac.rs)
  • Can Acetic Acid Assay Kit (Acetate Kinase Manual Format) (K-ACETRM) be use to test Sodium Acetate concentration? (megazyme.com)
  • Homeodomain-interacting protein kinases (HIPKs) belong to the CMGC kinase family and are closely related to dual-specificity tyrosine phosphorylation-regulated kinases (DYRKs). (nature.com)
  • Homeodomain-interacting protein kinases (HIPKs) are an evolutionarily conserved kinase family comprising the members HIPK1, HIPK2, and HIPK3 in vertebrates, and, additionally, HIPK4 in mammals. (nature.com)
  • Antioxidant activity in lingonberries (Vaccinium vitis-idaea L.) and its inhibitory effect on activator protein-1, nuclear factor-kappa B, and mitogen-activated protein kinases activation. (cdc.gov)
  • PMA failed to activate autophagy inducer AMP-activated protein kinase (AMPK) and inhibit autophagy suppressor mechanistic target of rapamycin complex 1 (mTORC1). (ac.rs)
  • 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)
  • Examination of the active site pocket revealed a plausible structural rationale for the greater specificity of the enzyme towards propionate than acetate. (rcsb.org)
  • This was further confirmed by kinetic studies with the purified enzyme, which showed about ten times lower K(m) for propionate (2.3 mM) than for acetate (26.9 mM). (rcsb.org)
  • This is because the Propionate and Acetate and cough remedies Trenaver for sale rhetoric enanthate from breast development (gynecomastia) in men. (ncfy.com)
  • The role of protein kinase C (PKC) isoforms in GnRH-stimulated MAPK [ERK and Jun N-terminal kinase (JNK)] was examined in the αT3-1 and LβT2 gonadotrope cells. (biu.ac.il)
  • Phosphoinositide 3-kinases (PI3Ks) are a family of lipid-modifying enzymes that phosphorylate the 3′-OH group of inositol phospholipids and play key roles in physiology ranging from cell growth and metabolism to organismal development. (nature.com)
  • eslicarbazepine acetate decreases levels of vandetanib by affecting hepatic/intestinal enzyme CYP3A4 metabolism. (medscape.com)
  • Isolation and characterization of acetate kinase and phosphotransacetylase mutants of Escherichia coli and Salmonella typhimurium. (yale.edu)
  • Our study examined the effect of a selective Rho kinase inhibitor, Y-27632, on corneal wound healing and potential stromal scarring after superficial keratectomy. (molvis.org)
  • After incubation with LSD synthetic substrates, extracts are cleaned using liquid-liquid extraction with ethyl acetate or protein precipitation using acetonitrile (ACN). (cdc.gov)
  • We investigated cold-induced water ACN phase separation (CIPS) to improve the combination of 6-plex and I2S extracts to create a 7-plex assay, and compared it to room temperature ACN and ethyl acetate liquid-liquid extraction. (cdc.gov)
  • Therefore, MAP kinases ERK and JNK control PMA-induced macrophage differentiation of HL-60 leukemia cells through AMPK/mTORC1-independent, TFEB/FOXO-mediated transcriptional and beclin-1-dependent post-translational activation of autophagy. (ac.rs)
  • Glutamate excitation induced a rapid alteration in the AMP:ATP ratio that was associated with the activation of the AMP-activated protein kinase (AMPK). (jneurosci.org)
  • HIPKs belong to the CMGC group of serine/threonine kinases and are part of the dual-specificity tyrosine phosphorylation-regulated kinase (DYRK) family. (nature.com)
  • C-terminally adjacent to the HID follows a proline, glutamate, serine, and threonine (PEST)-rich domain, mediating proteasomal degradation of these kinases. (nature.com)
  • The pathways involved in cellular differentiation or transformation are Smad, Rho proteins, and PI3-kinase. (molvis.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)
  • In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation. (wikipedia.org)
  • ILK is composed of three domains, an N-terminal ankryin domain, a pleckstrin homology domain, and a putative kinase domain. (jneurosci.org)
  • Taxonomy and function of C1 protein kinase C homology domains. (embl-heidelberg.de)
  • This study is being done to see how safe and effective abemaciclib is when given together with abiraterone acetate plus prednisone in participants with metastatic castration resistant prostate cancer. (dana-farber.org)
  • Prior treatment with abemaciclib or any cyclin-dependent kinase (CDK) 4 & 6 inhibitors. (dana-farber.org)
  • We determined the crystal structures of HIPK3 and DYRK1A bound to abemaciclib, showing a similar binding mode to the hinge region of the kinase as observed for Cdk6. (nature.com)
  • The expression of protein kinase C (PKC) isoenzymes and the effects of PKC activation on myocardial phospholipase A2 (PLA2) activity, platelet-activating factor (PAF) generation and eicosanoid release were studied in spontaneously beating cultured rat cardiomyocytes. (unige.ch)
  • Ang II-induced cellular events have been implicated, in part, in the activation of mitogen-activated protein (MAP) kinases. (aspetjournals.org)
  • Thus, we hypothesized that bioflavonoids may affect Ang II-induced MAP kinase activation in cultured rat aortic smooth muscle cells (RASMC). (aspetjournals.org)
  • MAP kinase-dependent autophagy controls phorbol myristate acetate-induced macrophage differentiation of HL-60 leukemia cells. (ac.rs)
  • Mandic M, Misirkic Marjanovic M, Vucicevic L, Jovanovic M, Bosnjak M, Perovic V, Ristic B, Ciric D, Harhaji-Trajkovic L, Trajkovic V. MAP kinase-dependent autophagy controls phorbol myristate acetate-induced macrophage differentiation of HL-60 leukemia cells. (ac.rs)
  • These highlights do not include all the information needed to use LEUPROLIDE ACETATE INJECTION safely and effectively. (nih.gov)
  • See full prescribing information for LEUPROLIDE ACETATE INJECTION. (nih.gov)
  • LEUPROLIDE ACETATE INJECTION DEPOT (leuprolide acetate for depot suspension). (nih.gov)
  • LEUPROLIDE ACETATE INJECTION DEPOT 22.5 mg for 3 months administration, given as a single intramuscular injection every 12 weeks. (nih.gov)
  • For Injection: 22.5 mg of leuprolide acetate in a single dose vial as a kit with a prefilled syringe containing diluent and a MIXJECT transfer device. (nih.gov)
  • Hypersensitivity to GnRH, GnRH agonist or any of the excipients in LEUPROLIDE ACETATE INJECTION DEPOT. (nih.gov)
  • Monitor serum levels of testosterone following injection of LEUPROLIDE ACETATE INJECTION DEPOT 22.5 mg for 3-month administration. (nih.gov)
  • Females and males of reproductive potential: LEUPROLIDE ACETATE INJECTION DEPOT may impair fertility. (nih.gov)
  • Geriatric: This label reflects clinical trials for LEUPROLIDE ACETATE INJECTION DEPOT in prostate cancer in which the majority of the subjects studied were at least 65 years of age. (nih.gov)
  • Integrin-linked kinase (ILK) is a major structural adaptor protein governing signaling complex formation and cytoskeletal dynamics. (jneurosci.org)
  • Within the HIPK family, HIPK1 and HIPK2 are the most closely related members, sharing about 93% sequence identity in their kinase domains, while HIPK3 is slightly less conserved with 87% identity. (nature.com)
  • The corticosteroid cortisone and the mineralocorticoid fludrocortisone acetate can be used in combination in patients suffering from adrenocortical insufficiency. (medscape.com)
  • Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich domains of the enzyme. (embl-heidelberg.de)
  • NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions. (embl-heidelberg.de)
  • In the present study, we evaluated the effects of chronic treatment with CXA-10 (10-nitro-9(E)-octadec-9-enoic acid) in the uninephrectomized deoxycorticosterone acetate-high-salt mouse model of CKD. (aspetjournals.org)
  • a promising test case, Mtb cytidylate kinase, is described. (rcsb.org)
  • The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydrate. (wikipedia.org)
  • The Newborn Screening Quality Assurance Program (NSQAP) at the U.S. Centers for Disease Control and Prevention (CDC) produced a set of seven prototype dried blood spot (DBS) reference materials spiked with varying levels of creatine kinase MM isoform (CK-MM). These DBS were evaluated over a 3-week period by CDC, NYS, and RTI, all using the same CK-MM isoform-specific fluoroimmunoassay. (cdc.gov)

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