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 class of enzymes that inactivate aminocyclitol-aminoglycoside antibiotics (AMINOGLYCOSIDES) by regiospecific PHOSPHORYLATION of the 3' and/or 5' hydroxyl.
A group of enzymes that transfers two phosphate groups from a donor such as ATP to two different acceptors. (From Enzyme Nomenclature, 1992) EC 2.7.9.
A group of enzymes that transfers a phosphate group onto an alcohol group acceptor. EC 2.7.1.
An enzyme that catalyzes reversibly the transfer of phosphoethanolamine from CDP-ethanolamine to diacylglycerol to yield phosphatidylethanolamine (cephalin) and CMP. The enzyme is found in the endoplasmic reticulum. EC 2.7.8.1.
Glycosylated compounds in which there is an amino substituent on the glycoside. Some of them are clinically important ANTIBIOTICS.
An enzyme that catalyzes the synthesis of phosphatidylcholines from CDPcholine and 1,2-diacylglycerols. EC 2.7.8.2.
A group of enzymes that catalyze an intramolecular transfer of a phosphate group. It has been shown in some cases that the enzyme has a functional phosphate group, which can act as the donor. These were previously listed under PHOSPHOTRANSFERASES (EC 2.7.-). (From Enzyme Nomenclature, 1992) EC 5.4.2.
A class of enzymes that transfers phosphate groups and has a carboxyl group as an acceptor. EC 2.7.2.
A group of enzymes that catalyzes the transfer of a phosphate group onto a nitrogenous group acceptor. EC 2.7.3.
A group of enzymes that catalyzes the transfer of a phosphate group onto a phosphate group acceptor. EC 2.7.4.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
The rate dynamics in chemical or physical systems.

A novel skeletal dysplasia with developmental delay and acanthosis nigricans is caused by a Lys650Met mutation in the fibroblast growth factor receptor 3 gene. (1/3825)

We have identified a novel fibroblast growth factor receptor 3 (FGFR3) missense mutation in four unrelated individuals with skeletal dysplasia that approaches the severity observed in thanatophoric dysplasia type I (TD1). However, three of the four individuals developed extensive areas of acanthosis nigricans beginning in early childhood, suffer from severe neurological impairments, and have survived past infancy without prolonged life-support measures. The FGFR3 mutation (A1949T: Lys650Met) occurs at the nucleotide adjacent to the TD type II (TD2) mutation (A1948G: Lys650Glu) and results in a different amino acid substitution at a highly conserved codon in the kinase domain activation loop. Transient transfection studies with FGFR3 mutant constructs show that the Lys650Met mutation causes a dramatic increase in constitutive receptor kinase activity, approximately three times greater than that observed with the Lys650Glu mutation. We refer to the phenotype caused by the Lys650Met mutation as "severe achondroplasia with developmental delay and acanthosis nigricans" (SADDAN) because it differs significantly from the phenotypes of other known FGFR3 mutations.  (+info)

Presynaptic inhibition of GABA(B)-mediated synaptic potentials in the ventral tegmental area during morphine withdrawal. (2/3825)

Opioids increase the firing of dopamine cells in the ventral tegmental area by presynaptic inhibition of GABA release. This report describes an acute presynaptic inhibition of GABAB-mediated IPSPs by mu- and kappa-opioid receptors and the effects of withdrawal from chronic morphine treatment on the release of GABA at this synapse. In slices taken from morphine-treated guinea pigs after washing out the morphine (withdrawn slices), a low concentration of a mu receptor agonist increased, rather than decreased, the amplitude of the GABAB IPSP. In withdrawn slices, after blocking A1-adenosine receptors with 8-cyclopentyl-1, 3-dipropylxantine, mu-opioid receptor activation inhibited the IPSP at all concentrations and increased the maximal inhibition. In addition, during withdrawal, there was a tonic increase in adenosine tone that was further increased by forskolin or D1-dopamine receptor activation, suggesting that metabolism of cAMP was the source of adenosine. The results indicate that during acute morphine withdrawal, there was an upregulation of the basal level of an opioid-sensitive adenylyl cyclase. Inhibition of this basal activity by opioids had two effects. First, a decrease in the formation of cAMP that decreased adenosine tone. This effect predominated at low mu receptor occupancy and increased the amplitude of the IPSP. Higher agonist concentrations inhibited transmitter release by both kinase-dependent and -independent pathways. This study indicates that the consequences of the morphine-induced upregulation of the cAMP cascade on synaptic transmission are dependent on the makeup of receptors and second messenger pathways present on any given terminal.  (+info)

The mouse Y-box protein, MSY2, is associated with a kinase on non-polysomal mouse testicular mRNAs. (3/3825)

In male germ cells many mRNAs are sequestered by proteins into translationally silent messenger ribo-nucleoprotein (mRNP) particles. These masked paternal mRNAs are stored and translated at specific times of germ cell development. Little is known about the mammalian testicular mRNA masking proteins bound to non-polysomal mRNAs. In this report, the major proteins binding to non-polysomal testicular mRNAs were isolated and analyzed. The two predominant proteins identified were: a Y-box protein (MSY2), the mammalian homolog to the Xenopus oocyte masking protein FRGY2/mRNP3+4, and a poly(A) binding protein. A kinase activity was also found associated with these non-polysomal RNAs. The kinase co-immunoprecipitates with MSY2 and phosphorylates MSY2 in vitro. The MSY2 associated kinase is not casein kinase 2, the kinase believed to phosphorylate mRNP3+4 in oocytes, but a yet unidentified kinase. MSY2 was found to be phosphorylated in vivo and MSY2 dephosphorylation led to a decrease in its affinity to bind RNA as judged by northwestern blotting. Therefore, testicular masked mRNAs may be regulated by the phosphorylation state of MSY2. Reconstitution experiments in which non-polysomal mRNA-binding proteins are dissociated from their RNAs and allowed to bind to exogenous mRNAs suggest that MSY2 binds RNA in a sequence-independent fashion. Furthermore, association of the non-polysomal derived proteins to exogenous non-specific mRNAs led to their translational repression in vitro.  (+info)

A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. (4/3825)

Sequence analysis of the probable archaeal phosphoglycerate mutase resulted in the identification of a superfamily of metalloenzymes with similar metal-binding sites and predicted conserved structural fold. This superfamily unites alkaline phosphatase, N-acetylgalactosamine-4-sulfatase, and cerebroside sulfatase, enzymes with known three-dimensional structures, with phosphopentomutase, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, phosphoglycerol transferase, phosphonate monoesterase, streptomycin-6-phosphate phosphatase, alkaline phosphodiesterase/nucleotide pyrophosphatase PC-1, and several closely related sulfatases. In addition to the metal-binding motifs, all these enzymes contain a set of conserved amino acid residues that are likely to be required for the enzymatic activity. Mutational changes in the vicinity of these residues in several sulfatases cause mucopolysaccharidosis (Hunter, Maroteaux-Lamy, Morquio, and Sanfilippo syndromes) and metachromatic leucodystrophy.  (+info)

The cellular distribution and kinase activity of the Cdk family member Pctaire1 in the adult mouse brain and testis suggest functions in differentiation. (5/3825)

Pctaire1, a member of the family of cyclin-dependent kinases, has been shown to be particularly abundantly expressed in differentiated tissues such as testis and brain. However, very little is known about the cellular and subcellular distribution and function of Pctaire1 protein(s), which is the focus of this study. We show that Pctaire1 encoded two major proteins of M(r) approximately 62,000 and approximately 68,000, found predominantly in testis and brain. Within these two tissues, Pctaire1 was most abundant in the cytoplasm of terminally differentiated cells, notably, the pyramidal neurons in brain and elongated spermatids in testis. Immunoprecipitation experiments further showed that a kinase activity toward myelin basic protein was associated with Pctaire1 in the adult testis and brain and that its activity was potentially regulated through association with regulatory partner(s). These results suggest that Pctaire1 kinase might have an important role in differentiated cells such as postmitotic neurons and spermatogenic cells.  (+info)

Involvement of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system in regulation of transcription of catabolic genes. (6/3825)

Synthesis of catabolite-sensitive enzymes is repressed in mutants defective in the general proteins (enzyme I and HPr) of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system (ptsI and ptsH mutations). To elucidate the mechanism of this phenomenon we constructed isogenic strains carrying pts mutations as well as different lesions of regulation of the lac operon or mutations affecting adenylate cyclase activity (cya mutation) and synthesis of cyclic AMP-receptor protein (crp mutation) Measurements of the differential rate of beta-galactosidase synthesis in these strains showed that the repressive effect of pts mutations was revealed in lac+, lacI, lacOc and cya bacteria, but it was lost in lacP and crp strains. It was concluded that mutational damage to the general components of the phosphoenolpyruvate-dependent phosphotransferase system diminishes activity of the lac promoter. The results obtained led to the conclusion that pts gene products (apparently phospho approximately HPr) are necessary for the initiation of transcription of catabolite-sensitive operons in E. coli.  (+info)

In vivo regulation of glycolysis and characterization of sugar: phosphotransferase systems in Streptococcus lactis. (7/3825)

Two novel procedures have been used to regulate, in vivo, the formation of phosphoenolpyruvate (PEP) from glycolysis in Streptococcus lactis ML3. In the first procedure, glucose metabolism was specifically inhibited by p-chloromercuribenzoate. Autoradiographic and enzymatic analyses showed that the cells contained glucose 6-phosphate, fructose 6-phosphate, fructose-1,6-diphosphate, and triose phosphates. Dithiothreitol reversed the p-chloromercuribenzoate inhibition, and these intermediates were rapidly and quantitatively transformed into 3- and 2-phosphoglycerates plus PEP. The three intermediates were not further metabolized and constituted the intracellular PEP potential. The second procedure simply involved starvation of the organisms. The starved cells were devoid of glucose 6-phosphate, fructose 6-phosphate, fructose- 1,6-diphosphate, and triose phosphates but contained high levels of 3- and 2-phosphoglycerates and PEP (ca. 40 mM in total). The capacity to regulate PEP formation in vivo permitted the characterization of glucose and lactose phosphotransferase systems in physiologically intact cells. Evidence has been obtained for "feed forward" activation of pyruvate kinase in vivo by phosphorylated intermediates formed before the glyceraldehyde-3-phosphate dehydrogenase reaction in the glycolytic sequence. The data suggest that pyruvate kinase (an allosteric enzyme) plays a key role in the regulation of glycolysis and phosphotransferase system functions in S. lactis ML3.  (+info)

A phosphotransferase that generates phosphatidylinositol 4-phosphate (PtdIns-4-P) from phosphatidylinositol and lipid A in Rhizobium leguminosarum. A membrane-bound enzyme linking lipid a and ptdins-4-p biosynthesis. (8/3825)

Membranes of Rhizobium leguminosarum contain a 3-deoxy-D-manno-octulosonic acid (Kdo)-activated lipid A 4'-phosphatase required for generating the unusual phosphate-deficient lipid A found in this organism. The enzyme has been solubilized with Triton X-100 and purified 80-fold. As shown by co-purification and thermal inactivation studies, the 4'-phosphatase catalyzes not only the hydrolysis of (Kdo)2-[4'-32P]lipid IVA but also the transfer the 4'-phosphate of Kdo2-[4'-32P]lipid IVA to the inositol headgroup of phosphatidylinositol (PtdIns) to generate PtdIns-4-P. Like the 4'-phosphatase, the phosphotransferase activity is not present in Escherichia coli, Rhizobium meliloti, or the nodulation-defective mutant 24AR of R. leguminosarum. The specific activity for the phosphotransferase reaction is about 2 times higher than that of the 4'-phosphatase. The phosphotransferase assay conditions are similar to those used for PtdIns kinases, except that ATP and Mg2+ are omitted. The apparent Km for PtdIns is approximately 500 microM versus 20-100 microM for most PtdIns kinases, but the phosphotransferase specific activity in crude cell extracts is higher than that of most PtdIns kinases. The phosphotransferase is absolutely specific for the 4-position of PtdIns and is highly selective for PtdIns as the acceptor. The 4'-phosphatase/phosphotransferase can be eluted from heparin- or Cibacron blue-agarose with PtdIns. A phosphoenzyme intermediate may account for the dual function of this enzyme, since a single 32P-labeled protein species (Mr approximately 68,000) can be trapped and visualized by SDS gel electrophoresis of enzyme preparations incubated with Kdo2-[4'-32P]lipid IVA. Although PtdIns is not detected in cultures of R. leguminosarum/etli (CE3), PtdIns may be synthesized during nodulation or supplied by plant membranes, given that soybean PtdIns is an excellent phosphate acceptor. A bacterial enzyme for generating PtdIns-4-P and a direct link between lipid A and PtdIns-4-P biosynthesis have not been reported previously.  (+info)

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.

Kanamycin Kinase is not a widely recognized medical term, but it is a concept from the field of microbiology. It refers to an enzyme produced by certain bacteria that catalyzes the phosphorylation of kanamycin, an aminoglycoside antibiotic. The phosphorylation of kanamycin inactivates its antibacterial activity, making it less effective against those bacteria that produce this kinase. This is one mechanism by which some bacteria develop resistance to antibiotics.

Ethanolaminephosphotransferase is an enzyme that plays a role in the biosynthesis of phosphatidylethanolamine, which is a type of phospholipid found in biological membranes. Phosphatidylethanolamine is an essential component of cell membranes and is involved in various cellular processes, including signal transduction and membrane trafficking.

Ethanolaminephosphotrtransferase catalyzes the transfer of a phosphoethanolamine group from CDP-ethanolamine to the hydroxyl group of diacylglycerol (DAG), resulting in the formation of phosphatidylethanolamine. This enzyme is widely distributed in nature and is found in various organisms, including bacteria, plants, and animals.

Defects in ethanolaminephosphotransferase have been associated with certain genetic disorders, such as congenital disorder of glycosylation type Ia (CDG-Ia) and autosomal recessive intellectual disability syndrome 26 (ARID26). These disorders can result in a range of symptoms, including developmental delays, seizures, and movement disorders.

Aminoglycosides are a class of antibiotics that are derived from bacteria and are used to treat various types of infections caused by gram-negative and some gram-positive bacteria. These antibiotics work by binding to the 30S subunit of the bacterial ribosome, which inhibits protein synthesis and ultimately leads to bacterial cell death.

Some examples of aminoglycosides include gentamicin, tobramycin, neomycin, and streptomycin. These antibiotics are often used in combination with other antibiotics to treat severe infections, such as sepsis, pneumonia, and urinary tract infections.

Aminoglycosides can have serious side effects, including kidney damage and hearing loss, so they are typically reserved for use in serious infections that cannot be treated with other antibiotics. They are also used topically to treat skin infections and prevent wound infections after surgery.

It's important to note that aminoglycosides should only be used under the supervision of a healthcare professional, as improper use can lead to antibiotic resistance and further health complications.

Diacylglycerol cholinephosphotransferase is an enzyme that plays a crucial role in the synthesis of phosphatidylcholine, which is a major component of biological membranes in animals and plants. The systematic name for this enzyme is CDP-choline:1,2-diacylglycerol cholinephosphotransferase.

The reaction catalyzed by this enzyme is as follows:
CDP-choline + 1,2-diacylglycerol → CMP + phosphatidylcholine

In this reaction, CDP-choline donates its phosphocholine headgroup to the acceptor molecule, diacylglycerol, forming phosphatidylcholine and releasing CMP as a byproduct. Phosphatidylcholine is an essential structural lipid in cell membranes and is also involved in various signaling pathways.

Deficiencies or mutations in the genes encoding this enzyme can lead to neurological disorders, highlighting its importance in maintaining proper cellular function.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

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.

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.

EC 2.7.1 Phosphotransferases with an alcohol group as acceptor EC 2.7.2 Phosphotransferases with a carboxy group as acceptor EC ... Phosphotransferases are a category of enzymes (EC number 2.7) that catalyze phosphorylation reactions. The general form of the ... The phosphotransferase system (PTS) is a complex group translocation system present in many bacteria. The PTS transports sugars ... The first step of this reaction is phosphorylation of the substrate via phosphotransferase during transport. In the case of ...
Other names in common use include yeast 2'-phosphotransferase, Tpt1, Tpt1p, and 2'-phospho-tRNA:NAD+ phosphotransferase. ... In enzymology, a 2'-phosphotransferase (EC 2.7.1.160) is an enzyme that catalyzes the chemical reaction 2'-phospho-[ligated ... Steiger MA, Kierzek R, Turner DH, Phizicky EM (2001). "Substrate recognition by a yeast 2'-phosphotransferase involved in tRNA ... Culver GM, McCraith SM, Consaul SA, Stanford DR, Phizicky EM (1997). "A 2'-phosphotransferase implicated in tRNA splicing is ...
... glucose-1-phosphate phosphotransferase, G-1-P phosphotransferase, and D-glucose-1-phosphate:riboflavin 5'-phosphotransferase. ... In enzymology, a riboflavin phosphotransferase (EC 2.7.1.42) is an enzyme that catalyzes the chemical reaction alpha-D-glucose ... The systematic name of this enzyme class is alpha-D-glucose-1-phosphate:riboflavin 5'-phosphotransferase. Other names in common ... Katagiri H, Yamada H, Imai K. "The transphosphorylation reactions catalyzed by glucose 1-phosphate phosphotransferases of ...
... phosphotransferase. Brunngraber EF, Chargaff E (1967). "Purification and properties of a nucleoside phosphotransferase from ... In enzymology, a nucleoside phosphotransferase (EC 2.7.1.77) is an enzyme that catalyzes the chemical reaction a nucleotide + a ... The systematic name of this enzyme class is nucleotide:nucleoside 5'-phosphotransferase. Other names in common use include ... Prasher DC, Carr MC, Ives DH, Tsai TC, Frey PA (1982). "Nucleoside phosphotransferase from barley. Characterization and ...
The systematic name of this enzyme class is phosphoenolpyruvate:glycerone phosphotransferase. Jin RZ, Lin EC (1984). "An ... In enzymology, a phosphoenolpyruvate-glycerone phosphotransferase (EC 2.7.1.121) is an enzyme that catalyzes the chemical ... inducible phosphoenolpyruvate: dihydroxyacetone phosphotransferase system in Escherichia coli". J. Gen. Microbiol. 130 (1): 83- ... phosphotransferases) with an alcohol group as acceptor. ...
The systematic name of this enzyme class is polyphosphate:D-glucose 6-phosphotransferase. Other names in common use include ... In enzymology, a polyphosphate-glucose phosphotransferase (EC 2.7.1.63) is an enzyme that catalyzes the chemical reaction.[ ... polyphosphate glucokinase, polyphosphate-D-(+)-glucose-6-phosphotransferase, and polyphosphate-glucose 6-phosphotransferase. ... phosphotransferases) with an alcohol group as acceptor. ...
Other names in common use include PPi-glycerol phosphotransferase, and pyrophosphate-glycerol phosphotransferase. Stetten MR ( ... In enzymology, a diphosphate-glycerol phosphotransferase (EC 2.7.1.79) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is diphosphate:glycerol 1-phosphotransferase. ... phosphotransferases) with an alcohol group as acceptor. ...
Other names in common use include pyrophosphate-serine phosphotransferase, and pyrophosphate-L-serine phosphotransferase. Cagen ... In enzymology, a diphosphate-serine phosphotransferase (EC 2.7.1.80) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is diphosphate:L-serine O-phosphotransferase. ... phosphotransferases) with an alcohol group as acceptor. ...
... phosphopyruvate-protein factor phosphotransferase, phosphopyruvate-protein phosphotransferase, sugar-PEP phosphotransferase ... phosphotransferases) with a nitrogenous group as acceptor. This enzyme participates in phosphotransferase system (pts). The ... In enzymology, a phosphoenolpyruvate-protein phosphotransferase (EC 2.7.3.9) is an enzyme that catalyzes the chemical reaction ... Postma PW, Roseman S (December 1976). "The bacterial phosphoenolpyruvate: sugar phosphotransferase system". Biochimica et ...
The systematic name of this enzyme class is phosphoramidate:hexose 1-phosphotransferase. Other names in common use include ... In enzymology, a phosphoramidate-hexose phosphotransferase (EC 2.7.1.62) is an enzyme that catalyzes the chemical reaction ... phosphotransferases) with an alcohol group as acceptor. ...
O-phosphotransferase, and (erroneous). Lam KS, Kasper CB (1980). "Pyrophosphate:protein phosphotransferase: a membrane-bound ... protein phosphotransferase (erroneous), diphosphate-protein phosphotransferase (erroneous), diphosphate:[microsomal-membrane- ... In enzymology, a triphosphate-protein phosphotransferase (EC 2.7.99.1) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is triphosphate:[microsomal-membrane-protein] phosphotransferase. Other names in ...
Undecaprenyl-phosphate+glucose+phosphotransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) ... Undecaprenyl-phosphate glucose phosphotransferase (EC 2.7.8.31, GumD, undecaprenylphosphate glucosylphosphate transferase) is ... an enzyme with systematic name UDP-glucose:ditrans,octacis-undecaprenyl-phosphate glucose phosphotransferase. This enzyme ...
Anderson RL; Kamel MY (1966). "Acyl phosphate:hexose phosphotransferase (hexose phosphate:hexose phosphotransferase)". Methods ... The systematic name of this enzyme class is acyl-phosphate:D-hexose phosphotransferase. This enzyme is also called hexose ... In enzymology, an acyl-phosphate-hexose phosphotransferase (EC 2.7.1.61) is an enzyme that catalyzes the chemical reaction acyl ... doi:10.1016/0076-6879(66)09080-3. Kamel MY, Anderson RL (1967). "Acyl phosphate: hexose phosphotransferase. Purification and ...
In enzymology, an undecaprenyl-phosphate galactose phosphotransferase (EC 2.7.8.6) is an enzyme that catalyzes the chemical ... The systematic name of this enzyme class is UDP-galactose:undecaprenyl-phosphate galactose phosphotransferase. Other names in ... common use include poly(isoprenol)-phosphate galactose phosphotransferase, poly(isoprenyl)phosphate ...
... (or PTS-AG superfamily according to TCDB) is a superfamily of phosphotransferase enzymes ... The bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) transports and phosphorylates its sugar substrates in a ... Family Phosphotransferases system Chen JS, Reddy V, Chen JH, Shlykov MA, Zheng WH, Cho J, Yen MR, Saier MH (2012-01-01). " ... sugar phosphotransferase system". Journal of Molecular Microbiology and Biotechnology. 11 (6): 345-60. doi:10.1159/000095636. ...
... may refer to: Riboflavin phosphotransferase, an enzyme Phosphoglucokinase, an enzyme ...
In enzymology, a dolichyl-diphosphate-polyphosphate phosphotransferase (EC 2.7.4.20) is an enzyme that catalyzes the chemical ... The systematic name of this enzyme class is dolichyl-diphosphate:polyphosphate phosphotransferase. This enzyme is also called ... dolichylpyrophosphate:polyphosphate phosphotransferase. Naumov AV, Shabalin YA, Vagabov VM, Kulaev IS. "Two pathways of ... phosphotransferases) with a phosphate group as acceptor. ...
ATP:guanido phosphotransferases contain a C-terminal catalytic domain which consists of a duplication where the common core ... In molecular biology, the ATP:guanido phosphotransferase family is a family of structurally and functionally related enzymes, ...
The systematic name of this enzyme class is 3-phospho-D-glyceroyl-phosphate:polyphosphate phosphotransferase. Other names in ... In enzymology, a 3-phosphoglyceroyl-phosphate-polyphosphate phosphotransferase (EC 2.7.4.17) is an enzyme that catalyzes the ... 3-diphosphoglycerate-polyphosphate phosphotransferase. Kulaev IS, Bobyk MA (1971). "[Detection in Neurospora crassa of a new ... enzyme--1,3-diphosphoglycerate: polyphosphate phosphotransferase]". Biokhimiia. 36 (2): 426-9. PMID 5557827. Kukaev IS, Bobyk ...
pyruvate,+phosphate+dikinase)-phosphate+phosphotransferase at the U.S. National Library of Medicine Medical Subject Headings ( ... Pyruvate, phosphate dikinase)-phosphate phosphotransferase (EC 2.7.4.27, PPDK regulatory protein, pyruvate, phosphate dikinase ... phosphate phosphotransferase. This enzyme catalyses the following chemical reaction [pyruvate, phosphate dikinase] phosphate + ...
... sucrose phosphotransferase system II, and protein-Npi-phosphohistidine:sugar N-pros-phosphotransferase. This enzyme ... PEP-dependent phosphotransferase enzyme II, PEP-sugar phosphotransferase enzyme II, phosphoenolpyruvate-sugar ... In enzymology, a protein-Npi-phosphohistidine-sugar phosphotransferase (EC 2.7.1.69) is an enzyme that catalyzes the chemical ... The systematic name of this enzyme class is protein-Npi-phosphohistidine:sugar Npi-phosphotransferase. Other names in common ...
... (EC 2.7.4.28, PSRP) is an enzyme with systematic name (pyruvate, water ... pyruvate,+water+dikinase)-phosphate+phosphotransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH ... dikinase) phosphate:phosphate phosphotransferase. This enzyme catalyses the following chemical reaction [pyruvate, water ...
The systematic name of this enzyme class is sn-glycerol-3-phosphate:D-glucose 6-phosphotransferase. Kiaira JK, Njogu RM (1989 ... In enzymology, a glycerol-3-phosphate-glucose phosphotransferase (EC 2.7.1.142) is an enzyme that catalyzes the chemical ... phosphotransferases) with an alcohol group as acceptor. ...
Other names in common use include UDP-glucose:glycoprotein glucose-1-phosphotransferase, GlcPTase, Glc-phosphotransferase, and ... In enzymology, an UDP-glucose-glycoprotein glucose phosphotransferase (EC 2.7.8.19) is an enzyme that catalyzes the chemical ... Koro LA, Marchase RB (1982). "A UDP-glucose:glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina". Cell ...
... the chloramphenicol phosphotransferase-like protein family includes the chloramphenicol 3-O phosphotransferase (CPT) expressed ... Izard T, Ellis J (June 2000). "The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation ... "Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity". ...
In enzymology, a 1-alkenyl-2-acylglycerol choline phosphotransferase (EC 2.7.8.22) is an enzyme that catalyzes the chemical ...
... galactose-1-phosphotransferase, and galactosyl phosphotransferase. Nakanishi Y, Otsu K, Suzuki S (1983). "Enzymatic transfer of ... The systematic name of this enzyme class is UDP-galactose:UDP-N-acetyl-D-glucosamine galactose phosphotransferase. Other names ... In enzymology, an UDP-galactose-UDP-N-acetylglucosamine galactose phosphotransferase (EC 2.7.8.18) is an enzyme that catalyzes ... in common use include uridine diphosphogalactose-uridine diphosphoacetylglucosamine galactose-1-phosphotransferase, ...
Aminoglycoside-3'-phosphotransferase (APH(3')), also known as aminoglycoside kinase, is an enzyme that primarily catalyzes the ... The systematic name of this enzyme class is ATP:kanamycin 3'-O-phosphotransferase. This enzyme is also called neomycin- ... Fong DH, Berghuis AM (2002). "Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type IIIa ADP Kanamycin A Complex". ... McKay GA, Thompson PR, Wright GD (1994). "Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: ...
There is a mitochondrial GTP:AMP phosphotransferase, also specific for the phosphorylation of AMP, that can only use GTP or ITP ... Adenylate kinase (EC 2.7.4.3) (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the ... Tomasselli AG, Noda LH (January 1979). "Mitochondrial GTP-AMP phosphotransferase. 2. Kinetic and equilibrium dialysis studies ...
The systematic name of this enzyme class is ATP:ammonia phosphotransferase. Other names in common use include phosphoramidate- ... adenosine diphosphate phosphotransferase, and phosphoramidate-ADP-phosphotransferase. Dowler MJ, Nakada HI (1968). "Yeast ... phosphoramidate-adenosine diphosphate phosphotransferase". J. Biol. Chem. 243 (7): 1434-40. PMID 5647264. Portal: Biology v t e ... phosphotransferases) with a nitrogenous group as acceptor. ...
EC 2.7.1 Phosphotransferases with an alcohol group as acceptor EC 2.7.2 Phosphotransferases with a carboxy group as acceptor EC ... Phosphotransferases are a category of enzymes (EC number 2.7) that catalyze phosphorylation reactions. The general form of the ... The phosphotransferase system (PTS) is a complex group translocation system present in many bacteria. The PTS transports sugars ... The first step of this reaction is phosphorylation of the substrate via phosphotransferase during transport. In the case of ...
Crystal structure of the GAF domain from Acinetobacter phosphoenolpyruvate-protein phosphotransferase ... Phosphoenolpyruvate-protein phosphotransferase. A, B. 171. Acinetobacter baylyi ADP1. Mutation(s): 0 Gene Names: ptsP, ... Crystal structure of the GAF domain from Acinetobacter phosphoenolpyruvate-protein phosphotransferase.. Cuff, M.E., Shackelford ... Crystal structure of the GAF domain from Acinetobacter phosphoenolpyruvate-protein phosphotransferase. *PDB DOI: https://doi. ...
choline-ethanolamine phosphotransferase activity. Introduction. Membrane phospholipids have a dual role as structural building ... This effect of NMDA is produced by a reduction of choline-ethanolamine phosphotransferase activity. Because PtdCho and PtdEtn ... NMDA Receptor Overactivation Inhibits Phospholipid Synthesis by Decreasing Choline-Ethanolamine Phosphotransferase Activity. ... NMDA Receptor Overactivation Inhibits Phospholipid Synthesis by Decreasing Choline-Ethanolamine Phosphotransferase Activity ...
Crystal structure of a putative phospho transferase (sp_1565) from streptococcus pneumoniae tigr4 at 2.00 A resolution. *PDB ...
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The enzyme is responsible for the synthesis of most of the cellular polyphosphate, using the terminal phosphate of ATP as substrate ...
"Phosphotransferases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Phosphotransferases" by people in this website by year, and ... Below are the most recent publications written about "Phosphotransferases" by people in Profiles. ... whether "Phosphotransferases" was a major or minor topic of these publications. To see the data from this visualization as text ...
GO:0016780: phosphotransferase activity, for other substituted phosphate groups (Molecular function). Catalysis of the ...
Phosphotransferases associated with the regulation of kinesin motor activity. Lisa Lindesmith, James M. McIlvain, Yair Argon, ... Phosphotransferases associated with the regulation of kinesin motor activity. Journal of Biological Chemistry. 1997 Sep 5;272( ... Phosphotransferases associated with the regulation of kinesin motor activity. In: Journal of Biological Chemistry. 1997 ; Vol. ... Phosphotransferases associated with the regulation of kinesin motor activity. / Lindesmith, Lisa; McIlvain, James M.; Argon, ...
Synonyms: ATP:pyruvate 2-O-phosphotransferase, PK. CAS 9001-59-6. Browse Pyruvate Kinase from rabbit muscle and related ...
We have partially purified phosphotransferase enzyme I and have purified a heat-stable phosphocarrier protein (HPr) to apparent ... The sucrose phosphotransferase system of Streptococcus mutans catalyzes the phosphorylation of sucrose to sucrose-6-phosphate ... Phosphoenolpyruvate Sugar Phosphotransferase System, Phosphotransferases (Nitrogenous Group Acceptor), Staphylococcus aureus, ... The sucrose phosphotransferase system of Streptococcus mutans catalyzes the phosphorylation of sucrose to sucrose-6-phosphate ...
Multiple whole-genome alignments shed light on to the presence of a novel cellobiose phosphotransferase system (PTS) exclusive ... A unique Phosphotransferase System (PTS) Cluster Conserved in P. parmentieri. A 4.5 kb region, which contained five genes, was ... Wu, M.-C.; Chen, Y.-C.; Lin, T.-L.; Hsieh, P.-F.; Wang, J.-T. Cellobiose-specific phosphotransferase system of Klebsiella ... Multiple whole-genome alignments shed light on to the presence of a novel cellobiose phosphotransferase system (PTS) exclusive ...
168 p., Dissertation Abstracts International, Volume: 27-10, Section: B, page: 3441. ...
Architects of the membrane: structures of eukaryotic choline phosphotransferase 1 and choline/ethanolamine phosphotransferase 1 ... New cryo-electron microscopy (cryo-EM) structures of CDP- and CDP-choline-bound choline phosphotransferase 1 (CHPT1) and ... choline/ethanolamine phosphotransferase 1 (CEPT1), involved in the metabolism of the two main lipids in eukaryotic cell ...
Phosphotransferases / classification * Phosphotransferases / genetics * Protein Serine-Threonine Kinases / genetics* * Protein- ...
MSMEG_3846 MSMEG_3846 Phosphotransferase enzyme family protein. Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155). ...
... of an enzyme called GlcNAc-1-phosphotransferase. Learn about this gene and related health conditions. ... GlcNAc-1-phosphotransferase is involved in the first step of making a molecule called mannose-6-phosphate (M6P). M6P acts as a ... Specifically, GlcNAc-1-phosphotransferase transfers a molecule called GlcNac-1-phosphate to a newly produced hydrolase. In the ... The GNPTG gene provides instructions for making one part, the gamma subunit, of an enzyme called GlcNAc-1-phosphotransferase. ...
Putative phosphotransferase with licD domain (involved in phosphorylcholine decoration of teichoic acid). 1,269. 33. ... Putative phosphotransferase with licD domain (involved in phosphorylcholine decoration of teichoic acid). 1,290. 45. ...
Neomycin phosphotransferase. MS medium:. Musashige and Skoog medium. GUS:. β-Glucuronidase. uidA :. β-Glucuronidase gene ...
enables tRNA 2-phosphotransferase activity NAS Non-traceable Author Statement. more info ...
Stereochemical course of reactions catalyzed by the bacterial phosphoenolpyruvate: glucose phosphotransferase system journal, ... Comparison of individual component deletions in a glucose-specific phosphotransferase system revealed their different ...
II-related mutations inhibit the exit from the endoplasmic reticulum and proteolytic cleavage of GlcNAc-1-phosphotransferase ...
A Membrane-Targeted Peptide Inhibiting PtxA of Phosphotransferase System Blocks Streptococcus mutans.. Xiang, Shao-Wen; Shao, ... takes up carbohydrates through the phosphoenolpyruvate sugar phosphotransferase system (PTS). This study aimed to identify a ...
Phosphoenolpyruvate-protein phosphotransferase (PtsI). Q99V14. 1.63 ↓. 19. Elongation factor Ts (Tsf). P99171. 1.59 ↓. 1.54 ↓. ...
AMINOGLYCOSIDE PHOSPHOTRANSFERASE (2)-IA (CTD OF AAC(6)- IE/APH(2)-IA) IN COMPLEX WITH GDP, MAGNESIUM, AND GENTAMICIN C1 ... AMINOGLYCOSIDE PHOSPHOTRANSFERASE (2)-IA (CTD OF AAC(6)- IE/APH(2)-IA) IN COMPLEX WITH GDP, MAGNESIUM, AND GENTAMICIN C1 ... AMINOGLYCOSIDE PHOSPHOTRANSFERASE (2)-IA (CTD OF AAC(6)- IE/APH(2)-IA) IN COMPLEX WITH GDP, MAGNESIUM, AND GENTAMICIN C1 ...
T1 - Confirmation and elimination of xylose metabolism bottlenecks in glucose phosphoenolpyruvate-dependent phosphotransferase ... Confirmation and elimination of xylose metabolism bottlenecks in glucose phosphoenolpyruvate-dependent phosphotransferase ... Confirmation and elimination of xylose metabolism bottlenecks in glucose phosphoenolpyruvate-dependent phosphotransferase ... Confirmation and elimination of xylose metabolism bottlenecks in glucose phosphoenolpyruvate-dependent phosphotransferase ...
Safety assessment of the neomycin phosphotransferase II (NPTII) protein. Bio/Technology 11, 1543-1547 (1993). ...
neomycin phosphotransferase II enzyme. allows transformed plants to metabolize neomycin and kanamycin antibiotics during ...
neomycin phosphotransferase II enzyme. allows transformed plants to metabolize neomycin and kanamycin antibiotics during ...
neomycin phosphotransferase II enzyme. allows transformed plants to metabolize neomycin and kanamycin antibiotics during ...
  • Streptococcus mutans , the primary cause of dental caries , takes up carbohydrates through the phosphoenolpyruvate sugar phosphotransferase system (PTS). (bvsalud.org)
  • We have partially purified phosphotransferase enzyme I and have purified a heat-stable phosphocarrier protein (HPr) to apparent homogeneity, by gel filtration and ion-exchange chromatography from the soluble fraction. (ox.ac.uk)
  • The GNPTG gene provides instructions for making one part, the gamma subunit, of an enzyme called GlcNAc-1-phosphotransferase. (medlineplus.gov)
  • To overcome this substrate utilization defect, a predicted glcG gene, encoding enzyme II of the D-glucose phosphoenolpyruvate-dependent phosphotransferase system (PTS), was first disrupted in the ABE-producing model strain Clostridium acetobutylicum ATCC 824, resulting in greatly improved D-xylose and L-arabinose consumption in the presence of D-glucose. (hw.ac.uk)
  • Phosphotransferases are generally classified according to the acceptor molecule. (wikipedia.org)
  • EC 2.7.1 Phosphotransferases with an alcohol group as acceptor EC 2.7.2 Phosphotransferases with a carboxy group as acceptor EC 2.7.3 Phosphotransferases with a nitrogenous group as acceptor EC 2.7.4 Phosphotransferases with a phosphate group as acceptor EC 2.7.9 Phosphotransferases with paired acceptors. (wikipedia.org)
  • The sucrose phosphotransferase system of Streptococcus mutans catalyzes the phosphorylation of sucrose to sucrose-6-phosphate with concomitant translocation of this disaccharide across the cytoplasmic membrane in reactions requiring intracellular phosphoenolpyruvate. (ox.ac.uk)
  • GlcNAc-1-phosphotransferase is involved in the first step of making a molecule called mannose-6-phosphate (M6P). (medlineplus.gov)
  • Specifically, GlcNAc-1-phosphotransferase transfers a molecule called GlcNac-1-phosphate to a newly produced hydrolase. (medlineplus.gov)
  • The bacteriocin Angicin interferes with bacterial membrane integrity through interaction with the mannose phosphotransferase system. (uni-ulm.de)
  • Resolution of the phosphotransferase enzymes of Streptococcus mutans: purification and preliminary characterization of a heat-stable phosphocarrier protein. (ox.ac.uk)
  • The nptII protein, neomycin phosphotransferase II, confers resistance to some aminoglycoside antibiotics including neomycin and kanamycin, and was used as a selectable marker for transformed plant cells. (cbd.int)
  • The phosphotransferase system (PTS) is a complex group translocation system present in many bacteria. (wikipedia.org)
  • A Membrane-Targeted Peptide Inhibiting PtxA of Phosphotransferase System Blocks Streptococcus mutans. (bvsalud.org)
  • Over-expression of Leishmania major MAP kinases reveals stage-specific inductin of phosphotransferase activity. (laserfocusworld.com)
  • Phosphotransferases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (wakehealth.edu)
  • Phosphotransferases are a category of enzymes (EC number 2.7) that catalyze phosphorylation reactions. (wikipedia.org)
  • The first step of this reaction is phosphorylation of the substrate via phosphotransferase during transport. (wikipedia.org)
  • Metabolic labeling experiments in whole cells showed that NMDA receptor overactivation does not modify the activity of phosphocholine or phosphoethanolamine cytidylyltransferases but strongly inhibits choline-ethanolamine phosphotransferase activity. (jneurosci.org)
  • These mutations result in reduced the activity of GlcNAc-1-phosphotransferase, which disrupts tagging of hydrolases with M6P. (medlineplus.gov)
  • GlcNAc-1-phosphotransferase helps prepare certain newly made enzymes for transport to lysosomes. (medlineplus.gov)
  • Pohl S, Tiede S, Castrichini M, Cantz M, Gieselmann V, Braulke T. Compensatory expression of human N-acetylglucosaminyl-1-phosphotransferase subunits in mucolipidosis type III gamma. (medlineplus.gov)
  • These mice harbor loxP sites that flank exons 2 through 4 of the Slc6a8 gene and a positive selection FRT-flanked neomycin phosphotransferase gene (neo) cassette. (jax.org)
  • EC 2.7.1 Phosphotransferases with an alcohol group as acceptor EC 2.7.2 Phosphotransferases with a carboxy group as acceptor EC 2.7.3 Phosphotransferases with a nitrogenous group as acceptor EC 2.7.4 Phosphotransferases with a phosphate group as acceptor EC 2.7.9 Phosphotransferases with paired acceptors. (wikipedia.org)
  • Analysis of mucolipidosis II/III GNPTAB missense mutations identifies domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase involved in catalytic function and lysosomal enzyme recognition. (nih.gov)
  • There are two paralogous Escherichia coli phosphotransferase systems, one for sugar import (PTS sugar ) and one for nitrogen regulation (PTS Ntr ), that utilize proteins enzyme I sugar (EI sugar ) and HPr, and enzyme I Ntr (EI Ntr ) and NPr, respectively. (nih.gov)
  • This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). (expasy.org)
  • The GNPTG gene provides instructions for making one part, the gamma subunit, of an enzyme called GlcNAc-1-phosphotransferase. (medlineplus.gov)
  • Structure of the NPr:EIN(Ntr) Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems. (nih.gov)
  • Phosphotransferases (Paired Acceptors)" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ucdenver.edu)
  • This graph shows the total number of publications written about "Phosphotransferases (Paired Acceptors)" by people in this website by year, and whether "Phosphotransferases (Paired Acceptors)" was a major or minor topic of these publications. (ucdenver.edu)
  • Below are the most recent publications written about "Phosphotransferases (Paired Acceptors)" by people in Profiles. (ucdenver.edu)
  • GlcNAc-1-phosphotransferase helps prepare certain newly made enzymes for transport to lysosomes. (medlineplus.gov)
  • Phosphotransferases are a category of enzymes (EC number 2.7) that catalyze phosphorylation reactions. (wikipedia.org)
  • Defects in the GlcNac-1-phosphotransferase complex cause two diseases, mucolipidosis type II and III, which are characterized by missorting and cellular loss of lysosomal enzymes, and lysosomal accumulation of storage material. (nih.gov)
  • The recent identification of two genes, GNPTAB and GNPTG, encoding the three subunits of GlcNac-1-phosphotransferase leads to an improvement of both pre- and postnatal diagnosis of affected individuals, and permits the analysis of structural requirements for efficient formation of mannose 6-phosphate residues on lysosomal enzymes. (nih.gov)
  • Pohl S, Tiede S, Castrichini M, Cantz M, Gieselmann V, Braulke T. Compensatory expression of human N-acetylglucosaminyl-1-phosphotransferase subunits in mucolipidosis type III gamma. (medlineplus.gov)
  • The main aim of the work presented in this thesis was to further our understanding of the role of Pyrrophosphate: fructose 6-phosphate 1-phosphotransferase (PFP) in sugarcane, by specifically investigating its potential contribution to phloem metabolism. (sun.ac.za)
  • The phosphoenolpyruvate-carbohydrate phosphotransferase system (PTS) is a multistep chemical process that regulates the intake and use of carbohydrates by bacteria. (emerging-researchers.org)
  • The role of the gamma-subunits for activity, stability and oligomerization of the GlcNac-1-phosphotransferase subunits is still unclear. (nih.gov)
  • The first step of this reaction is phosphorylation of the substrate via phosphotransferase during transport. (wikipedia.org)
  • 13. Mechanism of the reaction catalysed by cytosolic 5'-nucleotidase/phosphotransferase: formation of a phosphorylated intermediate. (nih.gov)
  • The bacterial phosphotransferase system (PTS) couples phosphoryl transfer, via a series of bimolecular protein-protein interactions, to sugar transport across the membrane. (nih.gov)
  • Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase. (expasy.org)
  • A bifunctional aminoglycoside acetyltransferase/phosphotransferase conferring tobramycin resistance provides an efficient selectable marker for plastid transformation. (mpg.de)
  • Analysis of the catalytic domain of phosphotransferase activity of two avian sarcoma virus-transforming proteins. (wikidata.org)
  • 9. The bifunctional cytosolic 5'-nucleotidase: regulation of the phosphotransferase and nucleotidase activities. (nih.gov)
  • Phosphotransferases are generally classified according to the acceptor molecule. (wikipedia.org)
  • We constructed ethanologenic E. coli strains with a glucose phosphotransferase (ptsG) mutation and used the mutants to ferment glucose, arabinose, and xylose, singly and in mixtures, to ethanol. (usda.gov)