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  • ¿µ¹®
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  • phospholipidemia
    ÀÎÁöÁúÇ÷Áõ(¡­úìñø).
  • phosphology
    Àλê»êÈ­·Ð(ìÝ߫߫ûùÖå).
  • phospholpid chemistry
    ÀÎÁöÁúÈ­ÇÐ
  • phospholysis
    °¡ÀλêºÐÇØ.
  • phosphomolybdate
    Àθô¸®ºêµ§»ê¿°
  • phosphomonoesterase
    Æ÷½ºÆ÷¸ð³ë¿¡½ºÅ×¶ó¾ÆÁ¦.
  • phosphomonoesterases
    Æ÷½ºÆ÷¸ð³ë¿¡½ºÅ×¶ó¾ÆÁ¦
  • phosphoprotein
    ÀδܹéÁú(ìÝÓ±ÛÜòõ).
  • phosphoptomaine
    Æ÷½ºÆ÷ÇÁÅ丶ÀÎ.
  • phosphopyruvic acid
    Æ÷½ºÆ÷ÇǺ긣»ê.
  • phosphorescence
    Àα¤(ìÝÎÃ)
  • phosphorescence
    Çü±¤, ¹ß±¤
  • phosphoriboisomerase
    Æ÷½ºÆ÷¸®º¸À̼ÒÀ̼Ҹ޶óÁ¦
  • phosphoribosyl pyrophosphatase
    Æ÷½ºÆ÷¸®º¸½ÇÇÇ·ÎÆ÷½ºÆ÷ŸÁ¦
  • phosphoribosyl pyrophosphate synthetase
    Æ÷½ºÆ÷¸®º¸½ÇÇÇ·ÎÆ÷½ºÆäÀÌÆ®½ÅÅןÁ¦<ÇÕ¼ºÈ¿¼Ò>
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    ÀÎÁöÁúÇ÷Áõ(¡­úìñø).
  • phosphology
    Àλê»êÈ­·Ð(ìÝ߫߫ûùÖå).
  • phospholpid chemistry
    ÀÎÁöÁúÈ­ÇÐ
  • phospholysis
    °¡ÀλêºÐÇØ.
  • phosphomolybdate
    Àθô¸®ºêµ§»ê¿°
  • phosphomonoesterase
    Æ÷½ºÆ÷¸ð³ë¿¡½ºÅ×¶ó¾ÆÁ¦.
  • phosphomonoesterases
    Æ÷½ºÆ÷¸ð³ë¿¡½ºÅ×¶ó¾ÆÁ¦
  • phosphopoda
  • phosphoprotein
    ÀδܹéÁú(ìÝÓ±ÛÜòõ).
  • phosphoptomaine
    Æ÷½ºÆ÷ÇÁÅ丶ÀÎ.
  • phosphopyruvic acid
    Æ÷½ºÆ÷ÇǺ긣»ê.
  • phosphorescence
    Çü±¤, ¹ß±¤
  • phosphorescence
    Àα¤(ìÝÎÃ)
  • phosphoriboisomerase
    Æ÷½ºÆ÷¸®º¸À̼ÒÀ̼Ҹ޶óÁ¦
  • phosphoribosyl pyrophosphatase
    Æ÷½ºÆ÷¸®º¸½ÇÇÇ·ÎÆ÷½ºÆ÷ŸÁ¦
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  • phosphoramidic acid
    Æ÷½ºÆ÷¶ó¹Ìµå»ê(ß«)
  • phosphorescence
    Àα¤(ìÝÎÃ)
  • phosphorimetry
    Àα¤ÃøÁ¤(ìÝÎÃö´ïÒ)
  • phosphoroclastic reaction
    ÀλêÀý´Ü ¹ÝÀÀ(×òß«ï·Ó¨Úãëë)
  • phosphoroimmunoassay
    Àλê¸é¿ª(×òß«Øóæ¹)¾Æ½êÀÌ
  • phosphorolysis
    °¡ÀλêºÐÇØ(Ê¥×òß«ÝÂú°)
  • phosphoryl group
    ÀλêÈ­±â(×òß«ûùÐñ)
  • phosphoryl transfer potential
    ÀλêÈ­ ÀüÀÌ ÀüÀ§(×òß«ûùï®ì¹ï³êÈ)
  • phosphoryl-group carrier
    ÀλêÈ­±â ¿î¹Ýü(×òß«ûùÐñê¡Úæô÷)
  • phosphoryl-group transfer
    ÀλêÈ­±â ÀüÀÌ(×òß«ûùÐñï®ì¹)
  • phosphorylase
    Æ÷½ºÆ÷¸±·¹À̽º
  • phosphorylase kinase
    Æ÷½ºÆ÷¸±·¹À̽ºÄ«À̳×À̽º
  • phosphorylase phosphatase
    Æ÷½ºÆ÷¸±·¹À̽ºÆ÷½ºÆÄÅ×À̽º
  • phosphorylation
    ÀλêÈ­(×òß«ûù)
  • phosphorylation potential
    ÀλêÈ­ ÀüÀ§(×òß«ûùï³êÈ)
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
phosphoenolpyruvate carboxylase <enzyme> An enzyme with high affinity for carbon dioxide. It catalyses irreversibly the formation of oxaloacetate from phosphoenolpyruvate and carbon dioxide. This fixation of carbon dioxide in several bacteria and some plants is the first step in the biosynthesis of glucose.
Chemical name: Orthophosphate:oxaloacetate carboxy-lyase (phosphorylating)
Registry number: EC 4.1.1.31
(12 Dec 1998)
phosphoenolpyruvate carboxylase kinase <enzyme> From bryophyllum fedtschenkoi plant and maise; phosphorylates phosphoenolpyruvate carboxylase on serine near the n-terminus; activity controlled by circadian rhythms
Registry number: EC 2.7.10.-
Synonym: pep carboxylase kinase, pepc kinase
(26 Jun 1999)
phosphoenolpyruvate mutase <enzyme> Isolated from t pyriformis; forms a carbon-phosphorus bond in the transformation of phosphoenolpyruvate to phosphonopyruvate
Registry number: EC 5.4.2.9
Synonym: phosphoenolpyruvate phosphomutase
(26 Jun 1999)
phosphoenolpyruvate sugar phosphotransferase system <enzyme> The bacterial sugar phosphotransferase system (pts) that catalyses the transfer of the phosphoryl group from phosphoenolpyruvate to its sugar substrates (the pts sugars) concomitant with the translocation of these sugars across the bacterial membrane. The phosphorylation of a given sugar requires four proteins, two general proteins, enzyme I and hpr and a pair of sugar-specific proteins designated as the enzyme II complex. The pts has also been implicated in the induction of synthesis of some catabolic enzyme systems required for the utilization of sugars that are not substrates of the pts as well as the regulation of the activity of adenylate cyclase.
Registry number: EC 2.7.1.-
(12 Dec 1998)
phosphoenolpyruvate-cellobiose phosphotransferase <enzyme> Catalytic domain of the phosphoenolpyruvate-dependent cellulose phosphotransferase system
Registry number: EC 2.7.1.-
Synonym: enzyme IIb(cellobiose), enzyme IIb (cel)
(26 Jun 1999)
phosphoenolpyruvate-glucose phosphotransferase <enzyme> Specific for glucose and nonmetabolizable analogs methyl alpha glucoside, beta-d-thioglucose and 5-thioglucose
Registry number: EC 2.7.1.-
Synonym: II-b(glc) peppts, enzyme II-b(glc) phosphoenolpyruvate phosphotransferase system, enzyme II (glucose), glucose-specific permease, phosphotransferase system, beta-glucosidase permease, beta-glucoside permease, glucose permease, enzyme II(glc), bglp gene product, syta gene product
(26 Jun 1999)
phosphoenolpyruvate-maltose phosphotransferase <enzyme> Partial amino acid sequence of enzyme identified from fusobacterium mortiferum.
Registry number: EC 2.7.1.-
Synonym: enzyme IIb (maltose), maltose enzyme IIb, malb gene product
(26 Jun 1999)
phosphoenolpyruvate-mannose phosphotransferase <enzyme> Consists of three subunits IIab(man), IIc(man), and IId(man); many encodes IIc(man) and manz encodes IId(man)
Registry number: EC 2.7.1.-
Synonym: enzyme II (mannose), mannose permease, many gene product, manz gene product, IIab(man) subunit, IIc(man) subunit, IId(man) subunit
(26 Jun 1999)
phosphoenolpyruvate-protein phosphotransferase <enzyme> Enzyme I of the system
Registry number: EC 2.7.3.9
Synonym: enzyme I, phosphoenolpyruvate sugar phosphotransferase system, enzyme I peppts, ptsi gene product, ptsj gene product, ptsp gene product, enzyme i(ntr)
(26 Jun 1999)
phosphoenolpyruvate-sorbose phosphotransferase <enzyme> From klebsiella pneumoniae; catalyses transport and phosphorylation of sorbose to sorbose 1-phosphate
Registry number: EC 2.7.1.-
Synonym: enzyme II (sorbose), sorbose-specific enzyme II, gene sora product
(26 Jun 1999)
phosphoenolpyruvate-trehalose phosphotransferase <enzyme> Trea encodes the enzyme from bacillus subtilis; the escherichia coli enzyme II specific for trehalose; genbank u06195; do not confuse with tax-responsive element treb protein
Registry number: EC 2.7.1.-
Synonym: enzyme II (trehalose), enzyme II(tre), eii(tre) protein, treb enzyme II protein, trep gene product
(26 Jun 1999)
phosphoenolpyruvic acid CH2==C(OPO3H2)-COOH;the phosphoric ester of pyruvic acid in the latter's enol form; an intermediate in the conversion of glucose to pyruvic acid and an example of a high energy phosphate ester.
Phosphoenolpyruvic acid carboxykinase, an enzyme that catalyses the reaction of oxaloacetate and GTP to form phosphoenolpyruvic acid, CO2, and GDP; a key enzyme in gluconeogenesis; the biosynthesis of this enzyme is decreased by insulin.
Synonym: phosphoenolpyruvate carboxykinase.
(05 Mar 2000)
phosphoethanolamine 2-O3POCH2CH2NH3 +;a key intermediate in the formation of cephalins; formed in liver and brain by phosphorylation of ethanolamine.
Phosphoethanolamine cytidylyltransferase, a key enzyme in the biosynthesis of cephalins; it catalyses the reaction of phosphoethanolamine and CTP to form CDP-ethanolamine and pyrophosphate.
(05 Mar 2000)
phosphoethanolamine methyltransferase <enzyme> Involved in the initial step in the sequential methylation of phosphoethanolamine to phosphocholine
Registry number: EC 2.1.1.-
Synonym: petn-mtase
(26 Jun 1999)
phosphofructokinase <enzyme> The pacemaker enzyme of glycolysis. Coverts fructose 6 phosphate to fructose 1,6 bisphosphate. A tetrameric allosteric enzyme that is sensitive to the ATP/ADP ratio.
(18 Nov 1997)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 5 ÆäÀÌÁö: 3
  • Phosphofructokinase-1 - »õâ An allosteric enzyme that regulates glycolysis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-1,6-bisphosphate. D-tagatose- 6-phosphate and sedoheptulose-7-phosphate also are acceptors. UTP, CTP, and ITP also are donors. In human phosphofructokinase-1, three types of subunits have been identified. They are PHOSPHOFRUCTOKINASE-1, MUSCLE TYPE; PHOSPHOFRUCTOKINASE-1, LIVER TYPE; and PHOSPHOFRUCTOKINASE-1, C TYPE; found in platelets, brain, and other tissues.
    Synonyms : 6-Phosphofructo-1-kinase, Fructose-6-P 1-Kinase, Fructose-6-phosphate 1-Phosphotransferase, 6 Phosphofructokinase, Phosphofructokinase 1
  • Phosphofructokinase-1, Liver Type - »õâ An allosteric enzyme that regulates glycolysis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-1,6-bisphosphate. In human liver, the 6-phosphofructose-1-kinase exists as the homotetramer of L subunits.
    Synonyms : Phosphofructo-1-kinase Isozyme B, Phosphofructokinase 1, Liver Type
  • Phosphofructokinase-1, Muscle Type - »õâ An allosteric enzyme that regulates glycolysis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-1,6-bisphosphate. In humans, PHOSPHOFRUCTOKINASE-1 in muscle exists as the homotetramer of M subunits. Defects in this muscle enzyme cause GLYCOGEN STORAGE DISEASE TYPE VII, also known as Tarui's disease.
    Synonyms : Phosphofructo-1-kinase Isozyme A, Phosphofructokinase 1, Muscle Type
  • Phosphofructokinase-1, Type C - »õâ An allosteric enzyme that regulates glycolysis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-1,6-bisphosphate. In the humans, 6-phosphofructose-1-kinase isozyme C is found in platelets, brain, heart, kidney, colon and testis. This isozyme C can exist as the homotetramer of C subunits (P subunits), or heterotetramer of C type and L type subunits.
    Synonyms : Phosphofructo-1-kinase Isozyme C, Phosphofructokinase 1, Type C
  • Phosphofructokinase-2 - »õâ An allosteric enzyme that regulates glycolysis and gluconeogenesis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-2,6-bisphosphate, an allosteric effector for the other 6-phosphofructokinase, PHOSPHOFRUCTOKINASE-1. Phosphofructokinase-2 is bifunctional: the dephosphorylated form is a kinase and the phosphorylated form is a phosphatase that breaks down fructose-2,6-bisphosphate to yield fructose-6-phosphate.
    Synonyms : 6-PF-2-K-Fru-2, 6-P(2)ase, 6-Phosphofructo 2-kinase-fructose 2, 6-bisphosphatase, 6PF2K, ATP-D-Fructose-6-phosphate 2-phosphotransferase, F Kinase-F-bisphosphatase, Fru-6-P, 2-kinase, Fru-kinase-Fru-bisphosphatase, Fructose 2, 6-bisphosphatase
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phosphorus a multivalent nonmetallic element of the nitrogen family that occurs commonly in inorganic phosphate rocks and as organic phosphates in all living cells; is highly reactive and occurs in several allotropic forms morning star: a planet (usually Venus) seen just before sunrise in the eastern sky
Ãâó: wordnet.princeton.edu/perl/webwn
phospho- Phosphorus, (from the Greek language Phosphoros meaning "light bearing"), is the chemical element in the periodic table that has the symbol P and atomic number 15. A multivalent, nonmetal of the nitrogen group, phosphorus is commonly found in inorganic phosphate rocks and in all living cells. Due to its high reactivity, it is never found as a free element in nature. ...
Ãâó: en.wikipedia.org/wiki/Phospho
phosphorous Phosphorus, (from the Greek language Phosphoros meaning "light bearing"), is the chemical element in the periodic table that has the symbol P and atomic number 15. A multivalent, nonmetal of the nitrogen group, phosphorus is commonly found in inorganic phosphate rocks and in all living cells. Due to its high reactivity, it is never found as a free element in nature. ...
Ãâó: en.wikipedia.org/wiki/Phosphorous
phosphorus-32 Phosphorus, (from the Greek language Phosphoros meaning "light bearing"), is the chemical element in the periodic table that has the symbol P and atomic number 15. A multivalent, nonmetal of the nitrogen group, phosphorus is commonly found in inorganic phosphate rocks and in all living cells. Due to its high reactivity, it is never found as a free element in nature. ...
Ãâó: en.wikipedia.org/wiki/Phosphorus-32
phosphorescence Phosphorescence is the result of a radiative (light emitting) transition involving a change in the spin multiplicity of (in most cases) a molecule from excited state singlet to excited state triplet. This transition is quantum mechanically forbidden as is the transition that leads to light emission. ...
Ãâó: en.wikipedia.org/wiki/Phosphorescence
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