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  • inosine phosphorylase deficiency
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  • muscle phosphorylase
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  • purine nucleoside phosphorylase
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  • polynucleotide phosphorylase
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  • polysaccharide phosphorylase
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  • starch phosphorylase
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  • synthase-phosphorylase kinase
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NP Nucleoside Phosphorylase
IP icterus praecox; imaging plate; immune precipitate; immunoblastic plasma; immunoperoxidase technique...
MTAP methylthioadenosine phosphorylase
NP nasopharynx, nasopharyngeal; near point; necrotizing pancreatitis; neonatal-perinatal; neuritic plag...
PBK phosphorylase B kinase
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GP Glycogen Phosphorylase
MTAP Methylthioadenosine phosphorylase
NP Nucleoside phosphorylase
PHK Phosphorylase kinase
PD-ECGF/TP Platelet-derived endothelial cell growth factor/thymidine phosphorylase
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CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 8 ÆäÀÌÁö: 1
phosphorylase <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase).
(21 Jun 2000)
phosphorylase a <enzyme> The phosphorylated and more active form of phosphorylase that functions as a regulatory enzyme during glycogen breakdown. The phosphate groups are hydrolytically removed by phosphorylase phosphatase to form phosphorylase b and orthophosphate.
Registry number: EC 2.4.1.-
(12 Dec 1998)
phosphorylase b <enzyme> The relatively inactive form of phosphorylase that is reactivated to form phosphorylase a by phosphorylase kinase, which catalyses the enzymatic phosphorylation of the serine residues at the expense of ATP.
Registry number: EC 2.4.1.-
(12 Dec 1998)
phosphorylase kinase <enzyme> The enzyme that regulates the activity of phosphorylase and glycogen synthetase by addition of phosphate groups. A large and complex enzyme, itself regulated by phosphorylation. Integrates the hormonal and calcium signals in muscle.
(18 Nov 1997)
phosphorylase kinase phosphatase <enzyme> Aspect of phosphoprotein phosphatase EC 3.1.3.16
Registry number: EC 3.1.3.-
(26 Jun 1999)
phosphorylase phosphatase <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form.
Chemical name: (Phosphorylase a) phosphohydrolase
Registry number: EC 3.1.3.17
(12 Dec 1998)
phosphorylase-rupturing enzyme <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form.
Chemical name: (Phosphorylase a) phosphohydrolase
Registry number: EC 3.1.3.17
(12 Dec 1998)
phosphorylases 1. General term for enzymes transferring an inorganic phosphate group to some organic acceptor, hence belonging to the transferases.
2. Specifically, enzymes that release a single glucosyl residue from a polyglucose as d-glucose 1-phosphate, the phosphate coming from inorganic orthophosphate; e.g., phosphophorylase, sucrose phosphorylases, cellobiose phosphorylases.
(05 Mar 2000)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
alpha,alpha-trehalose phosphorylase <enzyme> Chemical name: alpha-d-glucopyranosyl-alpha-d-glucopyranose orthophosphate glucosyltransferase
Registry number: EC 2.4.1.64
Synonym: trehalose phosphorylase
(26 Jun 1999)
alpha-glucan phosphorylase <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase).
(21 Jun 2000)
maltodextrin phosphorylase <enzyme> From E coli
Registry number: EC 2.4.1.-
Synonym: e350a
(26 Jun 1999)
GDPmannose phosphorylase <enzyme> A transferase that catalyses the transfer of GDP to the mannose of mannose-1-phosphate.
Consider also the bifunctional enzyme, phosphomannose isomerase-guanosine diphospho-d-mannose pyrophosphorylase; rfbm has similarity to long-chain, iron-containing alcohol dehydrogenases
Registry number: EC 2.7.7.13
Synonym: GDPmannose phosphorylase, GDP mannose pyrophosphorylase, GTP-alpha-d-mannose-1-phosphate guanylyltransferase, GDP-mannose pyrophosphorylase, rfbm gene product, rfbm protein
(26 Jun 1999)
cellodextrin phosphorylase <enzyme> Reverse reaction is used to synthesise cellodextrins
Registry number: EC 2.4.1.49
(26 Jun 1999)
glycogen phosphorylase <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase).
(21 Jun 2000)
muscle phosphorylase deficiency Type V glycogen storage disease, affecting muscle, caused by deficiency of muscle phosphorylase.
(05 Mar 2000)
polynucleotide phosphorylase <enzyme> An enzyme of the transferase class that catalyses the reaction RNA(n+1) and orthophosphate to yield RNA(n) and a nucleoside diphosphate, or the reverse reaction. ADP, idp, GDP, udp, and cdp can act as donors in the latter case.
Chemical name: Polyribonucleotide:orthophosphate nucleotidyltransferase
Registry number: EC 2.7.7.8
(12 Dec 1998)
xanthosine phosphorylase <enzyme> From E coli k-12; mw 18kda; inactivated by p-chloromercuriphenylsulfonic acid
Registry number: EC 2.4.2.-
Synonym: inosine-guanosine phosphorylase
(26 Jun 1999)
purine-nucleoside phosphorylase <enzyme> An enzyme that catalyses the reaction between a purine nucleoside and orthophosphate to form a free purine plus ribose-5-phosphate.
Chemical name: Purine-nucleoside:orthophosphate ribosyltransferase
Registry number: EC 2.4.2.1
(12 Dec 1998)
pyrimidine-nucleoside phosphorylase <enzyme> Consider uridine phosphorylase and thymidine phosphorylase
Registry number: EC 2.4.2.2
Synonym: pyrimidine nucleoside phosphorylase
(26 Jun 1999)
nucleoside phosphorylase <enzyme> From klebsiella sp.; acts on both purine and pyrimidine nucleosides and catalyses the production of araa from uridine arabinoside (arau) and adenine
Registry number: EC 2.4.2.-
(26 Jun 1999)
diadenosine 5,5'''-P(1),P(4)-tetraphosphate alpha,beta-phosphorylase <enzyme> Ap4a + inorganic po4 forms ATP + ADP
Registry number: EC 2.7.7.53
Synonym: ap4a phosphorylase, ATP adenylyltransferase
(26 Jun 1999)
orotidylic acid phosphorylase <enzyme> The enzyme catalyzing the formation of orotidine-5'-phosphoric acid (orotidylic acid) from orotic acid and 5-phosphoribosyl-1-pyrophosphate in the course of pyrimidine nucleotide biosynthesis.
Chemical name: Orotidine-5'-phosphate:pyrophosphate phospho-alpha-D-ribosyltransferase
Registry number: EC 2.4.2.10
(12 Dec 1998)
thymidine phosphorylase <enzyme> The enzyme catalyzing the transfer of 2-deoxy-d-ribose from thymidine to orthophosphate, thereby liberating thymidine.
Chemical name: Thymidine:orthophosphate deoxy-D-ribosyltransferase
Registry number: EC 2.4.2.4
(12 Dec 1998)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 5 ÆäÀÌÁö: 1
  • Phosphorylase a - »õâ The active form of GLYCOGEN PHOSPHORYLASE that is derived from the phosphorylation of PHOSPHORYLASE B. Phosphorylase a is deactivated via hydrolysis of phosphoserine by PHOSPHORYLASE PHOSPHATASE to form PHOSPHORYLASE B.
    Synonyms :
  • Phosphorylase b - »õâ The inactive form of GLYCOGEN PHOSPHORYLASE that is converted to the active form PHOSPHORYLASE A via phosphorylation by PHOSPHORYLASE KINASE and ATP.
    Synonyms :
  • Phosphorylase Kinase - »õâ An enzyme that catalyzes the conversion of ATP and phosphorylase b to ADP and phosphorylase a. EC 2.7.1.38.
    Synonyms : Glycogen Phosphorylase Kinase, Phosphorylase b Kinase, Kinase, Glycogen Phosphorylase, Kinase, Phosphorylase, Kinase, Phosphorylase b, Phosphorylase Kinase, Glycogen, b Kinase, Phosphorylase
  • Phosphorylase Phosphatase - »õâ An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. EC 3.1.3.17.
    Synonyms : Glycogen Phosphorylase Phosphatase, Phosphatase, Glycogen Phosphorylase, Phosphatase, Phosphorylase, Phosphorylase Phosphatase, Glycogen
  • Phosphorylases - »õâ A class of glucosyltransferases that catalyzes the degradation of storage polysaccharides, such as glucose polymers, by phosphorolysis in animals (GLYCOGEN PHOSPHORYLASE) and in plants (STARCH PHOSPHORYLASE).
    Synonyms : alpha-Glucan Phosphorylases
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phosphorylase b kinase deficiency glycogen storage disease A form of glycogen storage disease caused by an x-linked deficiency of the kinase that activates phosphorylase. Previously called type VIa, VIII, or IX.
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phosphorylase 1. any of a group of enzymes catalyzing phosphorolysis of glycosides, transferring the cleaved glycosyl group to inorganic phosphate. The term is usually qualified by adding the name of the substrate acted upon; when used alone it usually denotes glycogen phosphorylase (q.v.) in animals or starch phosphorylase in plants.  2. any of a group of transferases that catalyze the transfer of a phosphate group to an organic acceptor.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
phosphorylase b phosphorylase kinase.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
phosphorylase kinase [EC 2.7.1.38] an enzyme of the transferase class that catalyzes the phosphorylation of (inactive) glycogen phosphorylase b to form (active) glycogen phosphorylase a, a step in the cascade of reactions regulating glycogenolysis. The enzyme is itself activated via phosphorylation by cyclic-AMP–dependent protein kinase, and one of its four subunits is identical to calmodulin. Deficiency of the enzyme in liver, an X-linked trait, causes phosphorylase b kinase deficiency.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
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