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cellodextrin phosphorylase <enzyme> Reverse reaction is used to synthesise cellodextrins
Registry number: EC 2.4.1.49
(26 Jun 1999)
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)
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)
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)
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)
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