| 5 alpha-dihydroprogesterone 3 alpha-hydroxysteroid oxidoreductase | <enzyme> Catalyses conversion of 5 alpha-dihydroprogesterone to 3 alpha -hydroxy-5 alpha-pregnane-20-one Registry number: EC 1.1.1.- Synonym: 5-dp-3 alpha-hso, NADPH-5 alpha-dihydroprogesterone 3 alpha-hydroxysteroid oxidoreductase, alpha-hsor (26 Jun 1999) |
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| 5 beta-cholestane-3 alpha,7 alpha-diol 26-hydroxylase | <enzyme> Nadp-dependent Registry number: EC 1.14.13.- (26 Jun 1999) |
| 7 alpha-hydroxy-4-cholesten-3-one-12 alpha monooxygenase | <enzyme> Liver microsomal enzyme active in conversion of cholesterol to cholic acid; introduces a 12 alpha-hydroxyl group into the steroid nucleus of cholesterol Registry number: EC 1.14.99.- Synonym: 7-hco-monooxygenase, hco 12 alpha-hydroxylase (26 Jun 1999) |
| 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) |
| 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) |