| NDPKA | nucleoside diphosphate kinase A |
|---|---|
| NDPKB | nucleoside diphosphate kinase B |
| NMP | normal menstrual period; nucleoside monophosphate |
| NPR | net protein ratio; normal pulse rate; nucleoside phosphoribosyl |
| NTP | National Toxicology Program; nitroprusside; normal temperature and pressure; nucleoside triphosphate... |
| nucleoside-monophosphate | A nucleotide, e.g., AMP. (05 Mar 2000) |
|---|---|
| nucleoside-phosphate kinase | <enzyme> An enzyme that catalyses reversible reactions of a nucleoside triphosphate, e.g., ATP, with a nucleoside monophosphate, e.g., ump, to form ADP and udp. Many nucleoside monophosphates can act as acceptor while many ribo- and deoxyribonucleoside triphosphates can act as donor. Chemical name: ATP:nucleoside-phosphate phosphotransferase Registry number: EC 2.7.4.4 (12 Dec 1998) |
| nucleoside q | <chemical> (1s-(1 alpha,4 beta,5 beta))-2-amino-5-(((4,5-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-1,7-dihydro-7-beta-d-ribofuranosyl-4h-pyrrolo(2,3-d)pyrimidin-4-one. A modified nucleoside which is present in the first position of the anticodon of trna-tyrosine, trna-histidine, trna-asparagine and trna-aspartic acid of many organisms. It is believed to play a role in the regulatory function of trna. Nucleoside q can be further modified to nucleoside q*, which has a mannose or galactose moiety linked to position 4 of its cyclopentenediol moiety. Chemical name: 4H-Pyrrolo(2,3-d)pyrimidin-4-one, 2-amino-5-(((4,5-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-1,7-dihydro-7-beta-D-ribofuranosyl-, (1S-(1alpha,4beta,5beta))- (12 Dec 1998) |
| nucleoside-triphosphatase | <enzyme> Hydrolyzes various nucleotides to a nucleotide diphosphate + pi; inhibited by ca + ATP Registry number: EC 3.6.1.15 Synonym: nucleoside triphosphate phosphohydrolase, nucleoside triphosphatase, ntpase, nuclear envelope nucleoside triphosphatase, nuclear scaffold nucleoside triphosphatase, ns ntpase, nucleosidetriphosphatase (26 Jun 1999) |
| nucleoside triphosphate | A nucleoside in which the H of one of the ribose hydroxyls (usually the 5') is replaced by a triphosphoric group, -PO(OH)-O-PO(OH)-O-PO(OH)2; e.g., adenosine triphosphate. (05 Mar 2000) |
| nucleoside triphosphate-adenylate kinase | <enzyme> Other nucleoside triphosphates may replace GTP as substrate Registry number: EC 2.7.4.10 Synonym: GTP-AMP phosphotransferase, AMP-GTP phosphotransferase (26 Jun 1999) |
| 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) |
| 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) |