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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)
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