Purification and characterization of a specific nucleoside diphosphatase from soybean root nodules

A specific nucleoside diphosphatase was purified from the plant portion of soybean (Glycine max L.) root nodules. This enzyme is highly specific for nucleotide diphosphates; it is unable to hydrolyze nucleotide tri- and monophosphates or a variety of other phosphorylated compounds. It will, however,...

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Veröffentlicht in:Plant physiology (Bethesda) 1988-05, Vol.87 (1), p.41-45
Hauptverfasser: Doremus, H.D, Blevins, D.G
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description A specific nucleoside diphosphatase was purified from the plant portion of soybean (Glycine max L.) root nodules. This enzyme is highly specific for nucleotide diphosphates; it is unable to hydrolyze nucleotide tri- and monophosphates or a variety of other phosphorylated compounds. It will, however, hydrolyze any nucleotide disphosphate tested. The pH optimum of the enzyme is about 7.5; it requires a divalent cation for activity; and it is neither inhibited nor activated by any of the metabolites tested. It appears that in vivo this enzyme would be very active, but its function is not clear.
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This enzyme is highly specific for nucleotide diphosphates; it is unable to hydrolyze nucleotide tri- and monophosphates or a variety of other phosphorylated compounds. It will, however, hydrolyze any nucleotide disphosphate tested. The pH optimum of the enzyme is about 7.5; it requires a divalent cation for activity; and it is neither inhibited nor activated by any of the metabolites tested. It appears that in vivo this enzyme would be very active, but its function is not clear.</description><subject>Agronomy. Soil science and plant productions</subject><subject>Biological and medical sciences</subject><subject>Chromatography</subject><subject>Divalent cations</subject><subject>Economic plant physiology</subject><subject>ENZIMAS</subject><subject>ENZYME</subject><subject>ENZYMES</subject><subject>EPURATION</subject><subject>FORMATION DE NODOSITES</subject><subject>Fundamental and applied biological sciences. 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This enzyme is highly specific for nucleotide diphosphates; it is unable to hydrolyze nucleotide tri- and monophosphates or a variety of other phosphorylated compounds. It will, however, hydrolyze any nucleotide disphosphate tested. The pH optimum of the enzyme is about 7.5; it requires a divalent cation for activity; and it is neither inhibited nor activated by any of the metabolites tested. It appears that in vivo this enzyme would be very active, but its function is not clear.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>16666123</pmid><doi>10.1104/pp.87.1.41</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
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source JSTOR Archive Collection A-Z Listing; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection
subjects Agronomy. Soil science and plant productions
Biological and medical sciences
Chromatography
Divalent cations
Economic plant physiology
ENZIMAS
ENZYME
ENZYMES
EPURATION
FORMATION DE NODOSITES
Fundamental and applied biological sciences. Psychology
GLYCINE MAX
Metabolism and Enzymology
NODULACION
Nodules
NUCLEOSIDE
nucleoside-diphosphatase
NUCLEOSIDES
NUCLEOSIDOS
Nucleotides
Parasitism and symbiosis
Phosphatases
Plant physiology and development
Plants
PURIFICACION
PURIFICATION
ROOT NODULATION
Root nodules
roots
Soybeans
Symbiosis (nodules, symbiotic nitrogen fixation, mycorrhiza...)
title Purification and characterization of a specific nucleoside diphosphatase from soybean root nodules
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