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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
1992-6-29
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pubmed:abstractText |
1. Alkaline p-nitrophenylphosphate phosphatase (pNPPase) activity of Halobacterium halobium is selectively stabilized and stimulated by Mn2+ ions. 2. Mn2+ binding to native pNPPase is characterized by a dissociation constant of 0.35 mM at pH 8.5, 37 degrees C, with a Hill coefficient of 0.988. 3. Mn2+ behaves as a mixed type nonessential activator, increasing the Vmax value (beta = 6.09, pH 8.5) and decreasing the Km value for pNPP (alpha = 0.56, pH 8.5). The Ki value for inorganic phosphate (a competitive inhibitor) was also decreased in the presence of Mn2+. 4. Activation of native pNPPase by preincubation with Mn2+ is a slow temperature-dependent process, which can be described by an exponential relationship vs time. However, a weak but immediate activation was also detected. 5. Zn2+, Cu2+ and Ni2+ were found to inhibit both native and Mn(2+)-stimulated pNPPase, whereas Co2+ and Cd2+ inhibited the Mn(2+)-stimulated pNPPase but had no effect on the native enzyme form.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
May
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pubmed:issn |
0020-711X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
24
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
839-45
|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1317306-4-Nitrophenylphosphatase,
pubmed-meshheading:1317306-Cations, Divalent,
pubmed-meshheading:1317306-Enzyme Activation,
pubmed-meshheading:1317306-Enzyme Stability,
pubmed-meshheading:1317306-Halobacterium salinarum,
pubmed-meshheading:1317306-Kinetics,
pubmed-meshheading:1317306-Manganese
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pubmed:year |
1992
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pubmed:articleTitle |
Alkaline p-nitrophenylphosphate phosphatase activity from Halobacterium halobium. Selective activation by manganese and effect of other divalent cations.
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pubmed:affiliation |
División de Bioquímica, Facultad de Ciencias, Universidad de Alicante, Spain.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|