Zinc and Cobalt Alkaline Phosphatases

Simpson, Robert T.; Vallée, Bert L.

doi:10.1111/j.1749-6632.1969.tb46426.x

Cited by 24 publications

(7 citation statements)

References 30 publications

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“…Such a concept would be in accord with the known stabilizing effect of zinc on various macromolecules (Chvapil, 1973) and with its role in maintaining the conformational stability of enzymes such as alkaline phosphatase (Simpson & Vallee, 1969) and superoxide dismutase (Rotilio et al, 1972).…”

Section: Lysinementioning

confidence: 98%

The induction of metallothionein in rat liver by zinc injection and restriction of food intake

Bremner¹,

Davies²

1975

Biochemical Journal

317

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The isolation of two forms of hepatic zinc-thioneins after either zinc injection into rats or partial restriction of their food intake is described. The proteins differed slightly in their amino acid composition and electrophoretic mobilities. Increases in liver zinc content after both treatments were synchronous with, and associated almost completely with, increased zinc-binding to these proteins. The time-course for the appearance and disappearance of the zinc proteins is shown. It is suggested that metallothionein is involved in the normal metabolism of zinc, perhaps in some temporary storage or detoxication capacity.

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Section: Lysinementioning

confidence: 98%

The induction of metallothionein in rat liver by zinc injection and restriction of food intake

Bremner¹,

Davies²

1975

Biochemical Journal

317

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“…At intermediate zinc contents, two boundaries are observed. These experiments indicate that all four zinc atoms are necessary to stabilize the quaternary structure of this enzyme fully (8). The substitution of cobalt for the native zinc ions of alkaline phosphatase results in an active enzyme with distinctive optical properties, generated by the interaction of cobalt with the ligands of the protein.…”

mentioning

confidence: 95%

Structure and Function of Metalloenzymes

Ulmer

Vallée

1971

Advances in Chemistry

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In metalloenzymes, metals which affect function directly by participation in catalysis appear to have ligand sites which differ markedly from those of metals which influence function indirectly through modulation of protein structure. Thus, in both E. coli alkaline phosphatase and equine liver alcohol dehydrogenase, metals positioned at the active site interact selectively with chelating agents, undergo isotope exchange, and display distinctive physical chemical characteristics. Such active site metals may have an irregular geometry which facilitates their catalytic role. In contrast, nonactive site metals exhibit physical properties more like those of simple, bidentate model complexes; they frequently appear to stabilize structure or influence subunit interactions as shown by their effects on sedimentation or hydrogen exchange rates of proteins. Such "structural" metals may function importantly in control mechanisms for biochemical reactions.Touring the past two decades, considerable progress in understanding **** the role of metals in biological processes has resulted from the discovery and purification of a large number of metalloproteins and from efforts to ascertain their function-e.g., in catalysis, electron transport, or gas exchange (I). Studies of the physical chemical properties of this group of proteins have been of particular interest because of the presence of the inorganic moiety. In principle, metals should be excellent labels of the protein sites to which they bind owing to the distinctive physical properties of metal complexes with common ligands-e.g., color, in the case of copper, cobalt, or iron salts. Hence, one might have hoped that the basic characteristics of the metal, known from studies of inorganic complexes, would be preserved in biological systems and aid identification of the ligand groups and their properties at protein loci of special

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“…However, the metal-binding site in APase is not specific for Zn. It has been observed that Co and Cd can substitute equally well for Zn in E. coli APase (Applebury and Coleman 1968;Simpson and Vallee 1969;Gettins and Coleman 1982), following the general pattern of Co-Zn and Cd-Zn substitution seen in antagonistic metal uptake relationships in phytoplankton (Price and Morel 1990;Lee and Morel 1995). In addition to Zn-Cd-Co APase, it has also been reported that some organisms can produce a unique Co(II)requiring APase, such as the prokaryote Bacillus subtilis (Hulett et al 1991) and the hyperthermophilic bacterium Thermotoga maritime (Wojciechowski et al 2002).…”

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confidence: 99%

Differential effects of phosphorus limitation on cellular metals in Chlorella and Microcystis

Sherrell

2008

Limnology & Oceanography

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We investigated the effect of phosphate bioavailability on cellular metal quotas in two species of freshwater phytoplankton (the eukaryote Chlorella sp. UTCC522 and the cyanobacterium Microcystis sp. LE3), grown in semicontinuous culture over four controlled levels of phosphate availability, encompassing phosphorus (P) deplete to P replete conditions. P limitation caused reduced growth rate, high C : P (up to 1800 mol mol 21 ), and increased alkaline phosphatase (APase) activity. Low P availability led to enriched cobalt (Co), cadmium (Cd), and zinc (Zn) in Chlorella (up to 2.8-fold, 1.7-fold, and 1.8-fold, respectively, normalized to cellular N, relative to P-replete control) but resulted in enriched Co and nickel (Ni) in Microcystis (up to 4.4-fold and 3.0-fold). In contrast, cellular iron (Fe), manganese (Mn) and copper (Cu) were largely unchanged (6,20%) in both organisms. Cd and Co may substitute for Zn in the APase of Chlorella while in Microcystis the dominant phosphatase may be strictly Co-requiring, as has been reported for other prokaryotes and is consistent with its evolutionary emergence before the oxygenation of the atmosphere, when Co was relatively abundant in natural waters. By extension, the absolute Co requirement of the important marine cyanobacteria Synechococus and Prochlorococcus may be related in part to widespread depletion of orthophosphate (PO 3{ 4 ) in the oligotrophic surface ocean. The enrichment of Ni in Microcystis may indicate increased activity of Ni-requiring superoxide dismutase under P limitation or, speculatively, a co-uptake of Ni and Co by a shared transport system. These results shed light on the interaction between trace metals, macronutrient availability, and phytoplankton assemblage composition, and suggest intensified biological cycling of Zn, Cd, Co, and Ni in low-P freshwater and marine systems.Phosphorus (P) is an essential nutrient that all organisms require for energy transport, construction of membranes, and storage and replication of genetic information. P has been documented to limit community production in marine systems ranging from restricted seas (Krom et al. 1991;Nausch and Wasmund 2004) to the open ocean, including oligotrophic regions of the North Atlantic and the North Pacific (Cotner et al. 1997;Karl 1997;Wu et al. 2000). In addition, P is limiting in many large lakes, as most recently demonstrated for Lake Superior (Sterner et al. 2004). Low P availability has a substantial effect on the biochemistry and physiology of phytoplankton. Severe P limitation makes phytoplankton incapable of producing nucleic acids and leads to a decrease in the rate of protein synthesis, which in turn inhibits cell division and decreases rates of light utilization and carbon fixation (Cembella et al. 1984;Falkowski and Raven 1997). While these physiological effects have been well studied, the effect of P availability on trace metal uptake in phytoplankton is poorly understood. While changes in metalloenzyme activities may result from variations in P availability, th...

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Zinc and Cobalt Alkaline Phosphatases

Cited by 24 publications

References 30 publications

The induction of metallothionein in rat liver by zinc injection and restriction of food intake

The induction of metallothionein in rat liver by zinc injection and restriction of food intake

Structure and Function of Metalloenzymes

Differential effects of phosphorus limitation on cellular metals in Chlorella and Microcystis

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