Mechanism of Metal Ion Activation of Enzymes

Malmström, Bo G.; Rosenberg, Andreas

doi:10.1002/9780470122662.ch3

Cited by 5 publications

(4 citation statements)

References 105 publications

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“…Zn 2þ and Cu 2þ also inhibited the activity of cell-bound serine proteinase from various lactic acid bacteria (Naes et al, 1991;Shahbal et al, 1993;Tan, Pos, & Koning, 1991). This was because these ions can interact with histidine at the active site of serine proteinase (Fernández, Mohedano, Polanco, Medina, & Nuñez, 1996;Malmström & Rosenderg, 1960).…”

Section: Effect Of Inhibitors and Ions On Proteinases Activitymentioning

confidence: 98%

Characterization of Ca2+-activated cell-bound proteinase from Virgibacillus sp. SK37 isolated from fish sauce fermentation

Sinsuwan

Rodtong

Yongsawatdigul

2008

LWT - Food Science and Technology

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Section: Effect Of Inhibitors and Ions On Proteinases Activitymentioning

confidence: 98%

Characterization of Ca2+-activated cell-bound proteinase from Virgibacillus sp. SK37 isolated from fish sauce fermentation

Sinsuwan

Rodtong

Yongsawatdigul

2008

LWT - Food Science and Technology

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“…3, 4 Manganese-activated enzymes do not contain tightly bound Mn ions, and often contain no Mn whatsoever when they are isolated. The activity of these enzymes is dependent on the amount of free Mn II in solution, with Mn II dissociation constants typically in the µM to mM range.…”

Section: Introductionmentioning

confidence: 99%

Manganese Proteins with Mono‐ & Dinuclear Sites

Penner‐Hahn

2005

Encyclopedia of Inorganic Chemistry

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Although manganese is not as widely recognized as iron and copper, it nevertheless plays an essential role in several key biological processes. Consequently, manganese concentrations are tightly regulated in most cells. Several Mn‐specific transporters have been identified and a novel Mn‐regulatory protein has been characterized. Manganese‐activated enzymes are proteins that have relatively weak affinities for Mn; in many cases these are isolated without any metal bound. Manganese‐activated enzymes are especially important in hydrolytic reactions, and appear, in at least some cases, to have physiologically significant changes in activity that respond to changes in Mn concentration. The best characterized Mn proteins are redox‐active enzymes, where Mn typically cycles between the Mn II and Mn III oxidation states, although some Mn IV ‐containing species are known.

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“…Manganese is an essential trace metal for plant and animal metabolism. For example, manganese plays an important role in the accumulation of nitrate and carbon dioxide assimilation in plants, and activates a number of enzymatic systems in different animal species (Malmstron & Rosenberg 1959). High concentrations of manganese have been measured in the soft tissues of freshwater mussels since the beginning of the 20 th century (Bradley 1970a;1970b).…”

Section: Introductionmentioning

confidence: 99%

Relationship between anti-oxidant capacity and manganese accumulation in the soft tissues of two freshwater molluscs: Unio pictorum mancus (Lamellibranchia, Unionidae) and Viviparus ater (Gastropoda, Prosobranchia)

Campanella¹,

Gatta²,

Ravera³

2005

J Limnol

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Manganese is an element of great importance in the life cycle of plants and animals. For example, it plays an essential role as an activator of various enzymatic systems such as isoenzymes of superoxide dismutase. Freshwater Unionidae concentrate relatively large amounts of manganese in their tissues, but little is known about the physiological role of this metal. The aim of this research is to acquire a better knowledge of the role of manganese in molluscs which accumulate large amounts of this metal and in those with low manganese concentrations. As manganese is one of the metals present in the superoxide molecule, the possible relationship between manganese concentration in the soft tissues of molluscs and the antioxidant capacity of the metal can usefully be tested. To this end two species of molluscs were analysed: Unio pictorum mancus (Lamellibranchia, Unionidae), which is very rich in manganese, and Viviparus ater (Gastropoda, Prosobranchia) which has a low manganese content. The adults of both species were analysed for manganese concentration by ICP, and for antioxidant capacity as RAC (Relative Antioxidant Capacity) by a superoxide dismutase method. The results clearly demonstrate the active role played by manganese against free radicals and consequently the important role of the metal in protecting Unio against oxidative stress. The low concentration of manganese in Viviparus may be the result of the effective excretion of this metal, as was found for ruthenium

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Mechanism of Metal Ion Activation of Enzymes

Cited by 5 publications

References 105 publications

Characterization of Ca2+-activated cell-bound proteinase from Virgibacillus sp. SK37 isolated from fish sauce fermentation

Characterization of Ca2+-activated cell-bound proteinase from Virgibacillus sp. SK37 isolated from fish sauce fermentation

Manganese Proteins with Mono‐ & Dinuclear Sites

Relationship between anti-oxidant capacity and manganese accumulation in the soft tissues of two freshwater molluscs: Unio pictorum mancus (Lamellibranchia, Unionidae) and Viviparus ater (Gastropoda, Prosobranchia)

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