Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.

The glyoxalase system is present in the cytosol of cells and cellular organelles, particularly mitochondria. It is found throughout biological life and is thought to be ubiquitous. The widespread distribution and presence of the glyoxalase system in living organisms suggests it fulfils a function of fundamental importance to biological life. Recent investigations have brought new developments in the involvement of the glyoxalase in cell growth and vesicle mobilization, with increasing evidence of changes in the glyoxalase system during tumor growth and diabete mellitus, particularly relating to the development of associated clinical complications.

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The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life.

Glutathione, glutathione-dependent and antioxidant enzymes in mussel, Mytilus galloprovincialis, exposed to metals under field and laboratory conditions: implications for the use of biochemical biomarkers

Aldehydes are organic compounds that are widespread in nature. They can be formed endogenously by lipid peroxidation (LPO), carbohydrate or metabolism ascorbate autoxidation, amine oxidases, cytochrome P-450s, or myeloperoxidase-catalyzed metabolic activation. This review compares the reactivity of many aldehydes towards biomolecules particularly macromolecules. Furthermore, it includes not only aldehydes of environmental or occupational concerns but also dietary aldehydes and aldehydes formed endogenously by intermediary metabolism. Drugs that are aldehydes or form reactive aldehyde metabolites that cause side-effect toxicity are also included. The effects of these aldehydes on biological function, their contribution to human diseases, and the role of nucleic acid and protein carbonylation/oxidation in mutagenicity and cytotoxicity mechanisms, respectively, as well as carbonyl signal transduction and gene expression, are reviewed. Aldehyde metabolic activation and detoxication by metabolizing enzymes are also reviewed, as well as the toxicological and anticancer therapeutic effects of metabolizing enzyme inhibitors. The human health risks from clinical and animal research studies are reviewed, including aldehydes as haptens in allergenic hypersensitivity diseases, respiratory allergies, and idiosyncratic drug toxicity; the potential carcinogenic risks of the carbonyl body burden; and the toxic effects of aldehydes in liver disease, embryo toxicity/teratogenicity, diabetes/hypertension, sclerosing peritonitis, cerebral ischemia/neurodegenerative diseases, and other aging-associated diseases.

Aldehyde sources, metabolism, molecular toxicity mechanisms, and possible effects on human health.

The glyoxalase system in health and disease.

Purification and characterization of two forms of glyoxalase II from the liver and brain of Wistar rats.

1. 1. A soluble alkaline phosphatase (AP) present in the hepatopancreas of Squilla mantis was extracted. 2. 2. The enzyme was purified by acetone fractionation and then by DEAE-cellulose and Sephadex G-200 chromatography; a single AP form was obtained, which was characterized by studying molecular and catalytic properties. 3. 3. Kinetic studies were carried out using phosphoesters as inhibitors; all these substances led to competitive inhibition. The enzyme shows a higher affinity for ADP and ATP; glucose phosphoesters are weak inhibitors. 4. 4. Possible roles of the studied AP in vivo are discussed.

Characterization of the soluble alkaline phosphatase from hepatopancreas of Squilla mantis L.

Demonstration of glyoxalase II in rat liver mitochondria. Partial purification and occurrence in multiple forms.

Glyoxalase I and glyoxalase II from the outer green rind of Aloe vera leaves were purified by (matrix) affinity ligand-enzyme binding methods. The purified enzymes exhibited single protein bands on SDS-PAGE electrophoresis, with MW values of approximately 44,000 and 27,000 for glyoxalase I and glyoxalase II, respectively. The glyoxalase I is a basic protein (pI 7.8), while the glyoxalase II (3 protein bands) is acidic (pI 4.7, 4.8 [prevalent form], and 5.0). The kinetic constants, Km and Vmax, and Ki values for certain inhibitors are reported for both glyoxalase I and glyoxalase II. The glyoxalase enzymes from Aloe vera were compared with reported animal and plant glyoxalases.

Giovanni B. Principato

Papers

Purification and characterization of two forms of glyoxalase II from the liver and brain of Wistar rats.

Characterization of the soluble alkaline phosphatase from hepatopancreas of Squilla mantis L.

Demonstration of glyoxalase II in rat liver mitochondria. Partial purification and occurrence in multiple forms.

Glyoxalase I and glyoxalase II from Aloe vera: purification, characterization and comparison with animal glyoxalases.

Isolation of glyoxalase II from two different compartments of rat liver mitochondria. Kinetic and immunochemical characterization of the enzymes.