Oxidases glycerophosphate oxidase

DHAP can be prepared by oxidation of L-glycerol-3-phosphate (L- G3P) catalyzed by glycerophosphate oxidase, coupled with hydrogen peroxide decomposition in the presence of catalase (Scheme 4.5) [14]. More recently, this synthetic route has... 

Scheme 4.5 Enzymatic routes to DHAP based in the use of glycerophosphate oxidase (GPO) coupled with the aldolase-catalyzed reaction and with dephosphorylation of the aldol adduct.

Muller M (1975) Biochemistry of protozoan microbodies peroxisomes, alpha-glycerophosphate oxidase bodies, hydrogenosomes. Annu Rev Microbiol 29 467-483 Muller M (2003) Energy metabolism. Part I Anaerobic protozoa. In Marr JJ, Nilsen TW, Komnuniecki RW (eds) Molecular Medical Parasitology. Academic Press, New York, pp 125-139... 

Evidence for the existence of an a-glycerophosphate oxidase system with three phosphorylation sites and sensitive to rotenone and piericidin A. FEBS Letters, 10 109-12. 

Recently a variation of the above described approach was introduced. Rac-gly-cidol was treated with disodiumhydrogenphosphate and then oxidized by catalase and L-glycerophosphate oxidase to DHAP. These two steps were integrated with a RAMA-catalyzed step, yielding the phosphorylated aldol product. After adjusting the pH, phosphatase was added and the aldol could be isolated in good yield (Scheme 5.28) [48]. It can be assumed that all the above-mentioned... 

Reagent layer Buffer, pH 7.0 ADP, glycerol, peroxidase Magnesium acetate Diadenosine pentaphosphate Glycerol kinase Leuco dye Glycerophosphate oxidase... 

Glycerol kinase ATP, MgClj, diacetinase L-0- glycerophosphate oxidase... 

In the most commonly used methods, glycerophosphate is oxidized to dihydroxyacetone and H2O2 in a glycerophosphate oxidase-catalyzed reaction,... 

The FAD-requiring enzymes in mammalian systems include the D- and L-amino acid oxidases, mono- and diamine oxidases, glucose oxidase, succinate dehydrogenase, a-glycerophosphate dehydrogenase, and glutathione reductase. FMN is a cofactor for renal L-amino acid oxidase, NADH reductase, and a-hydroxy acid oxidase. In succinate dehydrogenase, FAD is linked to a histidyl residue in liver mitochondrial monoamine oxidase, to a cysteinyl residue. In other cases, the attachment is nonco-valent but the dissociation constant is very low. 

Bayne, R. A., Muse, K. E. and Roberts, J. F. (1969) Isolation of bodies containing the cyanide insensitive glycerophosphate oxidase of Trypanosoma equiperdum. Comp. Biochem. Physiol. 30 1049-1054. 

Iron deficiency is the most common nutritional cause of anemia in humans. It can result from inadequate iron intake, malabsorption, blood loss, or an increased requirement, as with pregnancy. When severe, it results in a characteristic microcytic, hypochromic anemia. Iron is an essential component of myoglobin heme enzymes such as the cytochromes, catalase, and peroxidase and the metalloflavoprotein enzymes, including xanthine oxidase and the mitochondrial enzyme a-glycerophosphate oxidase. Iron deficiency can affect metabohsm in muscle independent of the effect of anemia on delivery, possibly due to a reduction in the activity of iron-dependent mitochondrial enzymes. Iron deficiency also has been associated with behavioral and learning problems in children, abnormahties in catecholamine metabolism, and impaired heat production. 

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