Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The nature of molybdenum cofactor in the bacterial enzyme dimethyl sulfoxide reductase has been investigated by application of alkylation conditions that convert the molybdenum cofactor in chicken liver sulfite oxidase and milk xanthine oxidase to the stable, well-characterized derivative [di(carboxamidomethyl)]molybdopterin. The alkylated pterin obtained from dimethyl sulfoxide reductase was shown to be a modified form of alkylated molybdopterin with increased absorption in the 250-nm region of the spectrum and altered chromatographic behavior. The complex alkylated pterin was resolved into two components by treatment with nucleotide pyrophosphatase. These were identified as di(carboxamidomethyl)molybdopterin and GMP by their absorption spectra, coelution with standard compounds, and by further degradation by alkaline phosphatase to dephospho [di(carboxamidomethyl)]molybdopterin and guanosine. The GMP moiety was sensitive to periodate, identifying it as the 5' isomer. Chemical analysis of the intact alkylated pterin showed the presence of two phosphate residues per pterin. These results established that the pterin isolated from dimethyl sulfoxide reductase contains the phosphoric anhydride of molybdopterin and 5'-GMP, which is designated molybdopterin guanine dinucleotide.
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PMID:Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans. 232 78

The molybdenum cofactor common to a variety of molybdoenzymes has been shown to contain a novel pterin. The pterin has been isolated from sulfite oxidase from several sources, xanthine-oxidizing enzymes from milk and chicken liver, and nitrate reductase of Chlorella vulgaris after denaturation of the proteins in the presence of I2. Investigation of the anionic nature of the isolated pterin has revealed that it is a monophosphate ester susceptible to cleavage by alkaline phosphatase. Quantitative analyses have shown that one molecule of the pterin phosphate is associated with each molybdenum atom in sulfite oxidase. Studies to date have shown that the pterin is present in a reduced form in sulfite oxidase and xanthine dehydrogenase, and that in situ oxidation of the pterin leads to inactivation of sulfite oxidase.
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PMID:The pterin of the molybdenum cofactor. 695 16

The molybdenum cofactor isolated from sulfite oxidase (sulfite: ferricytochrome c oxidoreductase, EC 1.8.2.1) and xanthine dehydrogenase (xanthine:NAD+ oxidoreductase, EC 1.2.1.37) in the presence of iodine and KI (form A) has been shown to contain a pterin nucleus with an unidentified substituent in the 6 position [Johnson, J. L., Hainline, B. E. & Rajagopalan, K. V. (1980) J. Biol. Chem. 255, 1783-1786]. A second inactive form of the cofactor was isolated aerobically but in the absence of iodine and KI. The latter cofactor derivative (form B) is highly fluorescent, has a visible absorption band at 395 nm and, like form A, contains a phosphate group. Cleavage of the phosphate ester bond with alkaline phosphatase exposes a glycol function that is sensitive to periodate. Oxidation of form B with alkaline permanganate yields a highly polar compound with properties of a sulfonic acid, suggesting that the active molybdenum cofactor might contain sulfur. The sulfur-containing pterin urothione characterized by Goto et al. [Goto, M., Sakurai, A., Ohta, K. & Yamakami, H. (1969) J. Biochem. 65, 611-620] had been isolated from human urine. The permanganate oxidation product of urothione, characterized by Goto et al. as pterin-6-carboxylic-7-sulfonic acid, is identical to that obtained from form B. Because urothione also contains a periodate-sensitive glycol substituent, a structural relationship is suggested. The finding that urine samples from patients deficient in the molybdenum cofactor are devoid of urothione demonstrates a metabolic link between the two molecules.
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PMID:Structural and metabolic relationship between the molybdenum cofactor and urothione. 696 Mar 53