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Design and Synthesis of Different Pterin Derivatives - Enroute to Molybdopterin Mimics [PDF]
The dissertation presents an in-depth exploration into the synthesis of pterin-based compounds, with a particular focus on developing analogs of molybdopterin.
Correia, Jevy Vincent (PhD)
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The Mechanism of Nucleotide-assisted Molybdenum Insertion into Molybdopterin [PDF]
Journal of Biological Chemistry, 2006 Angel Llamas +4 more
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Archives of Biochemistry and Biophysics, 1990
The pterin cofactor (bactopterin) in the molybdoenzyme CO dehydrogenase isolated from Pseudomonas carboxydoflava has previously been shown to differ from molybdopterin in molecular mass, phosphate content, stability, and other properties, implying a novel structure.
J L, Johnson, K V, Rajagopalan, O, Meyer
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The pterin cofactor (bactopterin) in the molybdoenzyme CO dehydrogenase isolated from Pseudomonas carboxydoflava has previously been shown to differ from molybdopterin in molecular mass, phosphate content, stability, and other properties, implying a novel structure.
J L, Johnson, K V, Rajagopalan, O, Meyer
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Molybdopterin Radical in Bacterial Aldehyde Dehydrogenases
Biochemistry, 1998The EPR spectra of three different molybdoprotein aldehyde dehydrogenases, one purified from Comamonas testosteroni and two purified from Amycolatopsis methanolica, showed in their oxidized state a novel type of signal. These three enzymes contain two different [2Fe-2S] centers, one flavin and one molybdopterin cytosine dinucleotide, as cofactors all ...
D M, Luykx, J A, Duine, S, de Vries
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A molybdopterin-free form of xanthine oxidase
Archives of Biochemistry and Biophysics, 1987A previously unidentified fraction lacking xanthine:O2 activity has been isolated during affinity chromatography of bovine milk xanthine oxidase preparations on Sepharose 4B/folate gel. Unlike active, desulfo, or demolybdo forms of xanthine oxidase, this form, which typically comprises about 5% of an unfractionated enzyme solution, passes through the ...
S, Gardlik +2 more
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Studies on the oxidation state of molybdopterin
Polyhedron, 1986Abstract Molybdopterin, the organic component of the molybdenum cofactor common to all molybdenum-containing enzymes except nitrogenase, is proposed to contain two vicinal thiols capable of complexing Mo. The pterin ring is in an unknown state of reduction in the active cofactor.
K.V. Rajagopalan +2 more
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Molybdopterin from molybdenum and tungsten enzymes
2001Publisher Summary This chapter focuses on the structural data describing molybdenum cofactor (Moco)-containing enzymes and discusses their respective catalytic mechanisms. The crystal structures of Moco-containing enzymes have revealed a remarkable degree of structural diversity in the overall polypeptide folds, as well as in the composition and ...
H, Schindelin +2 more
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Specific Incorporation of Molybdopterin in Xanthine Dehydrogenase of Pseudomonas aeruginosa
Archives of Biochemistry and Biophysics, 1994All known molybdoenzymes other than nitrogenase contain the metal in association with molybdopterin or one of its dinucleotide variants. All eukaryotic molybdoproteins have been found to contain only molybdopterin, whereas the majority of bacterial enzymes contain one or another of the dinucleotides of molybdopterin. In contrast, xanthine dehydrogenase
M S, Joshi, K V, Rajagopalan
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Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency
American Journal of Medical Genetics, Part A, 2001Molybdenum cofactor deficiency is a rare inborn error of metabolism with generally severe symptoms, most often including neonatal seizures and severe developmental delay. We describe a patient with an unusually mild form of the disease. Two mutations in MOCS2A (molybdenum cofactor synthesis enzyme 2A) were identified: a single base change, 16C > T ...
Mark T Mackay +2 more
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The relationship of Mo, molybdopterin, and the cyanolyzable sulfur in the Mo cofactor
Archives of Biochemistry and Biophysics, 1984Reconstitution of the apoprotein of the molybdoenzyme nitrate reductase in extracts of the Neurospora crassa mutant nit-1 with molybdenum cofactor released by denaturation of purified molybdoenzymes is efficient in the absence of exogenous MoO2-4 under defined conditions.
R C, Wahl +2 more
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