Results 61 to 70 of about 116,948 (101)

Molybdenum enzymes and molybdenum cofactor in mycobacteria

Journal of Cellular Biochemistry, 2011
When intracelluar pathogens enter the host macrophages where in addition to oxidative and antibiotic mechanisms of antimicrobial activity, nutrients are deprived. Human pathogen Mycobacterium tuberculosis is one of macrophage parasitisms, which can replicate and persist for decades in dormancy state in virulent environments.
Tingyu, Shi, Jianping, Xie
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Diagnosis of molybdenum cofactor deficiency

The Lancet, 1999
cardiac death in postmenopausal women on oestrogen replacement therapy. Lancet 1998; 352: 1965–69. 2 Simpkins JW, Green PS, Gridley KE, Singh M, de Fiebre NC, Rajakumar G. Role of estrogen replacement therapy in memory enhancement and the prevention of neuronal loss associated with Alzheimer’s disease. Am J Med 1997; 103: 19S–25S. 3 Best PJ, Berger PB,
W S, Waring, S, Maxwell
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MOLYBDENUM COFACTOR BIOSYNTHESIS AND MOLYBDENUM ENZYMES

Annual Review of Plant Biology, 2006
The molybdenum cofactor (Moco) forms the active site of all eukaryotic molybdenum (Mo) enzymes. Moco consists of molybdenum covalently bound to two sulfur atoms of a unique tricyclic pterin moiety referred to as molybdopterin. Moco is synthesized from GTP by an ancient and conserved biosynthetic pathway that can be divided into four steps involving ...
Günter, Schwarz, Ralf R, Mendel
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Ahomocysteinemia in molybdenum cofactor deficiency

Neurology, 1998
We report an infant with molybdenum cofactor deficiency (MCD) and a unique clinical presentation of hemiplegia, hypotonia, dystonia, and bilateral basal ganglia changes. Biochemistry revealed absent serum homocysteine, low concentrations of plasma cystine, high levels of urinary S-sulfocysteine and sulfite, and high levels of oxypurines in serum and ...
W D, Graf, O E, Oleinik, R M, Jack, A H, Weiss, J L, Johnson   +4 more
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Biosynthesis and Insertion of the Molybdenum Cofactor

EcoSal Plus, 2008
The transition element molybdenum (Mo) is of primordial importance for biological systems, because it is required by enzymes catalyzing key reactions in the global carbon, sulfur, and nitrogen metabolism. To gain biological activity, Mo has to be complexed by a special cofactor.
Axel, Magalon, Ralf R, Mendel
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Molybdenum cofactor biosynthesis and deficiency

Cellular and Molecular Life Sciences, 2005
The molybdenum cofactor (Moco) forms the active site of all molybdenum (Mo) enzymes, except nitrogenase. Mo enzymes catalyze important redox reactions in global metabolic cycles. Moco consists of Mo covalently bound to one or two dithiolates attached to a unique tricyclic pterin moiety commonly referred to as molybdopterin (MPT). Moco is synthesized by
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Molybdenum cofactor and human disease

Current Opinion in Chemical Biology, 2016
Four molybdenum-dependent enzymes are known in humans, each harboring a pterin-based molybdenum cofactor (Moco) in the active site. They catalyze redox reactions using water as oxygen acceptor or donator. Moco is synthesized by a conserved biosynthetic pathway. Moco deficiency results in a severe inborn error of metabolism causing often early childhood
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Human Molybdenum Cofactor Deficiency

1993
Molybdenum cofactor deficiency is an inborn error of metabolism first identified in 1980.1,2 Cofactor deficient patients exhibit combined deficiencies of three molybdoenzymes, sulfite oxidase, xanthine dehydrogenase and aldehyde oxidase, all of which depend on the presence of a tightly bound molybdenum-molybdopterin complex for catalytic activity.
J L, Johnson, K V, Rajagopalan, S K, Wadman   +2 more
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Genetics of molybdenum cofactor deficiency

Human Genetics, 2000
Molybdenum cofactor (MoCo) deficiency leads to a combined deficiency of the molybdoenzymes sulphite oxidase, xanthine dehydrogenase and aldehyde oxidase. Effective therapy is not available for this rare disease, which results in neonatal seizures and other neurological symptoms identical to those of sulphite oxidase deficiency.
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Chemistry and biology of the molybdenum cofactor

Biochemical Society Transactions, 1985
All molybdenum-containing enzymes other than nitrogenase carry out either oxidative hydroxylation or reductive dehydroxylation of their substrates as exemplified by the reactions catalyzed by sulfite oxidase and nitrate reductase respectively, shown below. The results of X-ray absorbance fine structure studies on sulfite oxidase, xanthine dehydrogenase
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