Results 81 to 90 of about 120,575 (162)

Mouse model for molybdenum cofactor deficiency type B recapitulates the phenotype observed in molybdenum cofactor deficient patients

open access: yes, 2016
Molybdenum cofactor (MoCo) deficiency is a rare, autosomal-recessive disorder, mainly caused by mutations in MOCS1 (MoCo deficiency type A) or MOCS2 (MoCo deficiency type B) genes; the absence of active MoCo results in a deficiency in all MoCo-dependent ...
Metz, Imke   +9 more
core   +1 more source

Method for assessing the content of molybdenum enzymes in the internal organs of fish

open access: yesMethodsX
Molybdenum enzymes (Mo-enzymes) contain a molybdenum cofactor (MoCo) in the active site. These enzymes are potentially interesting for studying the survival mechanism of fish under hypoxic water conditions.
Mereke Satkanov   +8 more
doaj   +1 more source

A novel role for Arabidopsis mitochondrial ABC transporter ATM3 in molybdenum cofactor biosynthesis [PDF]

open access: yes, 2010
The molybdenum cofactor (Moco) is a prosthetic group required by a number of enzymes, such as nitrate reductase, sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase.
Schulze, Jutta   +17 more
core   +1 more source

Campylobacter jejuni Periplasmic Nitrate Reductase NapA as a Medium for Elucidating Molybdenum Cofactor Reactivity

open access: yes
IUIPeriplasmic nitrate reductase NapA is found within many gram-negative bacteria and catalyzes oxygen atom transfer reactions. NapA utilizes nitrate as a terminal electron acceptor in place of oxygen in low-air conditions, such as in the human ...
Metzger, Mikayla
core   +2 more sources

Synthesis of Cyclic Pyranopterin Monophosphate, a Biosynthetic Intermediate in the Molybdenum Cofactor Pathway

open access: yes, 2016
Cyclic pyranopterin monophosphate (1), isolated from bacterial culture, has previously been shown to be effective in restoring normal function of molybdenum enzymes in molybdenum cofactor (MoCo)-deficient mice and human patients.
Abdel A. Belaidi (1987222)   +10 more
core   +2 more sources

The mammalian aldehyde oxidase gene family

open access: yesHuman Genomics, 2009
Aldehyde oxidases (EC 1.2.3.1) are a small group of structurally conserved cytosolic proteins represented in both the animal and plant kingdoms. In vertebrates, aldehyde oxidases constitute the small sub-family of molybdo-flavoenzymes, along with the ...
Garattini Enrico   +2 more
doaj   +1 more source

Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism

open access: yesFrontiers in Physiology, 2018
Iron sulfur (Fe-S) clusters and the molybdenum cofactor (Moco) are present at enzyme sites, where the active metal facilitates electron transfer. Such enzyme systems are soluble in the mitochondrial matrix, cytosol and nucleus, or embedded in the inner ...
Zvonimir Marelja   +2 more
doaj   +1 more source

The Molybdenum Cofactor Biosynthesis Network: In vivo Protein-Protein Interactions of an Actin Associated Multi-Protein Complex [PDF]

open access: yes, 2017
Survival of plants and nearly all organisms depends on the pterin based molybdenum cofactor (Moco) as well as its effective biosynthesis and insertion into apo-enzymes.
Meinen, Rieke   +9 more
core   +1 more source

Tungsten Toxicity in Plants

open access: yesPlants, 2012
Tungsten (W) is a rare heavy metal, widely used in a range of industrial, military and household applications due to its unique physical properties.
Ioannis-Dimosthenis S. Adamakis   +2 more
doaj   +1 more source

The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans.

open access: yesPLoS ONE, 2013
In humans, the L-cysteine desulfurase NFS1 plays a crucial role in the mitochondrial iron-sulfur cluster biosynthesis and in the thiomodification of mitochondrial and cytosolic tRNAs. We have previously demonstrated that purified NFS1 is able to transfer
Zvonimir Marelja   +6 more
doaj   +1 more source

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