Results 61 to 70 of about 945 (112)

One molecule of molybdopterin guanine dinucleotide is associated with each subunit of the heterodimeric Mo-Fe-S protein transhydroxylase of Pelobacter acidigallici as determined by SDS/RAGE and mass spectrometry

, 1996
The molybdenum-containing iron-sulfur protein 1,2,3,5-tetrahydroxybenzene:1,2,3-trihydroxyben-zene hydroxyltransferase (transhydroxylase) of Pelobacter acidigallici was investigated by various techniques including mass spectrometry and electron ...
Schink, Bernhard, Rüdiger, Angelika, Reichenbecher, Wolfram, Kroneck, Peter M. H.   +3 more
core   +1 more source

The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor

Journal of Biological Chemistry, 1993
Molybdopterin, the universal component of the pterin molybdenum cofactors, contains a dithiolene group serving to bind Mo. Addition of the dithiolene sulfurs to a molybdopterin precursor requires the activity of the converting factor. Active converting factor has been purified from Escherichia coli chlA1 cells and found to have two subunits of mass 10 ...
D M, Pitterle, K V, Rajagopalan
openaire   +2 more sources

The two subunits of human molybdopterin in synthase:evidence for a bicistronic messenger RNA with overlapping reading frames

, 1999
Molybdoenzymes are ubiquitous and require a prosthetic group called the molybdenum cofactor for activity. We provide evidence here that the two heteromeric subunits (MOCO1-A and MOCO1-B) of human molybdopterin synthase, which is involved in the ...
Sloan, J, Kinghorn, James Robertson, Unkles, Sheila Eileen   +2 more
core   +1 more source

Molybdopterin Biosynthesis: Trapping of Intermediates for the MoaA-Catalyzed Reaction Using 2′-DeoxyGTP and 2′-ChloroGTP as Substrate Analogues.

, 2015
MoaA is a radical S-adenosylmethionine (AdoMet) enzyme that catalyzes a complex rearrangement of guanosine-5'-triphosphate (GTP) in the first step of molybdopterin biosynthesis.
Tadhg P. Begley (170128), Hui Xu (9203), Sameh H. Abdelwahed (1328640), Angad P. Mehta (1328637)   +3 more
core   +1 more source

The chaperone FdsC for Rhodobacter capsulatus formate dehydrogenase binds the bis-molybdopterin guanine dinucleotide cofactor

, 2014
Molybdoenzymes are complex enzymes in which the molybdenum cofactor (Moco) is deeply buried in the enzyme. Most molybdoenzymes contain a specific chaperone for the insertion of Moco.
Leimkühler, Silke (Prof. Dr.), Boehmer, Nadine, Hartmann, Tobias   +2 more
core   +1 more source

Topological structure of Molybdopterin-binding domain in human Xanthine oxidase

, 2013
Background: Domains are the basic functional units of proteins. Information on domain- domain interaction is favorable for more detailed understanding of protein-protein interactions, cellular function and biological processes.
Rastegari, A.A.
core  

Structure of the molybdenum-cofactor biosynthesis protein MoaB ofEscherichia coli

, 2004
The moaABC operon of Escherichia coli is involved in early steps of the biosynthesis of the molybdenum-binding cofactor molybdopterin, but the precise functions of the cognate proteins are not known. The crystal structure of the MoaB protein from E. coli
Gomez-Ortiz, Mariola, Huber, Robert, Bader, Gerd, Bacher, Adelbert, Haussmann, Christoph, Fischer, Markus   +5 more
core   +1 more source

Synthesis of Adenylated Molybdopterin [PDF]

Journal of Biological Chemistry, 2004
Angel Llamas, Ralf R. Mendel, Günter Schwarz   +2 more
openaire   +1 more source

Eukaryotic Molybdopterin Synthase [PDF]

Journal of Biological Chemistry, 1999
Shiela E. Unkles, Immanuel S. Heck, M. Virginia C.L. Appleyard, James R. Kinghorn   +3 more
openaire   +1 more source

Involvement of an unusual mol operon in molybdopterin cofactor biosynthesis in Ralstonia eutropha

, 2001
In contrast to its parent strain, transposon Tn5-Mob insertion mutant HB6 of the facultative chemoautotroph Ralstonia eutropha was unable to grow organoautotrophically on formate and exhibited no activity of Mo-dependent, membrane-bound formate ...
Bowien, Botho, Burgdorf, T., Bommer, D.
core   +2 more sources