scholarly journals Lessons From the Studies of a C C Bond Forming Radical SAM Enzyme in Molybdenum Cofactor Biosynthesis

2018 ◽  
pp. 485-522 ◽  
Author(s):  
Haoran Pang ◽  
Kenichi Yokoyama
Keyword(s):  
Molybdenum Cofactor ◽  
Radical Sam ◽  
Bond Forming ◽  
Cofactor Biosynthesis ◽  
Radical Sam Enzyme ◽  
Molybdenum Cofactor Biosynthesis

scholarly journals In VivoInteractions between Gene Products Involved in the Final Stages of Molybdenum Cofactor Biosynthesis inEscherichia coli

2002 ◽  
Vol 277 (50) ◽  
pp. 48199-48204 ◽  
Author(s):  
Axel Magalon ◽  
Chantal Frixon ◽  
Jeanine Pommier ◽  
Gérard Giordano ◽  
Francis Blasco
Keyword(s):  
Molybdenum Cofactor ◽  
Gene Products ◽  
Inescherichia Coli ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis

The molybdenum cofactor biosynthesis complex interacts with actin filaments via molybdenum insertase Cnx1 as anchor protein in Arabidopsis thaliana

Plant Science ◽  
2016 ◽  
Vol 244 ◽  
pp. 8-18 ◽  
Author(s):  
David Kaufholdt ◽  
Christin-Kirsty Baillie ◽  
Rolf Bikker ◽  
Valentin Burkart ◽  
Christian-Alexander Dudek ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Actin Filaments ◽  
Molybdenum Cofactor ◽  
Anchor Protein ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis

scholarly journals Dedicated Metallochaperone Connects Apoenzyme and Molybdenum Cofactor Biosynthesis Components

2008 ◽  
Vol 283 (31) ◽  
pp. 21433-21440 ◽  
Author(s):  
Olivier Genest ◽  
Meina Neumann ◽  
Farida Seduk ◽  
Walter Stöcklein ◽  
Vincent Méjean ◽  
...  
Keyword(s):  
Molybdenum Cofactor ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis

scholarly journals The maizeViviparous10/Viviparous13locus encodes theCnx1gene required for molybdenum cofactor biosynthesis

2006 ◽  
Vol 45 (2) ◽  
pp. 250-263 ◽  
Author(s):  
Timothy G. Porch ◽  
Chi-Wah Tseung ◽  
Eric A. Schmelz ◽  
A. Mark Settles
Keyword(s):  
Molybdenum Cofactor ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis

scholarly journals The L-Cysteine Desulfurase NFS1 Is Localized in the Cytosol where it Provides the Sulfur for Molybdenum Cofactor Biosynthesis in Humans

PLoS ONE ◽  
2013 ◽  
Vol 8 (4) ◽  
pp. e60869 ◽  
Author(s):  
Zvonimir Marelja ◽  
Mita Mullick Chowdhury ◽  
Carsten Dosche ◽  
Carsten Hille ◽  
Otto Baumann ◽  
...  
Keyword(s):  
Molybdenum Cofactor ◽  
Cysteine Desulfurase ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis

Structure of the molybdenum-cofactor biosynthesis protein MoaB ofEscherichia coli

2004 ◽  
Vol 60 (6) ◽  
pp. 1068-1075 ◽  
Author(s):  
Gerd Bader ◽  
Mariola Gomez-Ortiz ◽  
Christoph Haussmann ◽  
Adelbert Bacher ◽  
Robert Huber ◽  
...  
Keyword(s):  
Molybdenum Cofactor ◽  
Ofescherichia Coli ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis

scholarly journals Mechanism of pyranopterin ring formation in molybdenum cofactor biosynthesis

2015 ◽  
Vol 112 (20) ◽  
pp. 6347-6352 ◽  
Author(s):  
Bradley M. Hover ◽  
Nam K. Tonthat ◽  
Maria A. Schumacher ◽  
Kenichi Yokoyama
Keyword(s):  
Active Site ◽  
Biochemical Characterization ◽  
De Novo ◽  
Specific Binding ◽  
Molybdenum Cofactor ◽  
Enzyme Active Site ◽  
Complex Rearrangement ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis

The molybdenum cofactor (Moco) is essential for all kingdoms of life, plays central roles in various biological processes, and must be biosynthesized de novo. During Moco biosynthesis, the characteristic pyranopterin ring is constructed by a complex rearrangement of guanosine 5′-triphosphate (GTP) into cyclic pyranopterin (cPMP) through the action of two enzymes, MoaA and MoaC (molybdenum cofactor biosynthesis protein A and C, respectively). Conventionally, MoaA was considered to catalyze the majority of this transformation, with MoaC playing little or no role in the pyranopterin formation. Recently, this view was challenged by the isolation of 3′,8-cyclo-7,8-dihydro-guanosine 5′-triphosphate (3′,8-cH2GTP) as the product of in vitro MoaA reactions. To elucidate the mechanism of formation of Moco pyranopterin backbone, we performed biochemical characterization of 3′,8-cH2GTP and functional and X-ray crystallographic characterizations of MoaC. These studies revealed that 3′,8-cH2GTP is the only product of MoaA that can be converted to cPMP by MoaC. Our structural studies captured the specific binding of 3′,8-cH2GTP in the active site of MoaC. These observations provided strong evidence that the physiological function of MoaA is the conversion of GTP to 3′,8-cH2GTP (GTP 3′,8-cyclase), and that of MoaC is to catalyze the rearrangement of 3′,8-cH2GTP into cPMP (cPMP synthase). Furthermore, our structure-guided studies suggest that MoaC catalysis involves the dynamic motions of enzyme active-site loops as a way to control the timing of interaction between the reaction intermediates and catalytically essential amino acid residues. Thus, these results reveal the previously unidentified mechanism behind Moco biosynthesis and provide mechanistic and structural insights into how enzymes catalyze complex rearrangement reactions.

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