Document Detail

Catalysis of a new ribose carbon-insertion reaction by the molybdenum cofactor biosynthetic enzyme MoaA.
MedLine Citation:
PMID:  23286307     Owner:  NLM     Status:  MEDLINE    
MoaA, a radical S-adenosylmethionine enzyme, catalyzes the first step in molybdopterin biosynthesis. This reaction involves a complex rearrangement in which C8 of guanosine triphosphate is inserted between C2' and C3' of the ribose. This study identifies the site of initial hydrogen atom abstraction by the adenosyl radical and advances a mechanistic proposal for this unprecedented reaction.
Angad P Mehta; Jeremiah W Hanes; Sameh H Abdelwahed; David G Hilmey; Petra Hänzelmann; Tadhg P Begley
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2013-02-04
Journal Detail:
Title:  Biochemistry     Volume:  52     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-02-19     Completed Date:  2013-04-26     Revised Date:  2014-02-20    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1134-6     Citation Subset:  IM    
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MeSH Terms
Coenzymes / chemistry,  metabolism*
Guanosine Triphosphate / chemistry,  metabolism
Hydrolases / chemistry*,  metabolism*
Magnetic Resonance Spectroscopy
Metalloproteins / chemistry,  metabolism*
Models, Chemical
Pteridines / chemistry,  metabolism*
Ribose / chemistry
Spectrometry, Mass, Electrospray Ionization
Grant Support
Reg. No./Substance:
0/Coenzymes; 0/Metalloproteins; 0/Pteridines; 681HV46001/Ribose; 73508-07-3/molybdenum cofactor; 7440-44-0/Carbon; 86-01-1/Guanosine Triphosphate; EC 3.-/Hydrolases; EC enzyme MoaA, Staphylococcus aureus

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