PMID- 24955657
OWN - NLM
STAT- MEDLINE
DCOM- 20150526
LR  - 20211203
IS  - 1520-5126 (Electronic)
IS  - 0002-7863 (Print)
IS  - 0002-7863 (Linking)
VI  - 136
IP  - 30
DP  - 2014 Jul 30
TI  - Molybdopterin biosynthesis: trapping of intermediates for the MoaA-catalyzed 
      reaction using 2'-deoxyGTP and 2'-chloroGTP as substrate analogues.
PG  - 10609-14
LID - 10.1021/ja502663k [doi]
AB  - 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. In this paper, we provide additional characterization 
      of the MoaA reaction product, describe the use of 2'-chloroGTP to trap the GTP 
      C3' radical, generated by hydrogen atom transfer to the 5'-deoxyadenosyl radical, 
      and the use of 2'-deoxyGTP to block a late step in the reaction sequence. These 
      probes, coupled with the previously reported trapping of an intermediate in which 
      C3' of the ribose is linked to C8 of the purine, allow us to propose a plausible 
      mechanism for the MoaA-catalyzed reaction.
FAU - Mehta, Angad P
AU  - Mehta AP
AD  - Department of Chemistry, Texas A & M University , College Station, Texas 77843, 
      United States.
FAU - Abdelwahed, Sameh H
AU  - Abdelwahed SH
FAU - Xu, Hui
AU  - Xu H
FAU - Begley, Tadhg P
AU  - Begley TP
LA  - eng
GR  - R01 DK044083/DK/NIDDK NIH HHS/United States
GR  - R37 DK044083/DK/NIDDK NIH HHS/United States
GR  - DK44083/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20140718
PL  - United States
TA  - J Am Chem Soc
JT  - Journal of the American Chemical Society
JID - 7503056
RN  - 0 (Coenzymes)
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Metalloproteins)
RN  - 0 (Molybdenum Cofactors)
RN  - 0 (Pteridines)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - ATN6EG42UQ (molybdenum cofactor)
RN  - EC 5.- (Isomerases)
RN  - EC 5.- (MoaA protein, E coli)
SB  - IM
MH  - Coenzymes/*metabolism
MH  - Escherichia coli/*enzymology/metabolism
MH  - Escherichia coli Proteins/*metabolism
MH  - Guanosine Triphosphate/*analogs & derivatives/metabolism
MH  - Halogenation
MH  - Isomerases/*metabolism
MH  - Metalloproteins/*metabolism
MH  - Molybdenum Cofactors
MH  - Pteridines/*metabolism
MH  - Substrate Specificity
PMC - PMC4227724
EDAT- 2014/06/24 06:00
MHDA- 2015/05/27 06:00
PMCR- 2015/06/23
CRDT- 2014/06/24 06:00
PHST- 2014/06/24 06:00 [entrez]
PHST- 2014/06/24 06:00 [pubmed]
PHST- 2015/05/27 06:00 [medline]
PHST- 2015/06/23 00:00 [pmc-release]
AID - 10.1021/ja502663k [doi]
PST - ppublish
SO  - J Am Chem Soc. 2014 Jul 30;136(30):10609-14. doi: 10.1021/ja502663k. Epub 2014 
      Jul 18.