PMID- 16788179
OWN - NLM
STAT- MEDLINE
DCOM- 20060804
LR  - 20181113
IS  - 0021-9193 (Print)
IS  - 1098-5530 (Electronic)
IS  - 0021-9193 (Linking)
VI  - 188
IP  - 13
DP  - 2006 Jul
TI  - The ribulose monophosphate pathway substitutes for the missing pentose phosphate 
      pathway in the archaeon Thermococcus kodakaraensis.
PG  - 4698-704
AB  - The ribulose monophosphate (RuMP) pathway, involving 3-hexulose-6-phosphate 
      synthase (HPS) and 6-phospho-3-hexuloisomerase (PHI), is now recognized as a 
      widespread prokaryotic pathway for formaldehyde fixation and detoxification. 
      Interestingly, HPS and PHI homologs are also found in a variety of archaeal 
      strains, and recent biochemical and genome analyses have raised the possibility 
      that the reverse reaction of formaldehyde fixation, i.e., ribulose 5-phosphate 
      (Ru5P) synthesis from fructose 6-phosphate, may function in the biosynthesis of 
      Ru5P in some archaeal strains whose pentose phosphate pathways are imperfect. In 
      this study, we have taken a genetic approach to address this possibility by using 
      the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. This strain 
      possesses a single open reading frame (TK0475) encoding an HPS- and PHI-fused 
      protein. The recombinant HPS-PHI-fused enzyme exhibited the expected HPS and PHI 
      activities in both directions (formaldehyde fixing and Ru5P synthesizing). The 
      TK0475 deletion mutant Delta hps-phi-7A did not exhibit any growth in minimal 
      medium, while growth of the mutant strain could be recovered by the addition of 
      nucleosides to the medium. This auxotrophic phenotype together with the catalytic 
      properties of the HPS-PHI-fused enzyme reveal that HPS and PHI are essential for 
      the biosynthesis of Ru5P, the precursor of nucleotides, showing that the RuMP 
      pathway is the only relevant pathway for Ru5P biosynthesis substituting for the 
      classical pentose phosphate pathway missing in this archaeon.
FAU - Orita, Izumi
AU  - Orita I
AD  - Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto 
      University, Kitashirakawa-Oiwake, Kyoto 606-8502, Japan.
FAU - Sato, Takaaki
AU  - Sato T
FAU - Yurimoto, Hiroya
AU  - Yurimoto H
FAU - Kato, Nobuo
AU  - Kato N
FAU - Atomi, Haruyuki
AU  - Atomi H
FAU - Imanaka, Tadayuki
AU  - Imanaka T
FAU - Sakai, Yasuyoshi
AU  - Sakai Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Bacteriol
JT  - Journal of bacteriology
JID - 2985120R
RN  - 0 (Archaeal Proteins)
RN  - 0 (Ribulosephosphates)
RN  - 1HG84L3525 (Formaldehyde)
RN  - 4151-19-3 (ribulose 5-phosphate)
RN  - EC 4.1.2.- (Aldehyde-Lyases)
RN  - EC 4.1.2.- (hexose phosphate synthetase)
RN  - EC 5.3.1.- (Aldose-Ketose Isomerases)
RN  - EC 5.3.1.- (phospho-3-hexuloisomerase)
SB  - IM
MH  - Aldehyde-Lyases/*metabolism
MH  - Aldose-Ketose Isomerases/*metabolism
MH  - Archaeal Proteins/*metabolism
MH  - Formaldehyde/metabolism
MH  - Open Reading Frames
MH  - Pentose Phosphate Pathway
MH  - Ribulosephosphates/*biosynthesis
MH  - Thermococcus/growth & development/*metabolism
PMC - PMC1482999
EDAT- 2006/06/22 09:00
MHDA- 2006/08/05 09:00
PMCR- 2006/11/01
CRDT- 2006/06/22 09:00
PHST- 2006/06/22 09:00 [pubmed]
PHST- 2006/08/05 09:00 [medline]
PHST- 2006/06/22 09:00 [entrez]
PHST- 2006/11/01 00:00 [pmc-release]
AID - 188/13/4698 [pii]
AID - 0492-06 [pii]
AID - 10.1128/JB.00492-06 [doi]
PST - ppublish
SO  - J Bacteriol. 2006 Jul;188(13):4698-704. doi: 10.1128/JB.00492-06.