PMID- 22439765
OWN - NLM
STAT- MEDLINE
DCOM- 20120615
LR  - 20131121
IS  - 1520-4995 (Electronic)
IS  - 0006-2960 (Linking)
VI  - 51
IP  - 14
DP  - 2012 Apr 10
TI  - An enzymatic pathway for the biosynthesis of the formylhydroxyornithine required 
      for rhodochelin iron coordination.
PG  - 3059-66
LID - 10.1021/bi201837f [doi]
AB  - Rhodochelin, a mixed catecholate-hydroxamate type siderophore isolated from 
      Rhodococcus jostii RHA1, holds two L-delta-N-formyl-delta-N-hydroxyornithine (L-fhOrn) 
      moieties essential for proper iron coordination. Previously, bioinformatic and 
      genetic analysis proposed rmo and rft as the genes required for the tailoring of 
      the L-ornithine (L-Orn) precursor [Bosello, M. (2011) J. Am. Chem. Soc.133, 
      4587-4595]. In order to investigate if both Rmo and Rft constitute a pathway for 
      L-fhOrn biosynthesis, the enzymes were heterologously produced and assayed in 
      vitro. In the presence of molecular oxygen, NADPH and FAD, Rmo monooxygenase was 
      able to convert L-Orn into L-delta-N-hydroxyornithine (L-hOrn). As confirmed in a 
      coupled reaction assay, this hydroxylated intermediate serves as a substrate for 
      the subsequent N(10)-formyl-tetrahydrofolate-dependent (N(10)-fH(4)F) 
      Rtf-catalyzed formylation reaction, establishing a route for the L-fhOrn 
      biosynthesis, prior to its incorporation by the NRPS assembly line. It is of 
      particular interest that a major improvement to this study has been reached with 
      the use of an alternative approach to the chemoenzymatic FolD-dependent 
      N(10)-fH(4)F conversion, also rescuing the previously inactive CchA, the 
      Rft-homologue in coelichelin assembly line [Buchenau, B. (2004) Arch. 
      Microbiol.182, 313-325; Pohlmann, V. (2008) Org. Biomol. Chem.6, 1843-1848].
CI  - (c) 2012 American Chemical Society
FAU - Bosello, Mattia
AU  - Bosello M
AD  - Biochemistry, Department of Chemistry, Philipps-University Marburg, 
      Hans-Meerwein-Strasse, D-35043 Marburg, Germany.
FAU - Mielcarek, Andreas
AU  - Mielcarek A
FAU - Giessen, Tobias W
AU  - Giessen TW
FAU - Marahiel, Mohamed A
AU  - Marahiel MA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120330
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Bacterial Proteins)
RN  - 0 (Oligopeptides)
RN  - 0 (Recombinant Proteins)
RN  - 0 (rhodochelin)
RN  - E1UOL152H7 (Iron)
RN  - E524N2IXA3 (Ornithine)
RN  - EC 1.- (Mixed Function Oxygenases)
RN  - EC 2.1.2.- (Hydroxymethyl and Formyl Transferases)
SB  - IM
MH  - Bacterial Proteins/*chemistry/genetics
MH  - Binding Sites
MH  - Hydroxylation
MH  - Hydroxymethyl and Formyl Transferases/*chemistry/genetics
MH  - Iron/*chemistry/metabolism
MH  - Mixed Function Oxygenases/*chemistry/genetics
MH  - Oligopeptides/*chemistry/metabolism
MH  - Ornithine/*analogs & derivatives/biosynthesis/*chemistry
MH  - Recombinant Proteins/chemistry/genetics
MH  - Rhodococcus/metabolism
MH  - Substrate Specificity
EDAT- 2012/03/24 06:00
MHDA- 2012/06/16 06:00
CRDT- 2012/03/24 06:00
PHST- 2012/03/24 06:00 [entrez]
PHST- 2012/03/24 06:00 [pubmed]
PHST- 2012/06/16 06:00 [medline]
AID - 10.1021/bi201837f [doi]
PST - ppublish
SO  - Biochemistry. 2012 Apr 10;51(14):3059-66. doi: 10.1021/bi201837f. Epub 2012 Mar 
      30.