PMID- 20039350
OWN - NLM
STAT- MEDLINE
DCOM- 20100427
LR  - 20111117
IS  - 1521-3765 (Electronic)
IS  - 0947-6539 (Linking)
VI  - 16
IP  - 6
DP  - 2010 Feb 8
TI  - Targeting bacterial membranes: NMR spectroscopy characterization of substrate 
      recognition and binding requirements of D-arabinose-5-phosphate isomerase.
PG  - 1897-902
LID - 10.1002/chem.200902619 [doi]
AB  - Lipopolysaccharide (LPS) is an essential component of the outer membrane of 
      gram-negative bacteria and consists of three elements: lipid A, the core 
      oligosaccharide, and the O-antigen. The inner-core region is highly conserved and 
      contains at least one residue of 3-deoxy-D-manno-octulosonate (Kdo). 
      Arabinose-5-phosphate isomerase (API) is an aldo-keto isomerase catalyzing the 
      reversible isomerization of D-ribulose-5-phosphate (Ru5P) to 
      D-arabinose-5-phosphate (A5P), the first step of Kdo biosynthesis. By exploiting 
      saturation transfer difference (STD) NMR spectroscopy, the structural 
      requirements necessary for API substrate recognition and binding were identified, 
      with the aim of designing new API inhibitors. In addition, simple experimental 
      conditions for the STD experiments to perform a fast, robust, and efficient 
      screening of small libraries of potential API inhibitors, allowing the 
      identification of new potential leads, were set up. Due to the essential role of 
      API enzymes in LPS biosynthesis and gram-negative bacteria survival, by 
      exploiting these data, a new generation of potent antibacterial drugs could be 
      developed.
FAU - Airoldi, Cristina
AU  - Airoldi C
AD  - Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza 
      della Scienza 2, 20126, Milan, Italy.
FAU - Sommaruga, Silvia
AU  - Sommaruga S
FAU - Merlo, Silvia
AU  - Merlo S
FAU - Sperandeo, Paola
AU  - Sperandeo P
FAU - Cipolla, Laura
AU  - Cipolla L
FAU - Polissi, Alessandra
AU  - Polissi A
FAU - Nicotra, Francesco
AU  - Nicotra F
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Chemistry
JT  - Chemistry (Weinheim an der Bergstrasse, Germany)
JID - 9513783
RN  - 0 (Lipopolysaccharides)
RN  - 0 (O Antigens)
RN  - 0 (Polysaccharides, Bacterial)
RN  - 0 (Sugar Acids)
RN  - EC 5.3.1.- (Aldose-Ketose Isomerases)
RN  - EC 5.3.1.13 (arabinose-5-phosphate isomerase)
RN  - EC 5.3.1.3 (D-arabinose isomerase)
SB  - IM
MH  - Aldose-Ketose Isomerases/chemistry/*metabolism
MH  - Binding Sites
MH  - Escherichia coli/metabolism
MH  - Isomerism
MH  - Lipopolysaccharides/biosynthesis
MH  - Magnetic Resonance Spectroscopy/methods
MH  - Membranes/*chemistry/metabolism
MH  - O Antigens/*biosynthesis
MH  - Polysaccharides, Bacterial/biosynthesis
MH  - Substrate Specificity
MH  - Sugar Acids/metabolism
EDAT- 2009/12/30 06:00
MHDA- 2010/04/28 06:00
CRDT- 2009/12/30 06:00
PHST- 2009/12/30 06:00 [entrez]
PHST- 2009/12/30 06:00 [pubmed]
PHST- 2010/04/28 06:00 [medline]
AID - 10.1002/chem.200902619 [doi]
PST - ppublish
SO  - Chemistry. 2010 Feb 8;16(6):1897-902. doi: 10.1002/chem.200902619.