PMID- 10593920
OWN - NLM
STAT- MEDLINE
DCOM- 20000127
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 51
DP  - 1999 Dec 17
TI  - The fatty acid transport protein (FATP1) is a very long chain acyl-CoA
      synthetase.
PG  - 36300-4
AB  - The primary sequence of the murine fatty acid transport protein (FATP1) is very
      similar to the multigene family of very long chain (C20-C26) acyl-CoA
      synthetases. To determine if FATP1 is a long chain acyl coenzyme A synthetase,
      FATP1-Myc/His fusion protein was expressed in COS1 cells, and its enzymatic
      activity was analyzed. In addition, mutations were generated in two domains
      conserved in acyl-CoA synthetases: a 6- amino acid substitution into the putative
      active site (amino acids 249-254) generating mutant M1 and a 59-amino acid
      deletion into a conserved C-terminal domain (amino acids 464-523) generating
      mutant M2. Immunolocalization revealed that the FATP1-Myc/His forms were
      distributed between the COS1 cell plasma membrane and intracellular membranes.
      COS1 cells expressing wild type FATP1-Myc/His exhibited a 3-fold increase in the 
      ratio of lignoceroyl-CoA synthetase activity (C24:0) to palmitoyl-CoA synthetase 
      activity (C16:0), characteristic of very long chain acyl-CoA synthetases, whereas
      both mutant M1 and M2 were catalytically inactive. Detergent-solubilized
      FATP1-Myc/His was partially purified using nickel-based affinity chromatography
      and demonstrated a 10-fold increase in very long chain acyl-CoA specific activity
      (C24:0/C16:0). These results indicate that FATP1 is a very long chain acyl-CoA
      synthetase and suggest that a potential mechanism for facilitating mammalian
      fatty acid uptake is via esterification coupled influx.
FAU - Coe, N R
AU  - Coe NR
AD  - Department of Biochemistry, Molecular Biology and Biophysics, University of
      Minnesota, St. Paul, Minnesota 55108, USA.
FAU - Smith, A J
AU  - Smith AJ
FAU - Frohnert, B I
AU  - Frohnert BI
FAU - Watkins, P A
AU  - Watkins PA
FAU - Bernlohr, D A
AU  - Bernlohr DA
LA  - eng
GR  - DK49807/DK/NIDDK NIH HHS/United States
GR  - HD10981/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (Fatty Acid Transport Proteins)
RN  - 0 (Fatty Acids)
RN  - 0 (Membrane Proteins)
RN  - 0 (Membrane Transport Proteins)
RN  - EC 6.2.1.- (Coenzyme A Ligases)
SB  - IM
MH  - Animals
MH  - COS Cells
MH  - Carrier Proteins/*chemistry/*genetics/metabolism
MH  - Coenzyme A Ligases/*chemistry/*genetics/metabolism
MH  - Fatty Acid Transport Proteins
MH  - Fatty Acids/metabolism
MH  - Membrane Proteins/*chemistry/*genetics/metabolism
MH  - *Membrane Transport Proteins
MH  - Sequence Analysis
MH  - Transfection
EDAT- 1999/12/14 00:00
MHDA- 1999/12/14 00:01
CRDT- 1999/12/14 00:00
PHST- 1999/12/14 00:00 [pubmed]
PHST- 1999/12/14 00:01 [medline]
PHST- 1999/12/14 00:00 [entrez]
AID - 10.1074/jbc.274.51.36300 [doi]
AID - S0021-9258(19)53164-7 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Dec 17;274(51):36300-4. doi: 10.1074/jbc.274.51.36300.