Evidence that His110 of the protein FadL in the outer membrane of Escherichia coli is involved in the binding and uptake of long-chain fatty acids: possible role of this residue in carboxylate binding.
about
Modulating the import of medium-chain alkanes in E. coli through tuned expression of FadL.Ligand-gated diffusion across the bacterial outer membraneDisruption of the Saccharomyces cerevisiae homologue to the murine fatty acid transport protein impairs uptake and growth on long-chain fatty acids.Murine FATP alleviates growth and biochemical deficiencies of yeast fat1Delta strains.Molecular basis of bacterial outer membrane permeability revisitedTransmembrane movement of exogenous long-chain fatty acids: proteins, enzymes, and vectorial esterification.Bacterial long chain fatty acid transport: gateway to a fatty acid-responsive signaling system.Metabolic pathway for a new strain Pseudomonas synxantha LSH-7': from chemotaxis to uptake of n-hexadecane.Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity anMutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity.QSAR-based molecular signatures of prenylated (iso)flavonoids underlying antimicrobial potency against and membrane-disruption in Gram positive and Gram negative bacteria.
P2860
Q27300970-B3AB3A93-1422-4631-89F3-BCC591DCA77CQ27667890-0A881697-F187-4DBC-9D09-4BB36B693208Q27934119-952BDC09-16DF-4E9F-855C-4159E8E2F2F9Q27937668-37A66490-5315-4AE1-8BA9-D0030B46B19CQ29616208-C048022C-DC37-4BA0-AA10-4D334DFF850AQ35215951-F7C54F2F-4F21-4BAF-9440-2E1EBEE73BE9Q35878483-CFECA9CC-33C7-49B3-8376-AF5EEF144D55Q37554557-9438F4AE-7124-4825-BB60-1C21833FEE5FQ44009258-A82B4D7B-2AFC-4961-9568-3DB279D9502FQ54570547-DA8C3FE8-FFBA-4EE6-B34C-0F9104D1C28BQ55388106-94D90E88-5C5B-4497-8AA6-CBEF78D40017
P2860
Evidence that His110 of the protein FadL in the outer membrane of Escherichia coli is involved in the binding and uptake of long-chain fatty acids: possible role of this residue in carboxylate binding.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Evidence that His110 of the pr ...... esidue in carboxylate binding.
@en
type
label
Evidence that His110 of the pr ...... esidue in carboxylate binding.
@en
prefLabel
Evidence that His110 of the pr ...... esidue in carboxylate binding.
@en
P2860
P356
P1433
P1476
Evidence that His110 of the pr ...... residue in carboxylate binding
@en
P2093
P2860
P304
P356
10.1042/BJ3100389
P407
P478
310 ( Pt 2)
P577
1995-09-01T00:00:00Z