Modulation of ATPase activity by physical disengagement of the ATP-binding domains of an ABC transporter, the histidine permease.
Liu, P Q
Modulation of ATPase activity by physical disengagement of the ATP-binding domains of an ABC transporter, the histidine permease. [electronic resource] - The Journal of biological chemistry Jun 1999 - 18310-8 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0021-9258
10.1074/jbc.274.26.18310 doi
ATP-Binding Cassette Transporters--metabolism
Adenosine Triphosphatases--metabolism
Adenosine Triphosphate--metabolism
Amino Acid Transport Systems, Basic
Bacterial Proteins
Binding Sites
Biological Transport, Active
Escherichia coli
Hydrolysis
Macromolecular Substances
Membrane Proteins--metabolism
Membrane Transport Proteins--metabolism
Spectrometry, Fluorescence
Trypsin--metabolism
Modulation of ATPase activity by physical disengagement of the ATP-binding domains of an ABC transporter, the histidine permease. [electronic resource] - The Journal of biological chemistry Jun 1999 - 18310-8 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0021-9258
10.1074/jbc.274.26.18310 doi
ATP-Binding Cassette Transporters--metabolism
Adenosine Triphosphatases--metabolism
Adenosine Triphosphate--metabolism
Amino Acid Transport Systems, Basic
Bacterial Proteins
Binding Sites
Biological Transport, Active
Escherichia coli
Hydrolysis
Macromolecular Substances
Membrane Proteins--metabolism
Membrane Transport Proteins--metabolism
Spectrometry, Fluorescence
Trypsin--metabolism