000 01468 a2200361 4500
005 20250511191420.0
264 0 _c19920406
008 199204s 0 0 eng d
022 _a0006-2960
024 7 _a10.1021/bi00123a015
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aBraxton, B L
245 0 0 _aQuantifying the allosteric properties of Escherichia coli carbamyl phosphate synthetase: determination of thermodynamic linked-function parameters in an ordered kinetic mechanism.
_h[electronic resource]
260 _bBiochemistry
_cMar 1992
300 _a2309-16 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
650 0 4 _aAdenosine Triphosphatases
_xchemistry
650 0 4 _aAdenosine Triphosphate
_xbiosynthesis
650 0 4 _aAllosteric Regulation
_xdrug effects
650 0 4 _aCarbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)
_xchemistry
650 0 4 _aEnzyme Activation
_xdrug effects
650 0 4 _aEscherichia coli
_xenzymology
650 0 4 _aKinetics
650 0 4 _aOrnithine
_xpharmacology
650 0 4 _aStructure-Activity Relationship
650 0 4 _aSubstrate Specificity
_xdrug effects
650 0 4 _aThermodynamics
700 1 _aMullins, L S
700 1 _aRaushel, F M
700 1 _aReinhart, G D
773 0 _tBiochemistry
_gvol. 31
_gno. 8
_gp. 2309-16
856 4 0 _uhttps://doi.org/10.1021/bi00123a015
_zAvailable from publisher's website
999 _c1538250
_d1538250