000 | 01468 a2200361 4500 | ||
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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 |