| 000 | 01828 a2200493 4500 | ||
|---|---|---|---|
| 005 | 20250513041639.0 | ||
| 264 | 0 | _c19950601 | |
| 008 | 199506s 0 0 eng d | ||
| 022 | _a0006-2960 | ||
| 024 | 7 |
_a10.1021/bi00016a013 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aEberhard, M | |
| 245 | 0 | 0 |
_aIndoleglycerol phosphate synthase-phosphoribosyl anthranilate isomerase: comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domains. _h[electronic resource] |
| 260 |
_bBiochemistry _cApr 1995 |
||
| 300 |
_a5419-28 p. _bdigital |
||
| 500 | _aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAldose-Ketose Isomerases |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aBase Sequence |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 |
_aCarbohydrate Epimerases _xisolation & purification |
| 650 | 0 | 4 | _aChromatography, Gel |
| 650 | 0 | 4 | _aChromatography, Ion Exchange |
| 650 | 0 | 4 | _aEnzyme Stability |
| 650 | 0 | 4 |
_aEscherichia coli _xenzymology |
| 650 | 0 | 4 | _aGenes, Bacterial |
| 650 | 0 | 4 |
_aIndole-3-Glycerol-Phosphate Synthase _xisolation & purification |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 |
_aMultienzyme Complexes _xisolation & purification |
| 650 | 0 | 4 | _aMutagenesis, Site-Directed |
| 650 | 0 | 4 | _aOligodeoxyribonucleotides |
| 650 | 0 | 4 | _aOperon |
| 650 | 0 | 4 | _aProtein Engineering |
| 650 | 0 | 4 |
_aRecombinant Proteins _xisolation & purification |
| 650 | 0 | 4 | _aSpectrophotometry |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 700 | 1 | _aTsai-Pflugfelder, M | |
| 700 | 1 | _aBolewska, K | |
| 700 | 1 | _aHommel, U | |
| 700 | 1 | _aKirschner, K | |
| 773 | 0 |
_tBiochemistry _gvol. 34 _gno. 16 _gp. 5419-28 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1021/bi00016a013 _zAvailable from publisher's website |
| 999 |
_c7726769 _d7726769 |
||