| 000 | 01721 a2200493 4500 | ||
|---|---|---|---|
| 005 | 20250513040847.0 | ||
| 264 | 0 | _c19950510 | |
| 008 | 199505s 0 0 eng d | ||
| 022 | _a0006-2960 | ||
| 024 | 7 |
_a10.1021/bi00013a018 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aHendle, J | |
| 245 | 0 | 0 |
_aCrystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p). _h[electronic resource] |
| 260 |
_bBiochemistry _cApr 1995 |
||
| 300 |
_a4287-98 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 |
_aAcetyltransferases _xchemistry |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 |
_aAsparagine _xchemistry |
| 650 | 0 | 4 |
_aAzotobacter vinelandii _xenzymology |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aCatalysis |
| 650 | 0 | 4 | _aCrystallization |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 | _aDihydrolipoyllysine-Residue Acetyltransferase |
| 650 | 0 | 4 |
_aHistidine _xchemistry |
| 650 | 0 | 4 | _aHydrogen Bonding |
| 650 | 0 | 4 | _aHydrogen-Ion Concentration |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aMutagenesis, Site-Directed |
| 650 | 0 | 4 | _aPyruvate Dehydrogenase Complex |
| 650 | 0 | 4 |
_aSerine _xchemistry |
| 650 | 0 | 4 | _aStructure-Activity Relationship |
| 700 | 1 | _aMattevi, A | |
| 700 | 1 | _aWestphal, A H | |
| 700 | 1 | _aSpee, J | |
| 700 | 1 | _ade Kok, A | |
| 700 | 1 | _aTeplyakov, A | |
| 700 | 1 | _aHol, W G | |
| 773 | 0 |
_tBiochemistry _gvol. 34 _gno. 13 _gp. 4287-98 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1021/bi00013a018 _zAvailable from publisher's website |
| 999 |
_c7702652 _d7702652 |
||