| 000 | 01776 a2200517 4500 | ||
|---|---|---|---|
| 005 | 20250515103735.0 | ||
| 264 | 0 | _c20080806 | |
| 008 | 200808s 0 0 eng d | ||
| 022 | _a1097-0134 | ||
| 024 | 7 |
_a10.1002/prot.21898 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aIlari, Andrea | |
| 245 | 0 | 0 |
_aThe X-ray structure of N-methyltryptophan oxidase reveals the structural determinants of substrate specificity. _h[electronic resource] |
| 260 |
_bProteins _cJun 2008 |
||
| 300 |
_a2065-75 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aCatalysis |
| 650 | 0 | 4 | _aCatalytic Domain |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 |
_aEscherichia coli _xenzymology |
| 650 | 0 | 4 |
_aEscherichia coli Proteins _xanalysis |
| 650 | 0 | 4 |
_aFlavin-Adenine Dinucleotide _xmetabolism |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aMolecular Weight |
| 650 | 0 | 4 | _aMutation |
| 650 | 0 | 4 |
_aOxidoreductases, N-Demethylating _xanalysis |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 | _aProtein Structure, Tertiary |
| 650 | 0 | 4 | _aSequence Homology, Amino Acid |
| 650 | 0 | 4 | _aSpectrophotometry, Ultraviolet |
| 650 | 0 | 4 | _aSpectrum Analysis, Raman |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 650 | 0 | 4 |
_aThreonine _xchemistry |
| 700 | 1 | _aBonamore, Alessandra | |
| 700 | 1 | _aFranceschini, Stefano | |
| 700 | 1 | _aFiorillo, Annarita | |
| 700 | 1 | _aBoffi, Alberto | |
| 700 | 1 | _aColotti, Gianni | |
| 773 | 0 |
_tProteins _gvol. 71 _gno. 4 _gp. 2065-75 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1002/prot.21898 _zAvailable from publisher's website |
| 999 |
_c17695902 _d17695902 |
||