| 000 | 01876 a2200529 4500 | ||
|---|---|---|---|
| 005 | 20250516091202.0 | ||
| 264 | 0 | _c20120924 | |
| 008 | 201209s 0 0 eng d | ||
| 022 | _a1532-298X | ||
| 024 | 7 |
_a10.1105/tpc.112.097675 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aCobessi, David | |
| 245 | 0 | 0 |
_aBiochemical and structural characterization of the Arabidopsis bifunctional enzyme dethiobiotin synthetase-diaminopelargonic acid aminotransferase: evidence for substrate channeling in biotin synthesis. _h[electronic resource] |
| 260 |
_bThe Plant cell _cApr 2012 |
||
| 300 |
_a1608-25 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 |
_aAmino Acids _xchemistry |
| 650 | 0 | 4 |
_aArabidopsis _xenzymology |
| 650 | 0 | 4 |
_aArabidopsis Proteins _xchemistry |
| 650 | 0 | 4 | _aBiocatalysis |
| 650 | 0 | 4 | _aBiosynthetic Pathways |
| 650 | 0 | 4 |
_aBiotin _xanalogs & derivatives |
| 650 | 0 | 4 |
_aCarbon-Nitrogen Ligases _xchemistry |
| 650 | 0 | 4 | _aCatalytic Domain |
| 650 | 0 | 4 |
_aHoloenzymes _xchemistry |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aLigands |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 |
_aMutation _xgenetics |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Multimerization |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 | _aProtein Structure, Tertiary |
| 650 | 0 | 4 |
_aRecombinant Proteins _xbiosynthesis |
| 650 | 0 | 4 |
_aSubcellular Fractions _xenzymology |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 650 | 0 | 4 |
_aTransaminases _xchemistry |
| 700 | 1 | _aDumas, Renaud | |
| 700 | 1 | _aPautre, Virginie | |
| 700 | 1 | _aMeinguet, Céline | |
| 700 | 1 | _aFerrer, Jean-Luc | |
| 700 | 1 | _aAlban, Claude | |
| 773 | 0 |
_tThe Plant cell _gvol. 24 _gno. 4 _gp. 1608-25 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1105/tpc.112.097675 _zAvailable from publisher's website |
| 999 |
_c21745032 _d21745032 |
||