000 | 01755 a2200481 4500 | ||
---|---|---|---|
005 | 20250513143413.0 | ||
264 | 0 | _c19980716 | |
008 | 199807s 0 0 eng d | ||
022 | _a0021-9258 | ||
024 | 7 |
_a10.1074/jbc.273.23.14107 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aCollet, J F | |
245 | 0 | 0 |
_aA new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif. _h[electronic resource] |
260 |
_bThe Journal of biological chemistry _cJun 1998 |
||
300 |
_a14107-12 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
650 | 0 | 4 | _aAmino Acid Sequence |
650 | 0 | 4 |
_aAspartic Acid _xchemistry |
650 | 0 | 4 |
_aBacterial Proteins _xchemistry |
650 | 0 | 4 |
_aBorohydrides _xmetabolism |
650 | 0 | 4 | _aConserved Sequence |
650 | 0 | 4 | _aDatabases, Factual |
650 | 0 | 4 | _aHumans |
650 | 0 | 4 |
_aHydrolases _xchemistry |
650 | 0 | 4 |
_aLactobacillus _xenzymology |
650 | 0 | 4 | _aMass Spectrometry |
650 | 0 | 4 | _aMolecular Sequence Data |
650 | 0 | 4 |
_aMutagenesis, Site-Directed _xgenetics |
650 | 0 | 4 |
_aPeptide Fragments _xchemistry |
650 | 0 | 4 |
_aPhosphoric Monoester Hydrolases _xchemistry |
650 | 0 | 4 | _aPhosphorylation |
650 | 0 | 4 |
_aPhosphotransferases _xchemistry |
650 | 0 | 4 |
_aPhosphotransferases (Phosphomutases) _xchemistry |
650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
650 | 0 | 4 | _aSequence Alignment |
650 | 0 | 4 |
_aTrypsin _xmetabolism |
700 | 1 | _aStroobant, V | |
700 | 1 | _aPirard, M | |
700 | 1 | _aDelpierre, G | |
700 | 1 | _aVan Schaftingen, E | |
773 | 0 |
_tThe Journal of biological chemistry _gvol. 273 _gno. 23 _gp. 14107-12 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1074/jbc.273.23.14107 _zAvailable from publisher's website |
999 |
_c9570606 _d9570606 |