000 | 01866 a2200565 4500 | ||
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005 | 20250514212532.0 | ||
264 | 0 | _c20050718 | |
008 | 200507s 0 0 eng d | ||
022 | _a0021-924X | ||
024 | 7 |
_a10.1093/jb/mvh129 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aUmezawa, Yukiko | |
245 | 0 | 0 |
_aNovel prolyl tri/tetra-peptidyl aminopeptidase from Streptomyces mobaraensis: substrate specificity and enzyme gene cloning. _h[electronic resource] |
260 |
_bJournal of biochemistry _cSep 2004 |
||
300 |
_a293-300 p. _bdigital |
||
500 | _aPublication Type: Journal Article | ||
650 | 0 | 4 | _aAmino Acid Sequence |
650 | 0 | 4 | _aAminopeptidases |
650 | 0 | 4 | _aBase Sequence |
650 | 0 | 4 | _aBinding Sites |
650 | 0 | 4 | _aChromatography |
650 | 0 | 4 | _aCloning, Molecular |
650 | 0 | 4 |
_aDNA _xmetabolism |
650 | 0 | 4 | _aDipeptidyl-Peptidases and Tripeptidyl-Peptidases |
650 | 0 | 4 | _aElectrophoresis, Polyacrylamide Gel |
650 | 0 | 4 |
_aEndopeptidases _xbiosynthesis |
650 | 0 | 4 | _aHot Temperature |
650 | 0 | 4 | _aHydrogen-Ion Concentration |
650 | 0 | 4 | _aHydrolysis |
650 | 0 | 4 | _aIsoelectric Focusing |
650 | 0 | 4 | _aKinetics |
650 | 0 | 4 | _aMolecular Sequence Data |
650 | 0 | 4 | _aPeptides |
650 | 0 | 4 |
_aProline _xchemistry |
650 | 0 | 4 | _aSequence Homology, Amino Acid |
650 | 0 | 4 | _aSerine Proteases |
650 | 0 | 4 |
_aStreptomyces _xenzymology |
650 | 0 | 4 | _aSubstrate Specificity |
650 | 0 | 4 | _aTemperature |
650 | 0 | 4 |
_aTransglutaminases _xmetabolism |
650 | 0 | 4 | _aTripeptidyl-Peptidase 1 |
700 | 1 | _aYokoyama, Keiichi | |
700 | 1 | _aKikuchi, Yoshimi | |
700 | 1 | _aDate, Masayo | |
700 | 1 | _aIto, Kiyoshi | |
700 | 1 | _aYoshimoto, Tadashi | |
700 | 1 | _aMatsui, Hiroshi | |
773 | 0 |
_tJournal of biochemistry _gvol. 136 _gno. 3 _gp. 293-300 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1093/jb/mvh129 _zAvailable from publisher's website |
999 |
_c15281318 _d15281318 |