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    • 6. 发明授权
    • Human methionine aminopeptidase type 3
    • 人甲硫氨酸氨肽酶3型
    • US06953577B2
    • 2005-10-11
    • US10299867
    • 2002-11-19
    • Carolyn J. SympsonRajeev AuroraStanton B. DotsonRonald B. FrazierCynthia L. WoodsHamideh ZakeriXianzhi Zhou
    • Carolyn J. SympsonRajeev AuroraStanton B. DotsonRonald B. FrazierCynthia L. WoodsHamideh ZakeriXianzhi Zhou
    • A61K38/00A61K39/00C12N9/48A01N63/00C07H21/04C12N1/20C12N15/00
    • C12Y304/11018A61K38/00A61K39/00C12N9/48
    • Methionine aminopeptidases catalyse the co-translational removal of amino terminal methionine residues from nascent polypeptide chains. A newly-discovered enzyme, designated methionine aminopeptidase type-3 (MetAP-3), has a substrate specificity which is similar to MetAP-1 and MetAP-2, although it is not inhibited by fumagillin, an irreversible inhibitor of MetAP-2. MetAP-3 also preferentially localizes to mitochondria, unlike MetAP-1 and MetAP-2, which accumulate in the cytoplasm. One embodiment of the present invention relates to human cDNAs encoding polypeptides comprising MetAP-3. Other embodiments of the invention relate to nucleic acid molecules derived from these cDNAs, including complements, homologues, and fragments thereof, and methods of using these nucleic acid molecules, to generate polypeptides and fragments thereof. Other embodiments of the invention relate to antibodies directed against polypeptides comprising MetAP-3, and methods to screen for compounds or compositions that preferentially or specifically effect the activity of polypeptides comprising MetAP-3.
    • 甲硫氨酸氨基肽酶催化从新生多肽链共转移氨基末端甲硫氨酸残基。 称为甲硫氨酸氨基肽酶-3型(MetAP-3)的新发现的酶具有与MetAP-1和MetAP-2相似的底物特异性,尽管它不被万古霉素(Metap-2的不可逆抑制剂)抑制。 MetAP-3也优先定位于线粒体,不同于MetAP-1和MetAP-2,其积聚在细胞质中。 本发明的一个实施方案涉及编码包含MetAP-3的多肽的人cDNA。 本发明的其它实施方案涉及衍生自这些cDNA的核酸分子,包括其互补序列,同系物及其片段,以及使用这些核酸分子的方法来产生其多肽及其片段。 本发明的其它实施方案涉及针对包含MetAP-3的多肽的抗体,以及筛选优先或特异性影响包含MetAP-3的多肽的活性的化合物或组合物的方法。