3‐Azido‐L‐tyrosine as a photoinhibitor of tubulin:tyrosine ligase

FEBS Letters

Joniau, Marcel¹  Coudijzer, Katleen¹ 

[1] Interdisciplinary Research Center, KU Leuven, Campus Kortrijk, B-8500 Kortrijk, Belgium

关键词: Tubulin;    Tubulin:tyrosine ligase;    Posttranslational modification;    3-Azido-L-tyrosine;    Photoinaetivation;    Thiol group;    TTLase;    tubulin:tyrosine ligase;    Tub;    tubulin;    NH2Tyr;    3-amino-L-tyrosine;    Na3Tyr;    3-azido-L-tyrosine;    NH2Phe;    p-amino-L-phenylalanine;    N3Phe;    p-azido-L-phenylalanine;    pCMB;    p-chloromercuribenzoic acid;    DTE;    dithioerythritol;    DTNB (Ellman's reagent);    5;    5'-dithiobis-(2-nitrobenzoic acid);    Mes;    2-(N-morpholino)ethanesulfonic acid;    ME;    β-mercaptoethanol;   

DOI  :  10.1016/0014-5793(90)80981-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have synthesized the photoactivatable probes 3-azido-L-tyrosine andp-azido-L-phenylalanine and studied their capacity to inhibit the incorporation of[³H]tyrosine into tubulin catalyzed by tubulin:tyrosine ligase. Without illumination, only 3-azido-L-tyrosine reversibly inhibits the enzyme. Upon illumination, both reagents irreversibly photoinactivate the enzyme in a similar way. The ligase can be protected against photoinactivation by reversibly blocking essential thiol groups with pCMB during illumination.

【 授权许可】

Unknown