期刊论文详细信息
FEBS Letters | |
3‐Azido‐L‐tyrosine as a photoinhibitor of tubulin:tyrosine ligase | |
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
【 预 览 】
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