Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications.
Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications.
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DOI：
10.1021/cb500897w
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发表时间：
2015-01-16
影响因子：
4
通讯作者：
Bertozzi, Carolyn R.
中科院分区：
文献类型：
--
作者：
Appel, Mason J.;Bertozzi, Carolyn R.
甲酰甘氨酸(FGly)是一种催化必需残基，几乎只存在于I型硫酸酯酶的活性部位。这种醛功能化残基由半胱氨酸或丝氨酸侧链的翻译后氧化形成，参与了一种独特而高效的硫酸酯水解催化机制。产生fGly的酶，甲酰甘氨酸生成酶(FGE)和厌氧硫酸酯酶成熟酶(AnSME)，和fGly本身一样独特和专门化。尤其是FGE在结构和机械上是不同的，并且唯一的功能是激活I型硫酸酯酶靶标。本文综述了fGly在硫酸酯水解酶中的作用机制，fGly在FGE和anSME中生物合成的分子细节，以及fGly在天然催化作用之外的生物技术应用。
Formylglycine (fGly) is a catalytically essential residue found almost exclusively in the active sites of type I sulfatases. Formed by post-translational oxidation of cysteine or serine side chains, this aldehyde-functionalized residue participates in a unique and highly efficient catalytic mechanism for sulfate ester hydrolysis. The enzymes that produce fGly, formylglycine-generating enzyme (FGE) and anaerobic sulfatase-maturating enzyme (anSME), are as unique and specialized as fGly itself. FGE especially is structurally and mechanistically distinct, and serves the sole function of activating type I sulfatase targets. This review summarizes the current state of knowledge regarding the mechanism by which fGly contributes to sulfate ester hydrolysis, the molecular details of fGly biogenesis by FGE and anSME, and finally, recent biotechnology applications of fGly beyond its natural catalytic function.
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影响因子：
15
作者：
Benjdia, Alhosna;Leprince, Jerome;Berteau, Olivier
通讯作者：
Berteau, Olivier
影响因子：
5.7
作者：
Bond, CS;Clements, PR;Guss, JM
通讯作者：
Guss, JM
影响因子：
4.1
作者：
CHAI, CLL;LOUGHLIN, WA;LOWE, G
通讯作者：
LOWE, G
DOI：
10.1074/jbc.m800217200
发表时间：
2008-07-18
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Carlson BL;Ballister ER;Skordalakes E;King DS;Breidenbach MA;Gilmore SA;Berger JM;Bertozzi CR
通讯作者：
Bertozzi CR
影响因子：
3.9
作者：
Annunziata, Ida;Bouche, Valentina;Ballabio, Andrea
通讯作者：
Ballabio, Andrea