Formylglycine, a Post-Translationally Generated Residue with Unique Catalytic Capabilities and Biotechnology Applications

被引：123

作者：

Appel, Mason J. ^{[1
]}

Bertozzi, Carolyn R. ^{[1
,2
,3
]}

机构：

[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA

[3] Univ Calif Berkeley, Howard Hughes Med Inst, Berkeley, CA 94720 USA

来源：

ACS CHEMICAL BIOLOGY | 2015年 / 10卷 / 01期

关键词：

MULTIPLE SULFATASE DEFICIENCY; ALKALINE-PHOSPHATASE SUPERFAMILY; ALDEHYDE-TAGGED PROTEINS; PICTET-SPENGLER LIGATION; HUMAN ARYLSULFATASE-A; ENDOPLASMIC-RETICULUM; CRYSTAL-STRUCTURE; PSEUDOMONAS-AERUGINOSA; CHEMICAL-MODIFICATION; LYSOSOMAL SULFATASE;

D O I：

10.1021/cb500897w

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：72 / 84

页数：13

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