Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine

被引：71

作者：

Miech, C ^{[1
]}

Dierks, T ^{[1
]}

Selmer, T ^{[1
]}

von Figura, K ^{[1
]}

Schmidt, B ^{[1
]}

机构：

[1] Univ Gottingen, Biochem Abt 2, D-37073 Gottingen, Germany

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1998年 / 273卷 / 09期

关键词：

D O I：

10.1074/jbc.273.9.4835

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：

Eukaryotic sulfatases share an unusual posttranslational protein modification, which converts a cysteine into alpha-formylglycine. The alpha-formylglycine is essential for the catalytic activity. Klebsiella pneumoniae expresses an inducible arylsulfatase for which the DNA predicts a serine at the position occupied by the alpha-formylglycine residue in eukaryotic sulfatases. Structural analysis showed that the majority of the arylsulfatase polypeptides from K. pneumoniae carries the alpha-formylglycine, whereas the remaining arylsulfatase polypeptides contain the predicted serine residue. This demonstrates the evolutionary conservation between prokaryotes and eukaryotes of this novel protein modification that so far has been found only in sulfatases. alpha-Formylglycine in Klebsiella is generated from a serine and not from a cysteine as in eukaryotes.

引用

页码：4835 / 4837

页数：3

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