AphA is a magnesium-dependent, bacterial class B acid phosphatase that catalyzes the hydrolysis of a variety of phosphoester substrates and belongs to the DDDD superfamily of phosphohydrolases. The recently reported crystal structure of AphA from Escherichia coli has revealed the quaternary structure of the enzyme together with hints about its catalytic mechanism. The present work reports the crystal structures of AphA from E. coli in complex with substrate, transition-state, and intermediate analogues. The structures provide new insights into the mechanism of the enzyme and allow a revision of some aspects of the previously proposed mechanism that have broader implications for all the phosphatases of the DDDD superfamily. (C) 2008 Elsevier Ltd. All rights reserved.

Leone, R., Cappelletti, E., Benvenuti, M., Lentini, G., Thaller, M.C., & Mangani, S. (2008). Structural Insights into the Catalytic Mechanism of the Bacterial Class B Phosphatase AphA Belonging to the DDDD Superfamily of Phosphohydrolases. JOURNAL OF MOLECULAR BIOLOGY, 384(2), 478-488 [10.1016/j.jmb.2008.09.050].

Structural Insights into the Catalytic Mechanism of the Bacterial Class B Phosphatase AphA Belonging to the DDDD Superfamily of Phosphohydrolases

THALLER, MARIA CRISTINA;
2008

Abstract

AphA is a magnesium-dependent, bacterial class B acid phosphatase that catalyzes the hydrolysis of a variety of phosphoester substrates and belongs to the DDDD superfamily of phosphohydrolases. The recently reported crystal structure of AphA from Escherichia coli has revealed the quaternary structure of the enzyme together with hints about its catalytic mechanism. The present work reports the crystal structures of AphA from E. coli in complex with substrate, transition-state, and intermediate analogues. The structures provide new insights into the mechanism of the enzyme and allow a revision of some aspects of the previously proposed mechanism that have broader implications for all the phosphatases of the DDDD superfamily. (C) 2008 Elsevier Ltd. All rights reserved.
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore CHIM/03 - Chimica Generale e Inorganica
Settore BIO/19 - Microbiologia Generale
Settore MED/07 - Microbiologia e Microbiologia Clinica
English
Con Impact Factor ISI
bacterial phosphatase; catalytic mechanism; class B phosphatase; crystal structure; DDDD phosphohydrolase superfamily
Leone, R., Cappelletti, E., Benvenuti, M., Lentini, G., Thaller, M.C., & Mangani, S. (2008). Structural Insights into the Catalytic Mechanism of the Bacterial Class B Phosphatase AphA Belonging to the DDDD Superfamily of Phosphohydrolases. JOURNAL OF MOLECULAR BIOLOGY, 384(2), 478-488 [10.1016/j.jmb.2008.09.050].
Leone, R; Cappelletti, E; Benvenuti, M; Lentini, G; Thaller, Mc; Mangani, S
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/29086
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