Catalytic mechanisms of metallohydrolases containing two metal ions

Mitić, Nataša, Miraula, Manfredi, Selleck, Christopher, Hadler, Kieran S., Uribe, Elena, Pedroso, M. M. and Schenk, G. (2014). Catalytic mechanisms of metallohydrolases containing two metal ions. In Christo Z. Christov (Ed.), Metal-containing enzymes (pp. 49-81) Waltham, MA, United States: Academic Press. doi:10.1016/bs.apcsb.2014.07.002

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Author Mitić, Nataša
Miraula, Manfredi
Selleck, Christopher
Hadler, Kieran S.
Uribe, Elena
Pedroso, M. M.
Schenk, G.
Title of chapter Catalytic mechanisms of metallohydrolases containing two metal ions
Title of book Metal-containing enzymes
Language of Book Title eng
Place of Publication Waltham, MA, United States
Publisher Academic Press
Publication Year 2014
Sub-type Article (original research)
DOI 10.1016/bs.apcsb.2014.07.002
Year available 2014
Series Advances in protein chemistry and structural biology
ISBN 9780128000120
9780128007884
ISSN 1876-1623
1876-1631
Editor Christo Z. Christov
Volume number 97
Chapter number 3
Start page 49
End page 81
Total pages 33
Total chapters 5
Language eng
Abstract/Summary At least one-third of enzymes contain metal ions as cofactors necessary for a diverse range of catalytic activities. In the case of polymetallic enzymes (i.e., two or more metal ions involved in catalysis), the presence of two (or more) closely spaced metal ions gives an additional advantage in terms of (i) charge delocalisation, (ii) smaller activation barriers, (iii) the ability to bind larger substrates, (iv) enhanced electrostatic activation of substrates, and (v) decreased transition-state energies. Among this group of proteins, enzymes that catalyze the hydrolysis of ester and amide bonds form a very prominent family, the metallohydrolases. These enzymes are involved in a multitude of biological functions, and an increasing number of them gain attention for translational research in medicine and biotechnology. Their functional versatility and catalytic proficiency are largely due to the presence of metal ions in their active sites. In this chapter, we thus discuss and compare the reaction mechanisms of several closely related enzymes with a view to highlighting the functional diversity bestowed upon them by their metal ion cofactors.
Formatted Abstract/Summary
At least one-third of enzymes contain metal ions as cofactors necessary for a diverse range of catalytic activities. In the case of polymetallic enzymes (i.e., two or more metal ions involved in catalysis), the presence of two (or more) closely spaced metal ions gives an additional advantage in terms of (i) charge delocalisation, (ii) smaller activation barriers, (iii) the ability to bind larger substrates, (iv) enhanced electrostatic activation of substrates, and (v) decreased transition-state energies. Among this group of proteins, enzymes that catalyze the hydrolysis of ester and amide bonds form a very prominent family, the metallohydrolases. These enzymes are involved in a multitude of biological functions, and an increasing number of them gain attention for translational research in medicine and biotechnology. Their functional versatility and catalytic proficiency are largely due to the presence of metal ions in their active sites. In this chapter, we thus discuss and compare the reaction mechanisms of several closely related enzymes with a view to highlighting the functional diversity bestowed upon them by their metal ion cofactors.
Keyword Binuclear metalloenzymes
Metallo-β-lactamases
Organophosphate-degrading enzymes
Aminopeptidases
Purple acid phosphatases
Agmatinases
Catalytic mechanisms
Metallo-beta-lactamases
Q-Index Code B1
Q-Index Status Confirmed Code
Institutional Status UQ
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Created: Thu, 07 Aug 2014, 23:47:44 EST by Associate Professor Gary Schenk on behalf of School of Chemistry & Molecular Biosciences