Recent advances in zinc enzymology
Article Abstract:
The preference for zinc (Zn) in mononuclear and dinuclear metallopeptidases is due to the flexible coordination geometry, fast ligand exchange, polarizability and lack of redox activity of Zn. Zn ions play a major role in polarization of the electrophilic group and in the activation of the nucleophile for mono- and dinuclear metallohydrolases. Metalloenzyme catalysis controls the synthesis and degradation of the phosphodiester bond of DNA and RNA. The structure and mechanisms of Zn enzymes such as deaminases and dopachrome tautomerase are discussed.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 1996
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Comparison of the binuclear metalloenzymes diphosphoglycerate-independent phosphoglycerate mutase and alkaline phosphatase: their mechanism of catalysis via a phosphoserine interrmediate
Article Abstract:
The review discusses on some glycolytic enzymes such as 2,3-diphosphoglyceric acid independent phosphoglycerate mutase (iPGM), pyruvate kinase, and enolase with respect to their use of manganese, zinc, and magnesium to produce adenosine triphosphate. The focus of the article is iPGM from Bacillus stearothermophilus and alkaline phosphatase from Escherichia coli as binuclear metalloenzymes.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2001
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Biocatalysis in ionic liquids
Article Abstract:
The various issues related to biocatalysis in ionic liquids are reviewed. The effects of ionic liquids on the structure and activity of enzymes as well as on their thermal and operational stability are surveyed.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2007
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- Abstracts: Biomolecular solid state NMR: advances in structural methodology and applications to peptide and protein fibrils
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