PLP-Dependent Enzymes

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منابع مشابه

PLP-Dependent Enzymes

The main focus of this special issue is on structural, functional, and biomedical studies on pyridoxal-5-phosphate(PLP-) dependent enzymes. The unparalleled catalytic versatility of PLP, the active form of vitamin B6, originates from its unique electron-sinking properties, which stabilize reaction intermediates, thus lowering the activation barrier during catalysis. At least five different prot...

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Functional evolution of PLP-dependent enzymes based on active-site structural similarities.

Families of distantly related proteins typically have very low sequence identity, which hinders evolutionary analysis and functional annotation. Slowly evolving features of proteins, such as an active site, are therefore valuable for annotating putative and distantly related proteins. To date, a complete evolutionary analysis of the functional relationship of an entire enzyme family based on ac...

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PLP-dependent Enzymes: a Powerful Tool for Metabolic Synthesis of Non-canonical Amino Acids

An Overview on PLP-dependent Enzymes Pyridoxal 5’-phosphate (PLP), the biologically active of vitamin B6, was first identified in the mid-forties as the cofactor for the transamination reaction. Since then, PLP-dependent enzymes have been the focus of extensive biochemical research. The interest aroused by these enzymes is due to their unrivalled catalytic versatility and their widespread invol...

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A Strategy for Detection of Structural Conserved Regions and Contacts in Protein Superfamilies: Application to the PLP-Dependent Enzymes

During the last few years, structural and genomic projects provided us with a wealth of biological information that now opens new prospects of understanding life and evolution at the molecular level [1]. In the next future, one of the main challenges will be the organization and the interpretation of this exponentially growing amount of data. In this work, we show how the rational application o...

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ژورنال

عنوان ژورنال: BioMed Research International

سال: 2014

ISSN: 2314-6133,2314-6141

DOI: 10.1155/2014/856076