Effect of posttranslational modifications on enzyme function and assembly

0422889 - MBÚ 2014 RIV NL eng J - Journal Article
Ryšlavá, H. - Doubnerová, V. - Kavan, Daniel - Vaněk, O.
Effect of posttranslational modifications on enzyme function and assembly.
Journal of Proteomics. Roč. 92, OCT 2013 (2013), s. 80-109. ISSN 1874-3919. E-ISSN 1876-7737
R&D Projects: GA ČR(CZ) GAP207/10/1040; GA ČR GA303/09/0477; GA ČR GD305/09/H008; GA ČR(CZ) GAP504/11/0394
Institutional support: RVO:61388971
Keywords : Enzyme * Posttranslational modification * Structure
Subject RIV: CB - Analytical Chemistry, Separation
Impact factor: 3.929, year: 2013

The detailed examination of enzyme molecules by mass spectrometry and other techniques continues to identify hundreds of distinct PTMs. Recently, global analyses of enzymes using methods of contemporary proteomics revealed widespread distribution of PTMs on many key enzymes distributed in all cellular compartments. Critically, patterns of multiple enzymatic and nonenzymatic PTMs within a single enzyme are now functionally evaluated providing a holistic picture of a macromolecule interacting with low molecular mass compounds, some of them being substrates, enzyme regulators, or activated precursors for enzymatic and nonenzymatic PTMs. Multiple PTMs within a single enzyme molecule and their mutual interplays are critical for the regulation of catalytic activity. Full understanding of this regulation will require detailed structural investigation of enzymes, their structural analogs, and their complexes. Further, proteomics is now integrated with molecular genetics, transcriptomics, and other areas leading to systems biology strategies. These allow the functional interrogation of complex enzymatic networks in their natural environment. In the future, one might envisage the use of robust high throughput analytical techniques that will be able to detect multiple PTMs on a global scale of individual proteomes from a number of carefully selected cells and cellular compartments
Permanent Link: http://hdl.handle.net/11104/0229024