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J Proteomics. 2013 Oct 30;92:80-109. doi: 10.1016/j.jprot.2013.03.025. Epub 2013 Apr 17.

Effect of posttranslational modifications on enzyme function and assembly.

Author information

1
Department of Biochemistry, Faculty of Science, Charles University in Prague, Hlavova 8, CZ-12840 Prague 2, Czech Republic. Electronic address: helena.ryslava@natur.cuni.cz.

Abstract

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. This article is part of a Special Issue entitled: Posttranslational Protein modifications in biology and Medicine.

KEYWORDS:

ABRF; AGE; ALE; AML; APC/C; Association for Biomolecular Resource Facilities; CCT; CDK; CHO; COS-1; CSC; CV-1 in Origin carrying SV40 genetic material (cell line); Catalytic activity; Cellular localization; Chinese hamster ovary; EC; ECD; EGF; ER-associated protein degradation; ERAD; Enzyme; GFP; HECT; HEK; IP3; MDM; MMP; MRM; Posttranslational modification; RAGE; RING; RNS; S-adenosyl-l-homocysteine; S-adenosyl-l-methionine; SAH; SAM; SIL; Stability; Structure; TAS; TCP-1; acute myeloid leukemia; advanced glycosylation endproduct; advanced lipooxidation endproduct; anaphase-promoting complex/cyclosome; cell surface capture technology; chaperone containing TCP-1; cyclin-dependent kinase; electron capture dissociation; enzyme commission of IUPAC; epidermal growth factor; green fluorescent protein; homologous to the E6-AP carboxyl terminus; human embryonic kidney; inositoltrisphosphate; matrix metalloproteinase; multiple reaction monitoring; murine double minute; reactive nitrogen species; really interesting new gene; receptor for advanced glycosylation end products; stable isotope labeling; tagging via substrate approach; tailless complex polypeptide-1

PMID:
23603109
DOI:
10.1016/j.jprot.2013.03.025
[Indexed for MEDLINE]

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