Open AccessLysine carboxylation: unveiling a spontaneous post‐translational modification
Author(s) -
JimenezMorales David,
Adamian Larisa,
Shi Dashuang,
Liang Jie
Publication year - 2014
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s139900471302364x
Subject(s) - carboxylation , lysine , proteome , posttranslational modification , biochemistry , chemistry , enzyme , residue (chemistry) , computational biology , biology , amino acid , catalysis
The carboxylation of lysine residues is a post‐translational modification (PTM) that plays a critical role in the catalytic mechanisms of several important enzymes. It occurs spontaneously under certain physicochemical conditions, but is difficult to detect experimentally. Its full impact is unknown. In this work, the signature microenvironment of lysine‐carboxylation sites has been characterized. In addition, a computational method called Predictor of Lysine Carboxylation ( PreLysCar ) for the detection of lysine carboxylation in proteins with available three‐dimensional structures has been developed. The likely prevalence of lysine carboxylation in the proteome was assessed through large‐scale computations. The results suggest that about 1.3% of large proteins may contain a carboxylated lysine residue. This unexpected prevalence of lysine carboxylation implies an enrichment of reactions in which it may play functional roles. The results also suggest that by switching enzymes on and off under appropriate physicochemical conditions spontaneous PTMs may serve as an important and widely used efficient biological machinery for regulation.