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The ɛ-Amino Group of Protein Lysine Residues Is Highly Susceptible to Nonenzymatic Acylation by Several Physiological Acyl-CoA Thioesters.
- Source :
-
Chembiochem : a European journal of chemical biology [Chembiochem] 2015 Nov 02; Vol. 16 (16), pp. 2337-47. Date of Electronic Publication: 2015 Sep 18. - Publication Year :
- 2015
-
Abstract
- Mitochondrial enzymes implicated in the pathophysiology of diabetes, cancer, and metabolic syndrome are highly regulated by acetylation. However, mitochondrial acetyltransferases have not been identified. Here, we show that acetylation and also other acylations are spontaneous processes that depend on pH value, acyl-CoA concentration and the chemical nature of the acyl residue. In the case of a peptide derived from carbamoyl phosphate synthetase 1, the rates of succinylation and glutarylation were up to 150 times than for acetylation. These results were confirmed by using the protein substrate cyclophilin A (CypA). Deacylation experiments revealed that SIRT3 exhibits deacetylase activity but is not able to remove any of the succinyl groups from CypA, whereas SIRT5 is an effective protein desuccinylase. Thus, the acylation landscape on lysine residues might largely depend on the enzymatic activity of specific sirtuins, and the availability and reactivity of acyl-CoA compounds.<br /> (© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
- Subjects :
- Acylation
Amines chemistry
Amines metabolism
Crystallography, X-Ray
Cyclophilin A chemistry
Cyclophilin A metabolism
Humans
Kinetics
Lysine chemistry
Mitochondria metabolism
Molecular Conformation
Peptides chemistry
Recombinant Proteins biosynthesis
Recombinant Proteins chemistry
Sirtuin 3 chemistry
Sirtuin 3 genetics
Sirtuins chemistry
Sirtuins genetics
Sirtuins metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Thermodynamics
Acyl Coenzyme A metabolism
Lysine metabolism
Peptides metabolism
Sirtuin 3 metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1439-7633
- Volume :
- 16
- Issue :
- 16
- Database :
- MEDLINE
- Journal :
- Chembiochem : a European journal of chemical biology
- Publication Type :
- Academic Journal
- Accession number :
- 26382620
- Full Text :
- https://doi.org/10.1002/cbic.201500364