Non-Enzymatic Glycation of Aminotransferases and the Possibilities of Its Modulation

Boušová, Iva; Srbová, Lenka; Dršata, J

doi:10.5772/34924

Cited by 2 publications

(2 citation statements)

References 65 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The remaining lysine (4.77%) establishes a spatial association with an arginine residue. The maximum (Boušová et al, 2012) ** = Presence of other nearby basic residue in the primary sequence or in the tertiary structure.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Prediction of glycation sites: new insights from protein structural analysis

Suarez¹,

Poutou-Piñales²,

Santos³

et al. 2016

Turk J Biol

View full text Add to dashboard Cite

Glycation of proteins is a nonenzymatic process in which proteins react with reducing sugar molecules. This process takes place at ε-amino (ε-NH +) groups of lysine or hydroxylysine residues as well as α-amino groups of N-terminal residues. In the present study glycation of ε-NH + groups of lysines was computationally analyzed for 26 proteins based on their 3D structures. We determined the spatial relationship with acidic or basic residues and correlated them with the glycation prediction algorithm Netglycate 1.0 software, which employed primary structure exclusively for glycation site prediction. Of the lysines from 19 of the 20 proteins employed to build the Netglycate 1.0 algorithm 87.80% depicted a spatial relationship with acidic or basic residues. For the remaining seven proteins that were not included in the algorithm, 95.23% of the lysines exhibited a spatial relationship with acidic or basic residues. For these seven proteins, Netglycate 1.0 predicted only 52.38% of the lysines with a previously reported experimental glycation as potential glycation sites. In all cases, distances between residues were less than or equal to 9.78 Å. These results suggest that it is the spatial relationship of lysines with acidic or basic residues in the 3D conformation of a protein that determines the glycation target site, rather than a specific sequence of the primary structure.

show abstract

Section: Resultsmentioning

confidence: 99%

“…Spatial relationship between glycated lysine and acidic or basic residues in the tertiary structure for proteins not used in developing the Netglycate 1.0 algorithm. (Boušová et al, 2012) ** = Presence of other nearby basic residue in the primary sequence or in the tertiary structure.…”

Section: Protein Uniprotkb (Ac)mentioning

confidence: 99%

Prediction of glycation sites: new insights from protein structural analysis

Suarez¹,

Poutou-Piñales²,

Santos³

et al. 2016

Turk J Biol

View full text Add to dashboard Cite

show abstract

Oxidation as an important factor of protein damage: Implications for Maillard reaction

2015

View full text Add to dashboard Cite

Protein oxidation, the process caused especially by reactive oxygen and nitrogen species, is thought to play a major role in various oxidative processes within cells and is implicated in the development of many human diseases. This review provides a brief overview of the protein oxidation with the emphasis on the types of oxidation (oxidation of protein backbone and amino acid residues side chains, site-specific metal-catalysed protein oxidation), oxidationdependent generation of protein hydroperoxides, carbonyl derivatives and protein-protein cross-linkages. Nonenzymatic glycoxidation (also known as Maillard reaction) as an important factor of protein damage, consequences of oxidative protein impairment and related diseases as well as means of monitoring and assessment of protein modifications are discussed.

show abstract

Non-Enzymatic Glycation of Aminotransferases and the Possibilities of Its Modulation

Cited by 2 publications

References 65 publications

Prediction of glycation sites: new insights from protein structural analysis

Prediction of glycation sites: new insights from protein structural analysis

Oxidation as an important factor of protein damage: Implications for Maillard reaction

Contact Info

Product

Resources

About