1986/10/01 by Niggi Iberg, Rudolf Flückiger · 1 citation
Biochemistry, Genetics and Molecular Biology · Chemistry · Dentistry · Medicine · #Amadori rearrangement #Amino acid #Binding site #Biochemistry #Chemistry #Chronic Lymphocytic Leukemia Research #Glycation #Glycosylation #Glycosylation and Glycoproteins Research #Lysine #Oral Health Pathology and Treatment #Peptide sequence #Sequence (biology) #Stereochemistry
paper · doi:10.1016/s0021-9258(18)67052-8
openalex publication_date 1986/10/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
Nonenzymatic glycosylation of albumin in vivo occurs at multiple sites. Glucose gets attached to Lys-199, Lys-281, Lys-439, and Lys-525 as well as to some other lysine residues. The principal glycosylated site is Lys-525. Approximately 33% of the overall glycosylation occurs at this site. This site specificity is remarkable and is postulated to be a consequence of local catalysis of the nonenzymatic glycosylation reaction. It appears that positively charged amino groups in the protein catalyze the Amadori rearrangement at specific sites. The principal glycosylated site, Lys-525, lies in a Lys-Lys sequence; other glycosylated sites lie in a Lys-Lys, Lys-His, and Lys-His-Lys sequence or are near disulfide bridges, which are likely to place amino groups of more remote parts of the protein closer to these sites. The occurrence of nonenzymatic glycosylation at most of the identified sites in albumin from diabetic patients is explained by the concept of local acid-base catalysis of the Amadori rearrangement.