Possible Interaction: Aspartic Acid and Serine

“Mutation of serine to other amino acids with varying side chains: alanine, methionine, leucine, aspartic acid , asparagine, and arginine also resulted in significant activation, indicating a serine-specific inhibitory effect.”

“The substitution of serines at positions 51, 66, 76, and 91 with aspartic acid to mimic the phosphorylated enzyme hampers the association of DNA ligase I with the replication foci.”

“The negative charge of aspartic acid is believed to be able to mimic the phosphorylation state of serine , while alanine is a commonly used residue to substitute serine due to their similar structure.”

“Replacing either the serine or threonine with aspartic acid reduces surface expression and function, whereas substitution with neutral alanine has no effect on surface expression or function.”

“Mutagenesis of this serine to an aspartic acid resulted in an increase in DNA binding and transcriptional activity of MEF2C comparable to that observed when this site was phosphorylated, suggesting that phosphorylation augments DNA binding activity by introducing negative charge.”

“In the present study we have determined that replacement of Ser of CREB with Asp greatly decreases the ability of the cAMP-dependent protein kinase to activate CREB.”

“Excesses of aspartic acid and serine inhibited this reaction.”

“Mutagenesis of both serines to aspartic acid (phospho-mimetic), but not alanine (phospho-dead), results in approximately 80% reduction in nucleolar localization of BLM while retaining the biochemical functions and nuclear localization of BLM.”

“The formation of a strong hydrogen bond between His and Asp was shown to be important in lowering the activation energy in the reaction of Ser with substrate.”