868077-89-8Relevant academic research and scientific papers
Selective Targeting of AF9 YEATS Domain by Cyclopeptide Inhibitors with Preorganized Conformation
Jiang, Yixiang,Chen, Guochao,Li, Xiao-Meng,Liu, Sha,Tian, Gaofei,Li, Yuanyuan,Li, Xin,Li, Haitao,Li, Xiang David
supporting information, p. 21450 - 21459 (2021/01/11)
YEATS domains are newly identified epigenetic "readers"of histone lysine acetylation (Kac) and crotonylation (Kcr). The malfunction of YEATS-Kac/Kcr interactions has been found to be involved in the pathogenesis of human diseases, such as cancer. These di
Stereochemistry of reactions of the inhibitor/substrates L- And D-β-chloroalanine with β-mercaptoethanol catalysed by L-aspartate aminotransferase and D-amino acid aminotransferase respectively
Adams, Benjamin,Lowpetch, Kreingkrai,Thorndycroft, Faye,Whyte, Sheena M.,Young, Douglas W.
, p. 3357 - 3364 (2007/10/03)
Two members of the α-family of PLP-dependent enzymes, L-aspartate aminotransferase and D-amino acid aminotransferase, have been shown to catalyse β-substitution of L- and D-β-chloroalanine respectively with β-mercaptoethanol, reactions typical of the β-family of PLP-dependent enzymes. The reaction catalysed by L-aspartate aminotransferase has been shown to occur with retention of stereochemistry, a typical outcome for reactions catalysed by β-family enzymes. There are also indications that the reaction catalysed by D-amino acid aminotransferase may involve retention of stereochemistry. Both enzymes have been shown to catalyse exchange at C-3 when the appropriate enantiomer of β-chloroalanine is the substrate. The Royal Society of Chemistry 2005.
