N-acetyltransferases from three different organisms displaying distinct selectivity toward hexosamines and N-terminal amine of peptides. (15th January 2019)

• Record Type: Journal Article
• Authors: Zhang, Peiru; Liu, Pei; Xu, Yangyang; Liang, Yulu; Wang, Peng George; Cheng, Jiansong
• Is Part Of: Carbohydrate research. Volume 472(2019)
• Page Start: 72
• Page End: 75
• Publication Date: 2019-01-15
• Subjects: N-acetyltransferase -- Acetylation -- Glucosamine -- Peptide -- Specificity; Carbohydrates -- Periodicals; Chemistry, Organic -- Periodicals; Biochemistry -- Periodicals; Carbohydrates -- Periodicals; Chimie organique -- Périodiques; Glucides -- Périodiques; Biochemistry; Carbohydrates; Chemistry, Organic; Periodicals; Electronic journals; 507.78
• DOI: 10.1016/j.carres.2018.11.011
• Languages: English
• ISSNs: 0008-6215

Abstract

Abstract: N-acetyltransferases are a family of enzymes that catalyze the transfer of the acetyl moiety (COCH3 ) from acetyl coenzyme A (Acetyl-CoA) to a primary amine of acceptor substrates from small molecules such as aminoglycoside to macromolecules of various proteins. In this study, the substrate selectivity of three N-acetyltransferases falling into different phylogenetic groups was probed against a series of hexosamines and synthetic peptides. GlmA from Clostridium acetobutylicum and RmNag from Rhizomucor miehei, which have been defined as glucosamine N-acetyltransferases, were herein demonstrated to be also capable of acetylating the free amino group on the very first glycine residue of peptide in spite of varied catalytic efficiency. The human recombinant N-acetyltransferase of Naa10p, however, prefers primary amine groups in the peptides as opposed to glucosamine. The varied preference of GlmA, RmNag and Naa10p probably arose from the divergent evolution of these N-acetyltransferases. The expanded knowledge of acceptor specificity would as well facilitate the application of these N-acetyltransferases in the acetylation of hexosamines or peptides. Graphical abstract: Highlights: N-acetyltransferases of GlmA, RmNag and Naa10p are distantly related. RmNag from Rhizomucor miehei exhibits comparable activity toward GlcN and peptides with Gly N-termini. GlmA from Clostridium acetobutylicum exhibits much more efficiency for GlcN as opposed to Gly-starting peptides. Naa10p is predominantly active toward peptides starting with acidic residues as opposed to GlcN.