Identification of Catalytically Distinct Arylalkylamine N-acetyltransferase Splicoforms from Tribolium Castaneum

Overview

Journal Protein Expr Purif

Specialty Molecular Biology

Date 2020 Jul 19

PMID 32681959

Citations 1

Authors

Brian G OFlynn

Karin Claire Prins

Britney A Shepherd

Victoria E Forbrich

Gabriela Suarez

David J Merkler

Affiliations

Soon will be listed here.

Abstract

The assumption that structural or sequential homology between enzymes implies functional homology is a common misconception. Through in-depth structural and kinetic analysis, we are now beginning to understand the minute differences in primary structure that can alter the function of an enzyme completely. Alternative splicing is one method for which the activity of an enzyme can be controlled, simply by altering its length. Arylalkylamine N-acetyltransferase A (AANATA) in D. melanogaster, which catalyzes the N-acetylation of biogenic amines, has multiple splicoforms - alternatively spliced enzyme isoforms - with differing tissue distribution. As demonstrated here, AANAT1 from Tribolium castaneum is another such enzyme with multiple splicoforms. A screening assay was developed and utilized to determine that, despite only a 35 amino acid truncation, the shortened form of TcAANAT1 is a more active form of the enzyme. This implies regulation of enzyme metabolic activity via alternative splicing.

Citing Articles

Identification and characterization of a novel GNAT superfamily N -acetyltransferase from Salinicoccus halodurans H3B36.

Ma X, Jiang K, Zhou C, Xue Y, Ma Y Microb Biotechnol. 2022; 15(5):1652-1665.

PMID: 34985185 PMC: 9049628. DOI: 10.1111/1751-7915.13998.

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