An insight into the sequential, structural and phylogenetic properties of banana 1-aminocyclopropane-1-carboxylate synthase 1 and study of its interaction with pyridoxal-5'-phosphate and aminoethoxyvinylglycine

Journal of biosciences

Sujit Roy²  Swarup Roy Choudhury¹  Sanjay Kumar Singh¹  Dibyendu N Sengupta1¹ 

[1] Department of Botany, Bose Institute, 93/1, APC Road, Kolkata 700 009$$;Protein Chemistry Laboratory, Department of Chemistry, Bose Institute, 93/1, A.P.C Road, Kolkata 700 009$$

关键词: ACC synthase;    aminoethoxyvinylglycine;    ethylene;    ligand binding;    pyridoxal-5'-phosphate;    S-adenosyl-L-methionine;   

DOI  :  

来源: Indian Academy of Sciences

【 摘 要 】

In banana, ethylene production for ripening is accompanied by a dramatic increase in 1-aminocyclopropane-1-carboxylate (ACC) content, transcript level of Musa acuminata ACC synthase 1 (MA-ACS1) and the enzymatic activity of ACC synthase 1 at the onset of the climacteric period. MA-ACS1 catalyses the conversion of 𝑆-adenosyl-L-methionine (SAM) to ACC, the key regulatory step in ethylene biosynthesis. Multiple sequence alignments of 1-aminocyclopropane-1-carboxylate synthase (ACS) amino acid sequences based on database searches have indicated that MA-ACS1 is a highly conserved protein across the plant kingdom. This report describes an in silico analysis to provide the first important insightful information about the sequential, structural and phylogenetic characteristics of MA-ACS1. The three-dimensional structure of MA-ACS1, constructed based on homology modelling, in combination with the available data enabled a comparative mechanistic analysis of MA-ACS1 to explain the catalytic roles of the conserved and non-conserved active site residues. We have further demonstrated that, as in apple and tomato, banana-ACS1 (MA-ACS1) forms a homodimer and a complex with cofactor pyridoxal-5′-phosphate (PLP) and inhibitor aminoethoxyvinylglycine (AVG). We have also predicted that the residues from the PLP-binding pocket, essential for ligand binding, are mostly conserved across the MA-ACS1 structure and the competitive inhibitor AVG binds at a location adjacent to PLP.

【 授权许可】

Unknown