@article {44647,
	title = {Dynamics of loops at the substrate entry channel determine the specificity of iridoid synthases},
	journal = {Febs Letters},
	volume = {592},
	year = {2018},
	month = {AUG},
	pages = {2624-2635},
	abstract = {<p>Iridoid synthases belong to the family of short-chain dehydrogenase reductase involved in the biosynthesis of iridoids. Despite having high sequence and structural homology with progesterone 5 beta- reductase, these enzymes exhibit differential substrate specificities. Previously, two loops. L1 and L2 at substrate-binding pocket, were suggested to be involved in generating substrate specificity. However, the structural basis of specificity determinants was elusive. Here, combining sequence and structural analysis, site-directed mutagenesis, and molecular dynamics simulations, we have shown that iridoid synthase contains two channels for substrate entry whose geometries are altered by L1-L2 dynamics, primarily orchestrated by interactions of residues Glu161 and Gly162 of L1 and Asn358 of L2. A complex interplay of these interactions confer the substrate specificity to the enzyme.</p>},
	keywords = {iridoid synthase, iridoids, Molecular dynamics simulations, progesterone 5 beta-reductase, Substrate specificity},
	issn = {1873-3468},
	doi = {10.1002/1873-3468.13174},
	author = {Sandholu, Anand S. and Mohole, Madhura and Duax, William L. and Thulasiram, Hirekodathakallu V. and Sengupta, Durba and Kulkarni, Kiran}
}
