<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sandholu, Anand S.</style></author><author><style face="normal" font="default" size="100%">Mohole, Madhura</style></author><author><style face="normal" font="default" size="100%">Duax, William L.</style></author><author><style face="normal" font="default" size="100%">Thulasiram, Hirekodathakallu V.</style></author><author><style face="normal" font="default" size="100%">Sengupta, Durba</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Kiran</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Dynamics of loops at the substrate entry channel determine the specificity of iridoid synthases</style></title><secondary-title><style face="normal" font="default" size="100%">Febs Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">iridoid synthase</style></keyword><keyword><style  face="normal" font="default" size="100%">iridoids</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular dynamics simulations</style></keyword><keyword><style  face="normal" font="default" size="100%">progesterone 5 beta-reductase</style></keyword><keyword><style  face="normal" font="default" size="100%">Substrate specificity</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">592</style></volume><pages><style face="normal" font="default" size="100%">2624-2635</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">15</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.623</style></custom4></record></records></xml>