Remarkably different structures and reaction mechanisms of ketoreductases for the opposite stereochemical control in the biosynthesis of BIQ antibiotics

Taguchi, Takaaki, Kunieda, Kanako, Takeda-Shitaka, Mayuko, Takaya, Daisuke, Kawano, Noriaki, Kimberley, Meriel R., Booker-Milburn, Kevin I., Stephenson, G. Richard ORCID: https://orcid.org/0000-0003-1487-9178, Umeyama, Hideaki, Ebizuka, Yutaka and Ichinose, Koji (2004) Remarkably different structures and reaction mechanisms of ketoreductases for the opposite stereochemical control in the biosynthesis of BIQ antibiotics. Bioorganic & Medicinal Chemistry, 12 (22). pp. 5917-5927. ISSN 0968-0896

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Abstract

Two ketoreductases, RED1 and RED2, are involved in the biosynthesis of actinorhodin in Streptomyces coelicolor A3(2) and dihydrogranaticin in S. violaceoruher Tu22 respectively. They are responsible for the stereospecific reductions of the bicyclic intermediate to give (S)- or (R)-DNPA although there is no similarity between their amino acid sequences. Biotransformation using synthetic analogous substrates revealed that the substrate specificities are quite different. Homology modelling studies and site directed mutagenesis showed remarkable differences in three-dimensional structures and catalytic mechanisms between RED1 and RED2. (C) 2004 Elsevier Ltd. All rights reserved.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Chemistry
UEA Research Groups:	Faculty of Science > Research Groups > Synthetic Chemistry (former - to 2017) Faculty of Science > Research Groups > Chemistry of Materials and Catalysis
Depositing User:	Rachel Smith
Date Deposited:	08 Jun 2011 11:08
Last Modified:	24 Oct 2022 02:47
URI:	https://ueaeprints.uea.ac.uk/id/eprint/32007
DOI:	10.1016/j.bmc.2004.08.026

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