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

Takaaki Taguchi; Kanako Kunieda; Mayuko Takeda-Shitaka; Daisuke Takaya; Noriaki Kawano; Meriel R. Kimberley; Kevin I. Booker-Milburn; G. Richard Stephenson; Hideaki Umeyama; Yutaka Ebizuka; Koji Ichinose

doi:10.1016/j.bmc.2004.08.026

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

Takaaki Taguchi, Kanako Kunieda, Mayuko Takeda-Shitaka, Daisuke Takaya, Noriaki Kawano, Meriel R. Kimberley, Kevin I. Booker-Milburn, G. Richard Stephenson, Hideaki Umeyama, Yutaka Ebizuka, Koji Ichinose

Chemistry of Materials and Catalysis

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

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.

Original language	English
Pages (from-to)	5917-5927
Number of pages	11
Journal	Bioorganic & Medicinal Chemistry
Volume	12
Issue number	22
DOIs	https://doi.org/10.1016/j.bmc.2004.08.026
Publication status	Published - 2004

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10.1016/j.bmc.2004.08.026

Cite this

Taguchi, T., Kunieda, K., Takeda-Shitaka, M., Takaya, D., Kawano, N., Kimberley, M. R., Booker-Milburn, K. I., Stephenson, G. R., Umeyama, H., Ebizuka, Y., & Ichinose, K. (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), 5917-5927. https://doi.org/10.1016/j.bmc.2004.08.026

@article{6f8671e7d13a4a4fb9dbd99092f6d236,

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

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.",

author = "Takaaki Taguchi and Kanako Kunieda and Mayuko Takeda-Shitaka and Daisuke Takaya and Noriaki Kawano and Kimberley, {Meriel R.} and Booker-Milburn, {Kevin I.} and Stephenson, {G. Richard} and Hideaki Umeyama and Yutaka Ebizuka and Koji Ichinose",

year = "2004",

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language = "English",

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publisher = "Elsevier",

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Taguchi, T, Kunieda, K, Takeda-Shitaka, M, Takaya, D, Kawano, N, Kimberley, MR, Booker-Milburn, KI, Stephenson, GR, Umeyama, H, Ebizuka, Y & Ichinose, K 2004, 'Remarkably different structures and reaction mechanisms of ketoreductases for the opposite stereochemical control in the biosynthesis of BIQ antibiotics', Bioorganic & Medicinal Chemistry, vol. 12, no. 22, pp. 5917-5927. https://doi.org/10.1016/j.bmc.2004.08.026

TY - JOUR

T1 - Remarkably different structures and reaction mechanisms of ketoreductases for the opposite stereochemical control in the biosynthesis of BIQ antibiotics

AU - Taguchi, Takaaki

AU - Kunieda, Kanako

AU - Takeda-Shitaka, Mayuko

AU - Takaya, Daisuke

AU - Kawano, Noriaki

AU - Kimberley, Meriel R.

AU - Booker-Milburn, Kevin I.

AU - Stephenson, G. Richard

AU - Umeyama, Hideaki

AU - Ebizuka, Yutaka

AU - Ichinose, Koji

PY - 2004

Y1 - 2004

N2 - 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.

AB - 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.

U2 - 10.1016/j.bmc.2004.08.026

DO - 10.1016/j.bmc.2004.08.026

M3 - Article

VL - 12

SP - 5917

EP - 5927

JO - Bioorganic & Medicinal Chemistry

JF - Bioorganic & Medicinal Chemistry

SN - 0968-0896

IS - 22

ER -