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4 article(s) from Abe, Ikuro

Structural basis for endoperoxide-forming oxygenases

Takahiro Mori and
Ikuro Abe

Beilstein J. Org. Chem. 2022, 18, 707–721, doi:10.3762/bjoc.18.71

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Graphical Abstract

Figure 1: Examples of endoperoxide-containing natural products.

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Scheme 1: Reactions of COXs.

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Figure 2: Structures of COXs [52,53]. (A) The overall structure of ovine COX-1. (B and C) Comparison of the cyclooxy...

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Scheme 2: Proposed reaction mechanisms of COXs [24].

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Scheme 3: General reaction mechanism of Fe/2OG oxygenases.

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Scheme 4: Reaction of FtmOx1 [68-71].

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Figure 3: Structure of FtmOx1 [71]. (A) The FtmOx1 binary structure in complex with 2OG. (B and C) Comparison of ...

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Scheme 5: Proposed COX-like mechanism of FtmOx1 [68].

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Scheme 6: Proposed CarC-like mechanism of FtmOx1 [70].

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Scheme 7: Reaction of NvfI [28].

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Scheme 8: Possible reaction pathways leading to fumigatonoid A [28].

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Figure 4: Structure of NvfI [28]. (A–C) Conformational changes of loop regions: (A) open conformation, (B) partia...

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Scheme 9: Another possible reaction pathway for the formation of fumigatonoid A [28].

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Album

Review

Published 21 Jun 2022

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Inherent atomic mobility changes in carbocation intermediates during the sesterterpene cyclization cascade

Hajime Sato,
Takaaki Mitsuhashi,
Mami Yamazaki,
Ikuro Abe and
Masanobu Uchiyama

Beilstein J. Org. Chem. 2019, 15, 1890–1897, doi:10.3762/bjoc.15.184

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Scheme 1: The regio- and stereoselectivity in quiannulatene and sesterfisherol biosynthesis are determined by...

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Scheme 2: Reaction mechanism of quiannulatene biosynthesis. GFPP: geranylfarnesyl diphosphate, IM: intermedia...

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Scheme 3: Reaction mechanisms of sesterfisherol biosynthesis. Sesterfisherol is formed by the hydration of IM...

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Figure 1: Energy diagram and heat map analysis of 5/12/5 tricycle formation (A) IM1–IM4 in quiannulatene bios...

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Figure 2: Energy diagram and heat map analysis of conformational change and hydrogen shift (A) IM4–IM6e in qu...

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Figure 3: Energy diagram and heat map analysis of ring rearrangement (A) IM6e–IM11 in quiannulatene biosynthe...

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Album

Supp Info

Letter

Published 07 Aug 2019

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Molecular basis for the plasticity of aromatic prenyltransferases in hapalindole biosynthesis

Takayoshi Awakawa and
Ikuro Abe

Beilstein J. Org. Chem. 2019, 15, 1545–1551, doi:10.3762/bjoc.15.157

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Graphical Abstract

Figure 1: The reactions of aromatic PTases.

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Figure 2: The reactions catalyzed by AmbP1 (A) and AmbP3 (B).

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Figure 3: The overall structure of apo-AmbP1 (A), the Mg²⁺-free structure (B), and the Mg²⁺-bound structure (...

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Figure 4: The active site structure of AmbP1. 1 and GSPP were bound in the active site without Mg²⁺ (A, Mg²⁺-...

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Figure 5: The active site structure of AmbP3 with substrates. The AmbP3 structure in complex with hapalindole...

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Figure 6: Multiple amino acid sequence alignment of AmbP1, AmbP3, and other ABBA PTases, visualized by ESPrip...

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Album

Review

Published 11 Jul 2019

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Posttranslational isoprenylation of tryptophan in bacteria

Masahiro Okada,
Tomotoshi Sugita and
Ikuro Abe

Beilstein J. Org. Chem. 2017, 13, 338–346, doi:10.3762/bjoc.13.37

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Figure 1: (A) Schematic representation of pheromone-induced conjugation tube formation for mating in Tremella...

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Figure 2: Chemical structures of (A) surfactin A and (B) poly-γ-glutamic acid.

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Figure 3: (A) Two types of posttranslational isoprenylations of ComX variants. The modified tryptophan residu...

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Figure 4: (A) Schematic representation of the signal transduction cascade of quorum sensing stimulated by the...

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Figure 5: Amino acid sequences of ComX from seven Bacillus strains. The sequences of the mature pheromones ar...

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Figure 6: Chemical structure of kawaguchipeptin A. Dimethylallylated tryptophan residues are colored blue.

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Album

Review

Published 22 Feb 2017

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