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Search for "conserved motifs" in Full Text gives 11 result(s) in Beilstein Journal of Organic Chemistry.

Bioinformatic prediction of the stereoselectivity of modular polyketide synthase: an update of the sequence motifs in ketoreductase domain

  • Changjun Xiang,
  • Shunyu Yao,
  • Ruoyu Wang and
  • Lihan Zhang

Beilstein J. Org. Chem. 2024, 20, 1476–1485, doi:10.3762/bjoc.20.131

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  • medicines such as erythromycin and rapamycin. They are often rich in stereocenters biosynthesized by the ketoreductase (KR) domain within the polyketide synthase (PKS) assembly line. Previous studies have identified conserved motifs in KR sequences that enable the bioinformatic prediction of product
  • : bioinformatics; conserved motifs; ketoreductase; polyketide synthase; stereocontrol; Introduction Type I modular polyketide synthases (PKSs) are large enzyme complexes that play a crucial role in the biosynthesis of bacterial polyketides, including many important clinical drugs such as erythromycin (antibiotic
  • binding motif can be used to predict C2-type KRs [9]. These conserved motifs have been widely used to predict the stereochemical outcome of modular cis-AT PKSs and have facilitated bioinformatics-guided structural determination of complex polyketides [12][13][14][15][16][17]. However, despite being widely
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Published 02 Jul 2024

Enhancing structural diversity of terpenoids by multisubstrate terpene synthases

  • Min Li and
  • Hui Tao

Beilstein J. Org. Chem. 2024, 20, 959–972, doi:10.3762/bjoc.20.86

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  • diphosphate (HexPP, 38, Figure 1), respectively. Similarly, a related TS, BalTS [35][36] from Bacillus alcalophilus was discovered to convert C25, C30, and C35 prenyl diphosphates (39, Figure 1) into the corresponding β-prenes (36, 37, and 40, Figure 3b) [37]. Although BalTS shows no conserved motifs and
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Published 30 Apr 2024

Functional characterisation of twelve terpene synthases from actinobacteria

  • Anuj K. Chhalodia,
  • Houchao Xu,
  • Georges B. Tabekoueng,
  • Binbin Gu,
  • Kizerbo A. Taizoumbe,
  • Lukas Lauterbach and
  • Jeroen S. Dickschat

Beilstein J. Org. Chem. 2023, 19, 1386–1398, doi:10.3762/bjoc.19.100

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  • ), geranylgeranyl pyrophosphate (GGPP) and geranylfarnesyl pyrophosphate (GFPP). Sesquiterpene synthases The enzyme from K. kofuensis (Table 1, entry 1) exhibited all highly conserved motifs required for functionality including the aspartate-rich motif (83DDAYCD) and the NSE triad (223NDIASYYKE, Figure S2
  • related enzymes from other actinomycetes with a pairwise identity of 69% may also function as (+)-δ-cadinol synthases (Figure S11, Supporting Information File 1). The enzyme from S. jumonjiensis (Table 1, entry 2) showed the fully established conserved motifs including the aspartate-rich region (83DDVRSE
  • (+)-α-cadinene synthases (Figure S21, Supporting Information File 1). The enzyme from S. lavendulae (Table 1, entry 3) exhibited all highly conserved motifs including the aspartate-rich sequence (83DDQHD) and the NSE triad (226NDVFSLPKE, Figure S22, Supporting Information File 1). The closely related
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Published 15 Sep 2023

Targeting active site residues and structural anchoring positions in terpene synthases

  • Anwei Hou and
  • Jeroen S. Dickschat

Beilstein J. Org. Chem. 2021, 17, 2441–2449, doi:10.3762/bjoc.17.161

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  • from A222V (37% ee), A222L (7% ee) and A222I (32% ee). Conclusion Terpene synthases contain several well-known highly conserved motifs and single residues that are believed to be generally important for structure and function. As we show here, in special cases such as the sestermobaraene synthase SmTS1
  • incorporated by its nucleophilic attack at a cationic intermediate, leading to terpene alcohols [5][6] or sometimes ethers [7][8]. Substrate ionisation by TPSs is achieved through binding of the diphosphate portion to a trinuclear Mg2+ cluster in the active site that is itself bound to two highly conserved
  • motifs (Supporting Information File 1, Figure S1), composed in bacterial and non-plant eukaryotic enzymes of the aspartate-rich motif DDXX(X)D around position 90 and the NSE triad ND(L,I,V)XSXX(K,R)E near position 230 (Figure 1) [9]. While the amino acid sequences of two TPSs can strongly deviate, their
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Published 17 Sep 2021

Bacterial terpene biosynthesis: challenges and opportunities for pathway engineering

  • Eric J. N. Helfrich,
  • Geng-Min Lin,
  • Christopher A. Voigt and
  • Jon Clardy

Beilstein J. Org. Chem. 2019, 15, 2889–2906, doi:10.3762/bjoc.15.283

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  • . Indeed, besides the influence on kinetic properties by changing the conserved motifs, many bacterial TCs are able to produce novel skeletons through mutations of other active-site residues. This could result in either the arrest of catalytic intermediates or the creation of new trajectories to quench the
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Published 29 Nov 2019

Emission and biosynthesis of volatile terpenoids from the plasmodial slime mold Physarum polycephalum

  • Xinlu Chen,
  • Tobias G. Köllner,
  • Wangdan Xiong,
  • Guo Wei and
  • Feng Chen

Beilstein J. Org. Chem. 2019, 15, 2872–2880, doi:10.3762/bjoc.15.281

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  • two types of terpene synthases are associated with conserved motifs: class I TPSs contain a ‘DDxxD/E’ and a ‘NSD/DTE’ motif while class II TPSs contain a ‘DxDD’ motif. While PpolyTPS1 and PpolyTPS4 contain the ‘DDxxD’ motif, PpolyTPS2 and PployTPS3 contain a ‘DDxxE’ motif. PpolyTPS1, PpolyTPS4, and
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Published 28 Nov 2019

Phylogenomic analyses and distribution of terpene synthases among Streptomyces

  • Lara Martín-Sánchez,
  • Kumar Saurabh Singh,
  • Mariana Avalos,
  • Gilles P. van Wezel,
  • Jeroen S. Dickschat and
  • Paolina Garbeva

Beilstein J. Org. Chem. 2019, 15, 1181–1193, doi:10.3762/bjoc.15.115

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  • synthase in Streptomyces sp. SAT1 is expressed, and to further determine the role of terpenoids in the endophytic life style. The first geosmin synthase was characterised from Streptomyces coelicolor [18]. Geosmin synthases are composed of two domains that both exhibit the typical highly conserved motifs
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Published 29 May 2019

Mechanistic investigations on multiproduct β-himachalene synthase from Cryptosporangium arvum

  • Jan Rinkel and
  • Jeroen S. Dickschat

Beilstein J. Org. Chem. 2019, 15, 1008–1019, doi:10.3762/bjoc.15.99

Graphical Abstract
  • Information File 1) shares conserved motifs for TSs, but is phylogenetically distant to BbS and does not possess a close characterised relative among other bacterial TSs (Figure S2, Supporting Information File 1). Therefore, its gene was cloned into the E. coli expression vector pYE-Express [14] for
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Published 02 May 2019

Stereochemical investigations on the biosynthesis of achiral (Z)-γ-bisabolene in Cryptosporangium arvum

  • Jan Rinkel and
  • Jeroen S. Dickschat

Beilstein J. Org. Chem. 2019, 15, 789–794, doi:10.3762/bjoc.15.75

Graphical Abstract
  • features known conserved motifs both for binding [14] and activation [15] of the diphosphate moiety together with structurally important residues [16][17] (Figure S2, Supporting Information File 1). For in vitro activity testing, the enzyme was expressed in E. coli BL21(DE3), purified (Figure S3
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Published 27 Mar 2019

A detailed view on 1,8-cineol biosynthesis by Streptomyces clavuligerus

  • Jan Rinkel,
  • Patrick Rabe,
  • Laura zur Horst and
  • Jeroen S. Dickschat

Beilstein J. Org. Chem. 2016, 12, 2317–2324, doi:10.3762/bjoc.12.225

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  • conserved motifs including the aspartate-rich motif (DDXXD) and the NSE triad (ND(L,I,V)XSXXXE, modified in plants to a DTE triad: DD(L,I,V)XTXXXE) [8]. Their substrates bind with the diphosphate portion to the (Mg2+)3 cluster and via hydrogen bridges to a highly conserved arginine (diphosphate sensor) and
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Published 04 Nov 2016

Mechanistic investigations on six bacterial terpene cyclases

  • Patrick Rabe,
  • Thomas Schmitz and
  • Jeroen S. Dickschat

Beilstein J. Org. Chem. 2016, 12, 1839–1850, doi:10.3762/bjoc.12.173

Graphical Abstract
  • -ylangene [39]. The (−)-enantiomer of 1 has not been isolated as a natural product before. Type I terpene cyclases exhibit a few highly conserved motifs that are directly involved in binding of the Mg2+ cofactor to which in turn the substrate’s diphosphate portion is bound [10]. This includes the aspartate
  • moiety of the substrate [26]. Mutation within these conserved motifs is usually critical for enyzme functionality [26][41]. The (−)-α-amorphene synthase from S. viridochromogenes DSM 40736 displays the aspartate-rich motif (105DDRAE), the NSE triad (242PDLFSAVKE) starting with a proline instead of the
  • highly conserved motifs including the aspartate-rich motif (80DDQFD), the NSE triad (223NDIHSFERE), the pyrophosphate sensor (R-177), and the 317RY dimer. Closely related enzymes are encoded in more than 35 of the genome sequenced streptomycetes with the enzyme from S. chartreusis NRRL 12338 as closest
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Published 15 Aug 2016
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