2020
DOI: 10.1007/s10295-020-02327-y
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Correction to: Synthetic biology, combinatorial biosynthesis, and chemo-enzymatic synthesis of isoprenoids

Abstract: Unfortunately, the article title was published incorrectly in the HTML version (online version only) of the online published article.

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“…The aim of this mini‐review is to explore what has been done in previous years to diversify the structure of the terpene precursors IPP and DMAPP, either chemically or enzymatically, and how the terpene landscape has thus been enlarged. This mini‐review complements two recently published reviews describing the substrate promiscuity of terpene synthases/cyclases [2,3] that readers are encouraged to consult for a general overview of the enzymatic generation of unnatural terpenes. It also highlights the potential of the recently developed Terpene Mini‐Path (TMP) to easily access non‐canonical terpenes enzymatically instead of chemically, either in vivo or in vitro (see also [3] in this context).…”
Section: Introductionmentioning
confidence: 84%
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“…The aim of this mini‐review is to explore what has been done in previous years to diversify the structure of the terpene precursors IPP and DMAPP, either chemically or enzymatically, and how the terpene landscape has thus been enlarged. This mini‐review complements two recently published reviews describing the substrate promiscuity of terpene synthases/cyclases [2,3] that readers are encouraged to consult for a general overview of the enzymatic generation of unnatural terpenes. It also highlights the potential of the recently developed Terpene Mini‐Path (TMP) to easily access non‐canonical terpenes enzymatically instead of chemically, either in vivo or in vitro (see also [3] in this context).…”
Section: Introductionmentioning
confidence: 84%
“…This mini‐review complements two recently published reviews describing the substrate promiscuity of terpene synthases/cyclases [2,3] that readers are encouraged to consult for a general overview of the enzymatic generation of unnatural terpenes. It also highlights the potential of the recently developed Terpene Mini‐Path (TMP) to easily access non‐canonical terpenes enzymatically instead of chemically, either in vivo or in vitro (see also [3] in this context). Here we will first focus on the substrate promiscuity of enzymes involved in the synthesis or modification of C 5 diphosphate precursors, then on the substrate promiscuity of prenyl transferases (aromatic or aliphatic) and finally on the biosynthesis and chemo‐enzymatic synthesis of terpenes using non‐canonical prenylated diphosphates.…”
Section: Introductionmentioning
confidence: 84%