The reaction rate of a catalyzed reaction is faster than the reaction rate of the uncatalyzed reaction at the same temperature. 139755-85-4, Name is 5-(2-Ethoxy-5-((4-(2-hydroxyethyl)piperazin-1-yl)sulfonyl)phenyl)-1-methyl-3-propyl-1H-pyrazolo[4,3-d]pyrimidin-7(6H)-one, SMILES is O=C1C(N(C)N=C2CCC)=C2N=C(C3=CC(S(=O)(N4CCN(CCO)CC4)=O)=CC=C3OCC)N1, in an article , author is Yuan, Bochuan, once mentioned of 139755-85-4, Recommanded Product: 139755-85-4.
Piperazine ring formation by a single-module NRPS and cleavage by an alpha-KG-dependent nonheme iron dioxygenase in brasiliamide biosynthesis
Brasiliamides are a class of piperazine-containing alkaloids produced by Penicillium brasilianum with a range of pharmaceutical activities. The mechanism of brasiliamide biosynthesis, including piperazine ring formation and multiple tailoring modifications, still remains unclear. In this study, the biosynthetic gene cluster of brasiliamides, brs, was identified from the marine-derived fungal strain Penicillium brasilianum WZXY-M122-9. Deletion of a histone deacetylase-encoding gene using a CRISPR/Cas9 gene editing system led to the production of a new compound, namely brasiliamide I (1). The brs-encoded single-module nonribosomal peptide synthetase (NRPS) BrsA is involved in the formation of the piperazine skeleton of brasiliamides. Full-length BrsA protein (113.6 kDa) was purified, and reconstitution of enzymatic activity in vitro confirmed that BrsA stereoselectively accepts l-phenylalanine as the substrate. Multiple deletion of tailoring genes and analysis of purified proteins in vitro enabled us to propose a brasiliamide biosynthetic pathway. In the tailoring steps, an alpha-ketoglutarate (KG)-dependent nonheme iron dioxygenase, BrsJ, was identified to catalyze piperazine ring cleavage during biosynthesis of brasiliamide A (2).
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Reference:
Piperazine – Wikipedia,
,Piperazines – an overview | ScienceDirect Topics