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Front Cover: A Promiscuous Cytochrome P450 Hydroxylates Aliphatic and Aromatic C−H Bonds of Aromatic 2,5‐Diketopiperazines (ChemBioChem 8/2019)
Author(s) -
Jiang Guangde,
Zhang Yi,
Powell Magan M.,
Hylton Sarah M.,
Hiller Nicholas W.,
Loria Rosemary,
Ding Yousong
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900174
Subject(s) - hydroxylation , chemistry , stereochemistry , biocatalysis , aromatic amino acids , bacillus subtilis , cytochrome p450 , organic chemistry , catalysis , enzyme , bacteria , biology , reaction mechanism , genetics
The front cover picture shows a versatile biocatalytic synthesis of hydroxylated di‐N‐methylated aromatic diketopiperazines (ADKPs). Di‐N‐methylated ADKPs were synthesized from two amino acids with TxtA and TxtB (yellow) from Streptomyces scabies , or from ADKP with one N ‐methyltransferase Amir_4628 (green) from Actinosynnema mirum . Human methionine adenosyltransferase hMAT2A (purple) was recruited to synthesize the methyl donor SAM. The P450 TxtC (pink) along with the NADPH‐recycling glucose dehydrogenase (cyan) from Bacillus subtilis promoted aliphatic and/or aromatic C−H hydroxylation on di‐N‐methylated ADKPs. More information can be found in the full paper by Y. Ding et al. on page 1068 in Issue 8, 2019 (DOI: 10.1002/cbic.201800736).