Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Evaldas Klumbys"'
Autor:
Evaldas Klumbys, Wei Xu, Lokanand Koduru, Elena Heng, Yifeng Wei, Fong Tian Wong, Huimin Zhao, Ee Lui Ang
Publikováno v:
Microbial Cell Factories, Vol 23, Iss 1, Pp 1-12 (2024)
Abstract Background Streptomyces is renowned for its robust biosynthetic capacity in producing medically relevant natural products. However, the majority of natural products biosynthetic gene clusters (BGCs) either yield low amounts of natural produc
Externí odkaz:
https://doaj.org/article/c15208acd87340bbb1be85956098c0c5
Publikováno v:
Metabolic Engineering Communications, Vol 10, Iss , Pp e00108- (2020)
Natural products and their related derivatives play a significant role in drug discovery and have been the inspiration for the design of numerous synthetic bioactive compounds. With recent advances in molecular biology, numerous engineering tools and
Externí odkaz:
https://doaj.org/article/b185e4bc1d8d42c293352f6043260e5a
Publikováno v:
Klumbys, E, Zebec, Z, Weise, N, Turner, N & Scrutton, N 2018, ' Bio-derived Production of Cinnamyl Alcohol via a Three Step Biocatalytic Cascade and Metabolic Engineering ', Green Chemistry . https://doi.org/10.1039/C7GC03325G
Green Chemistry
Green Chemistry
The construction of biocatalytic cascades for the production of chemical precursors is fast becoming one of the most efficient approaches to multi-step synthesis in modern chemistry. However, despite the use of low solvent systems and renewably resou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9080521de99f2614974f5c0bb93de22c
https://europepmc.org/articles/PMC6546598/
https://europepmc.org/articles/PMC6546598/
Autor:
Nicholas J. Turner, Mark S. Dunstan, A. Hill, Daniela Quaglia, David Leys, Deepankar Gahloth, Evaldas Klumbys, Nigel S. Scrutton, Michael P. Lockhart-Cairns, Sasha R. Derrington
Publikováno v:
Gahloth, D, Dunstan, M S, Quaglia, D, Klumbys, E, Lockhart-Cairns, M P, Hill, A, Derrington, S R, Scrutton, N S, Turner, N J & Leys, D 2017, ' Structures of carboxylic acid reductase reveal domain dynamics underlying catalysis ', Nature chemical biology, vol. 13, pp. 975-981 . https://doi.org/10.1038/nchembio.2434
Nature chemical biology
Nature chemical biology
Carboxylic acid reductase (CAR) catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes. The enzyme is related to the nonribosomal peptide synthetases, consisting of an adenylation domain fused via a peptid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::391421accf42fd9e5ffac4e4205efe85
https://pure.manchester.ac.uk/ws/files/59204978/18692_3_merged_1496951682.pdf
https://pure.manchester.ac.uk/ws/files/59204978/18692_3_merged_1496951682.pdf