Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Gustavo Perez Ortiz"'
Autor:
Gustavo Perez-Ortiz, John D. Sidda, Jessica Peate, Davide Ciccarelli, Yaoyu Ding, Sarah M. Barry
Publikováno v:
Frontiers in Microbiology, Vol 14 (2023)
Heme is best known for its role as a versatile prosthetic group in prokaryotic and eukaryotic proteins with diverse biological functions including gas and electron transport, as well as a wide array of redox chemistry. However, free heme and related
Externí odkaz:
https://doaj.org/article/70e69a4eaeb24f66947879fa14656451
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
The discovery of new enzymes, alongside the push to make chemical processes more sustainable, has resulted in increased industrial interest in the use of biocatalytic processes to produce high-value and chiral precursor chemicals. Huge strides in pro
Externí odkaz:
https://doaj.org/article/483d7b4b79df4f49bcf30d6e04fc2bdc
Autor:
Silvia Anselmi, Alexandra T. P. Carvalho, Angela Serrano-Sanchez, Jose L. Ortega-Roldan, Jill Caswell, Iman Omar, Gustavo Perez-Ortiz, Sarah M. Barry, Thomas S. Moody, Daniele Castagnolo
Publikováno v:
ACS Catalysis. 13:4742-4751
Autor:
Shona M. Richardson, Peter J. Harrison, Michael A. Herrera, Menglu Wang, Rebecca Verez, Gustavo Perez Ortiz, Dominic J. Campopiano
Publikováno v:
Richardson, S M, Harrison, P J, Herrera, M A, Wang, M, Verez, R, Ortiz, G P & Campopiano, D J 2022, ' BioWF: A naturally-fused, di-domain biocatalyst from biotin biosynthesis displays an unexpectedly broad substrate scope ', ChemBioChem . https://doi.org/10.1002/cbic.202200171
The carbon backbone of biotin is constructed from the C 7 di-acid pimelate, which is converted to an acyl-CoA thioester by an ATP-dependent, pimeloyl-CoA synthetase (PCAS, encoded by BioW). The acyl-thioester is condensed with ʟ-alanine in a decarbo
Autor:
Gustavo Perez Ortiz, John D. Sidda, Emmanuel L. C. de los Santos, Sarah M. Barry, Catherine B. Hubert
Publikováno v:
Chemical Communications (Cambridge, England)
The antimycobacterial peptides, rufomycins, have their antibiotic activity conferred by oxidative tailoring of the cyclic peptide. Here we elucidate the roles of cytochrome P450s RufS and RufM in regioselective epoxidation and alkyl oxidation respect