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Deacetoxycephalosporin C synthase is an iron(II) 2-oxoglutaratedependent oxygenase that catalyzes the oxidative ring-expansion of penicillin N to deacetoxycephalosporin C. The wild-type enzyme is only able to efficiently utilize 2-oxoglutarate and 2-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::3eb88c2d306417aa943ebc49127aa406
https://ora.ox.ac.uk/objects/uuid:f8904bd0-8b4b-46c2-b65a-75e8eecaa764
https://ora.ox.ac.uk/objects/uuid:f8904bd0-8b4b-46c2-b65a-75e8eecaa764
Autor:
Roach, PL, Clifton, IJ, Hensgens, CMH, Shibata, N, Long, AJ, Strange, RW, Hasnain, SS, Schofield, CJ, Baldwin, JE, Hajdu, J
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::25a56de374cfda719ca8f2041267401c
https://ora.ox.ac.uk/objects/uuid:38c8e8ba-a27e-41ec-9f1e-2c3abb146e30
https://ora.ox.ac.uk/objects/uuid:38c8e8ba-a27e-41ec-9f1e-2c3abb146e30
The substrate analog L-S-(a-aminoadipoyl)-L-cysteinyl-glycine (ACG) was co-crystallised with isopenicillin N synthase using the hanging-drop vapourdiffusion method in an anaerobic environment. ' X-ray crystallography revealed a different mode of bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::d6576ae2d789aefaf49b8fbd51b92c67
https://ora.ox.ac.uk/objects/uuid:615d0e21-d29d-4a61-906b-2dd2b826611a
https://ora.ox.ac.uk/objects/uuid:615d0e21-d29d-4a61-906b-2dd2b826611a
Autor:
Steven Jerie, Baldwin Jenya
Publikováno v:
Iranian Journal of Health, Safety and Environment, Vol 7, Iss 3, Pp 1509-1518 (2022)
The aim of this study was to examine industrial waste minimisation through material and energy recovery at Hwange Power Station in Zimbabwe. This project is significant in that it envisages the opportunities of boosting power output through the use o
Externí odkaz:
https://doaj.org/article/c96b7b3697e64d5693137794f711d58a
Autor:
Hewitson Ks, Baldwin Je, Peter L. Roach, Yiannis Sanakis, Ollagnier-De Choudens S, Marc Fontecave, Eckard Münck
Publikováno v:
Biochemistry. 39:4165-4173
Biotin synthase and lipoate synthase are homodimers that are required for the C-S bond formation at nonactivated carbon in the biosynthesis of biotin and lipoic acid, respectively. Aerobically isolated monomers were previously shown to contain a (2Fe
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