Zobrazeno 1 - 10
of 221
pro vyhledávání: '"Paul C. Engel"'
Publikováno v:
Green Chemistry. 19:503-510
Halogenated derivatives of phenylalanine can be used as cross-coupling reagents for making drug-like molecules, and pure enantiomers of these precursors are therefore highly desirable. In our exploration of enzymatic routes to simplify the deracemisa
Autor:
Nayla Munawar, Paul C. Engel
Publikováno v:
Current Biotechnology. 2:334-344
Autor:
Paul C. Engel
Publikováno v:
The Biochemist. 35:40-43
This BJ Classic article assesses the legacy of the Hill equation 100 years after the Nobel Laureate Archibald Hill published a paper entitled ‘The combinations of haemoglobin with oxygen and with carbon monoxide’1 in the Biochemical Journal.
Publikováno v:
FEBS Journal. 280:4681-4692
Glutamate dehydrogenases (EC 1.4.1.2–4) catalyse the oxidative deamination of l-glutamate to α-ketoglutarate using NAD+ and/or NADP+ as a cofactor. Subunits of homo-hexameric bacterial enzymes comprise a substrate-binding Domain I followed by a nu
Autor:
Paul C. Engel
Publikováno v:
Neurochemical Research. 39:426-432
NAD(+) and NADP(+), chemically similar and with almost identical standard oxidation-reduction potentials, nevertheless have distinct roles, NAD(+) serving catabolism and ATP generation whereas NADPH is the biosynthetic reductant. Separating these rol
Autor:
David W. Rice, Timothy J. Stillman, Xing-Guo Wang, K. Linda Britton, Patrick J. Baker, Paul C. Engel, Jonathan Dean
Publikováno v:
Scopus-Elsevier
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c9121569be19226902abbd6a29f7720
https://ora.ox.ac.uk/objects/uuid:e8d15964-9312-452b-bcd3-199c0c968233
https://ora.ox.ac.uk/objects/uuid:e8d15964-9312-452b-bcd3-199c0c968233
Publikováno v:
Acta crystallographica. Section F, Structural biology communications. 72(Pt 6)
Glutamate dehydrogenases (EC 1.4.1.2–4) catalyse the oxidative deamination of L-glutamate to α-ketoglutarate using NAD(P)+as a cofactor. The bacterial enzymes are hexameric, arranged with 32 symmetry, and each polypeptide consists of an N-terminal
Autor:
Paul C. Engel, Nayla Munawar
Publikováno v:
Extremophiles. 17:43-51
Heat- and solvent-tolerant enzymes from halophiles, potentially important industrially, offer a robust framework for protein engineering, but few solved halophilic structures exist to guide this. Homology modelling has guided mutations in glutamate d
Publikováno v:
FEBS Journal. 279:3003-3009
Active-site mutants of glutamate dehydrogenase from Clostridium symbiosum have been designed and constructed and the effects on coenzyme preference evaluated by detailed kinetic measurements. The triple mutant F238S/P262S/D263K shows complete reversa
Autor:
Nayla Munawar, Paul C. Engel
Publikováno v:
Extremophiles. 16:463-476
Enzymes produced by halophilic archaea are generally heat resistant and organic solvent tolerant, and accordingly important for biocatalytic applications in 'green chemistry', frequently requiring a low-water environment. NAD(+)-dependent glutamate d