Kinetics and structure-guided characterisation and engineering of aldehyde deformylating oxygenase (ADO) for a renewable microbial biofuel platform

Autor: Menon, Navya

The increased demand for an alternative form of fuel has raised a great interest towards exploring various metabolic pathways and enzymes in several microbial species for hydrocarbon production. In recent years, cyanobacteria have emerged as an attra

Externí odkaz: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.719280

Halogenases for biosynthetic pathway engineering: Toward new routes to naturals and non-naturals.

Autor: Menon, Binuraj R. K., Richmond, Daniel, Menon, Navya

Publikováno v: Catalysis Reviews: Science & Engineering; 2022, Vol. 64 Issue 3, p533-591, 59p

Glutamate 338 is an electrostatic facilitator of C-Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase.

Autor: Menon, Binuraj R. K.¹, Menon, Navya¹, Fisher, Karl¹, Rigby, Stephen E. J.¹, Leys, David¹, Scrutton, Nigel S.¹

Publikováno v: FEBS Journal. Apr2015, Vol. 282 Issue 7, p1242-1255. 14p.

Glutamate 338 is an electrostatic facilitator of C-Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase

Autor: Menon, Binuraj R K, Menon, Navya, Fisher, Karl, Rigby, Stephen E J, Leys, David, Scrutton, Nigel S

Publikováno v: Menon, B, Menon, N, Fisher, K, Rigby, S E J, Leys, D & Scrutton, N S 2015, ' Glutamate 338 is an electrostatic facilitator of C-Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase. ', The FEBS Journal, vol. 282, no. 7, pp. 1242-1255 . https://doi.org/10.1111/febs.13215
The Febs Journal

How cobalamin-dependent enzymes promote C-Co homolysis to initiate radical catalysis has been debated extensively. For the pyridoxal 5'-phosphate and cobalamin-dependent enzymes lysine 5,6-aminomutase and ornithine 4,5-aminomutase (OAM), large-scale

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::08cc45aaa0d58fa48036183df152cbce
https://doi.org/10.1111/febs.13215

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