Role of active site loop in coenzyme binding and flavin reduction in cytochrome P450 reductase.
Structural and kinetic insight into the biosynthesis of H2S and L-lanthionine from L-cysteine by a PLP-dependent enzyme from Fusobacterium nucleatum.
Fusobacterium nucleatum is a common oral bacterium and a major producer of H2S, a toxic gas linked to the pathogenesis of periodontal disease. The bacterium encodes a fold type II…
Optimal electrostatic interactions between substrate and protein are essential for radical chemistry in ornithine 4,5-aminomutase.
A Fold Type II PLP-Dependent Enzyme from Fusobacterium nucleatum Functions as a Serine Synthase and Cysteine Synthase.
It is shown that SS can also function as a cysteine synthase, catalyzing the β-replacement of l-serine with bisulfide to produce l-cysteine and H2O and highlighting the multiple catalytic roles of D232 in a new member of the fold type II family of PLP-dependent enzymes.
S224 Presents a Catalytic Trade-off in PLP-Dependent l-Lanthionine Synthase from Fusobacterium nucleatum.
- Robert G Mothersole, Cory R Billett, G. Saini, Mina K Mothersole, Amanda L Darbyshire, K. Wolthers
- Chemistry, BiologyBiochemistry
- 28 October 2020
Presteady state kinetic analysis showed that the reaction between S224A and l-cysteine leads to the formation of the more reactive ketoenamine tautomer of the α-aminoacrylate, which is not an observable intermediate in the analogous reaction with the wild type.
Sequence Divergence in the Arginase Domain of Ornithine Decarboxylase/Arginase in Fusobacteriacea Leads to Loss of Function in Oral Associated Species.
- Robert G Mothersole, M. Kolesnikov, A. Chan, Emmanuel Oduro, M. Murphy, K. Wolthers
- Biology, ChemistryBiochemistry
- 22 June 2022
Engineering of the complete metal coordination environment through site-directed mutagenesis restored Mn2+ binding capacity and arginase activity, although the catalytic efficiency for l-arginine was low (60-100 M-1 s-1) and metal ions are absent in the active site.
Characterisation of three cofactor-containing proteins from the oral bacterium Fusobacterium nucleatum
- Robert G Mothersole
Structural insight into the high reduction potentials observed for Fusobacterium nucleatum flavodoxin
- Robert G Mothersole, M. Macdonald, M. Kolesnikov, M. Murphy, K. Wolthers
- Biology, ChemistryProtein science : a publication of the Protein…
- 1 August 2019
It is shown that natural substitutions of highly conserved residues partially account for these more electropositive reduction potentials of known long‐chain flavodoxins.