Accessibility statement

Dr Mahima Sharma

Tel: (+44) (0)1904 32 8276
Email: mahima.sharma@york.ac.uk

Postdoctoral Research Associate

Mahima is a Postdoctoral Research Associate working with Prof. Gideon Davies, FMedSci, FRS, at the York Structural Biology Laboratory. She completed her DPhil in Chemical Biology from the University of Oxford in 2015. Previously, Mahima worked on designing artificial metalloenzymes for C-C cross-coupling reactions under the supervision of Prof. Benjamin G. Davis, FRS, and also, on structural and biochemical studies of enzymes enabling chiral amine synthesis (IREDs and reductive aminases) in Prof. Gideon Grogan’s group.

Research Interests

Her current project is focussed upon investigation of degradation pathways of sulfoquinovose (SQ), a sulfur containing sugar liberated from sulfolipids found in thylakoid membrane of chloroplasts in plants. These SQ catabolic pathways prevalent in the environment will further our understanding of how sulfur is circulated from this major organosulfur reservoir.

Selected Publications

  • Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria.
    M. Sharma. et al. Proceedings of National Academy of Sciences 2022, DOI: 10.1073/pnas.2116022119.
  • Sulfoglycolysis: catabolic pathways for the breakdown of sulfoquinovose.
    A. J. D. Snow, L. Burchill, M. Sharma*, G. J. Davies*, S. J. Williams*. Chemical Society Reviews 2021, 50, 13628. DOI: 10.1039/D1CS00846C [*corresponding author].
  • Inverting the stereoselectivity of an NADH-dependent imine-reductase variant
    P. Stockinger, N. Borlinghaus, M. Sharma, G. Grogan, J. Pleiss, B. Nestl. ChemCatChem 2021, 13, 5210. DOI: 10.1002/cctc.202101057.
  • The molecular basis of Sulfosugar selectivity in Sulfoglycoysis
    M. Sharma et al, ACS Central Science 2021, 7, 476. DOI: 10.1021/acscentsci.0c01285.
  • Substrate Anchoring and Flexibility Reduction in CYP153AM.aq Leads to Highly Improved Efficiency toward Octanoic Acid.
    L. R. Rapp et al. ACS Catalysis 2021, 11 (5), 3182-3189. DOI: 10.1021/acscatal.0c05193.
  • Asymmetric synthesis of primary amines catalyzed by fungal reductive aminases
    J. Mangas-Sanchez & M. Sharma et al., Chemical Science, 2020, DOI:10.1039/D0SC02253E
  • Dynamic Structural Changes Accompany the Production of 2-Dihydroxypropanesulfonate by Sulfolactaldehyde Reductase
    M. Sharma et al., ACS Catalysis, 2020, 10 (4), 2826-2836 DOI: 10.1021/acscatal.9b04427
  • A sulfoglycolytic Entner-Doudoroff pathway in Rhizobium leguminosarum bv. trifolii SRDI565
    J. Li, R. Epa et al., Appl. Environ. Microbiol., 2020, DOI: 10.1128/AEM.00750-20
  • Inverted binding of non-natural substrates in strictosidine synthase leads to a switch of stereochemical outcome in enzyme-catalyzed Pictet-Spengler reactions
    E. Eger et al., J. Am. Chem. Soc., 2020, 142, 792−800. DOI: 10.1021/jacs.9b08704
  • Asymmetric Synthesis of β-Fluoroamines using Reductive Aminases from Fungi
    González-Martínez et al,ChemCatChem, 2020, DOI: 10.1002/cctc.201901999
  • Identification and characterization of cytochrome P450 1232A24 and 1232F1 from Arthrobacter sp. and their role in the metabolic pathway of papaverine
    J. M. Klenk et al., The Journal of Biochemistry, 2019, DOI: 10.1093/jb/mvz010
  • Structure-guided engineering of the novel versatile terpene hydroxylase CYP109Q5 from Chondromyces apiculatus
    J. M. Klenk et al., Microbial Biotechnology, 2019, 12, 2, 377. DOI: 10.1111/1751-7915.13354
  • A Mechanism for Fungal Reductive Aminases (RedAms)
    M. Sharma et al., ACS Catal., 2018, 8, 12, 11534. DOI: 10.1021/acscatal.8b03491
  • New Imine Reducing Enzymes from β-Hydroxyacid Dehydrogenases by Single Amino Acid Substitutions
    M. Lenz et al., Protein Eng. Des. Sel., 2018, 31, 4, 109. DOI: 10.1093/protein/gzy006
  • Biocatalytic Routes to Enantiomerically Enriched Dibenz[c,e]azepines
    P. France et al.,Angew. Chem. Int. Ed., 2017, 56, 15589. DOI: 10.1002/anie.201708453
  • A Reductive Aminase Enzyme from Aspergillus oryzae
    A. Aleku et al., Nat Chem,2017, 9, 961. DOI: 10.1038/nchem.2782
  • NAD(P)H-Dependent Dehydrogenases for the Asymmetric Reductive Amination of Ketones: Structure, Mechanism, Evolution and Application
    Sharma et al., Adv. Synth. Catal., 20173592011. DOI:10.1002/adsc.201700356
  • Imine Reductases (IREDs)
    J. Mangas-Sanchez et al., Curr. Opin. Chem. Biol. 2017, 37, 19. DOI: 10.1016/j.cbpa.2016.11.022