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Jennifer A. Littlechild

Jennifer A. Littlechild

D-Index & Metrics

Chemistry

D-Index
51
Citations
7855
World Ranking
14131
National Ranking
787

Overview

Jennifer A. Littlechild is affiliated with the University of Exeter in the United Kingdom. Their research spans the field of Biochemistry, Genetics and Molecular Biology, with a primary focus on Molecular Biology, Materials Chemistry, and Biochemistry. Other areas of interest include Biotechnology and Organic Chemistry.

The scientist's work covers several topics primarily related to enzyme science and biocatalysis. These include:

  • Enzyme Catalysis and Immobilization
  • Enzyme Structure and Function
  • Amino Acid Enzymes and Metabolism
  • Microbial Metabolic Engineering and Bioproduction
  • Chemistry and Chemical Engineering
  • Protein Structure and Dynamics
  • Enzyme Production and Characterization

Jennifer A. Littlechild has frequently published in the following venues:

  • ChemSusChem
  • Frontiers in Microbiology
  • Frontiers in Bioengineering and Biotechnology
  • Zenodo (CERN European Organization for Nuclear Research)
  • Frontiers in Catalysis

Their recent papers include:

  • Biocatalysis as Key to Sustainable Industrial Chemistry, 2022, ChemSusChem
  • Biosensors and Diagnostics for Fungal Detection, 2020, Journal of Fungi
  • Biocatalysis as Key to Sustainable Industrial Chemistry, 2022, ChemSusChem
  • Structural Insights into a Novel Esterase from the East Pacific Rise and Its Improved Thermostability by a Semirational Design, 2021, Journal of Agricultural and Food Chemistry
  • Structural insights into the NAD+-dependent formate dehydrogenase mechanism revealed from the NADH complex and the formate NAD+ ternary complex of the Chaetomium thermophilum enzyme, 2020, Journal of Structural Biology

Collaborations have involved frequent co-authors such as Michail N. Isupov, Roland Wohlgemuth, S.A. De Rose, Andrés R. Alcántara, and Pablo Domínguez de María.

Jennifer A. Littlechild has also contributed to book publications, notably a title titled Systems Biocatalysis for Bioprocess Design published by Frontiers Media in 2022.

Best Publications

  • Metal and redox modulation of cysteine protein function.

    Niroshini M Giles;Aaron B Watts;Gregory I Giles;Fiona H Fry

  • Arabidopsis thaliana VTC4 Encodes L-Galactose-1-P Phosphatase, a Plant Ascorbic Acid Biosynthetic Enzyme

    Patricia L. Conklin;Stephan Gatzek;Glen L. Wheeler;John Dowdle

  • Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis.

    Michail N. Isupov;Andrew R. Dalby;Amanda A. Brindley;Yoshikazu Izumi

  • Tps1 regulates the pentose phosphate pathway, nitrogen metabolism and fungal virulence

    Richard A. Wilson;Joanna M. Jenkinson;Robert P. Gibson;Jennifer A. Littlechild

  • Biocatalysis as Key to Sustainable Industrial Chemistry.

    Unknown

  • Enzymes from Extreme Environments and Their Industrial Applications

    Jennifer Ann Littlechild

  • An NADPH-dependent genetic switch regulates plant infection by the rice blast fungus

    Richard A. Wilson;Robert P. Gibson;Cristian F. Quispe;Cristian F. Quispe;Jennifer A. Littlechild

  • Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

    Mirella Vivoli;Halina R. Novak;Jennifer A. Littlechild;Nicholas J. Harmer

  • Haloperoxidases and their role in biotransformation reactions.

    Jennifer Littlechild

  • Activity and specificity of human aldolases.

    Steven J. Gamblin;Gideon J. Davies;Jonathan M. Grimes;Richard M. Jackson

  • Development of the biocatalytic resolution of 2-azabicyclo[2.2.1]hept-5-en-3-one as an entry to single-enantiomer carbocyclic nucleosides

    Stephen Jc Taylor;Raymond McCague;Richard Wisdom;Carol Lee

  • Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 å crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase

    Michail N Isupov;Galya Obmolova;Susanna Butterworth;Marie-Ange Badet-Denisot

  • Characterization of Carboxylic Acid Reductases as Enzymes in the Toolbox for Synthetic Chemistry

    William Finnigan;Adam Thomas;Holly Cromar;Ben Gough

  • Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications.

    Andrew Dalby;Zbigniev Dauter;Jennifer A. Littlechild

  • Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 A.

    G.J. Davies;S.J. Gamblin;J.A. Littlechild;Z. Dauter

  • The structure of a thermally stable 3-phosphoglycerate kinase and a comparison with its mesophilic equivalent.

    Gideon J. Davies;Steven J. Gamblin;Jennifer A. Littlechild;Herman C. Watson

  • Thermophilic Microbes in Environmental and Industrial Biotechnology

    Tulasi Satyanarayana;Jennifer Littlechild;Yutaka Kawarabayasi

  • Crystal structure of a thermostable Old Yellow Enzyme from Thermus scotoductus SA-01

    Diederik J. Opperman;Bryan T. Sewell;Derek Litthauer;Mikhail N. Isupov

  • Structural studies on the dodecameric vanadium bromoperoxidase from Corallina species

    Jennifer Littlechild;Esther Garcia-Rodriguez

  • The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix.

    Jodie E. Guy;Michail N. Isupov;Jennifer A. Littlechild

  • Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.

    Michail N. Isupov;Toni M. Fleming;Andrew R. Dalby;Gina S. Crowhurst

Frequent Co-Authors

Gideon J. Davies
Gideon J. Davies University of York
Robert J. P. Williams
Robert J. P. Williams University of Oxford
Elizaveta A. Bonch-Osmolovskaya
Elizaveta A. Bonch-Osmolovskaya Russian Academy of Sciences
Paul G. Winyard
Paul G. Winyard University of Exeter
John M. Ward
John M. Ward University College London
Don A. Cowan
Don A. Cowan University of Pretoria
Peter W. Piper
Peter W. Piper University of Sheffield
Gillian M. Greenway
Gillian M. Greenway University of Hull
Paul Eggleton
Paul Eggleton University of Exeter
Vladimir Popov
Vladimir Popov Institute for Theoretical and Experimental Physics

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