A5059187791- Enzyme Structure and Function
- Metalloenzymes and iron-sulfur proteins
- Carbohydrate Chemistry and Synthesis
- Metal-Catalyzed Oxygenation Mechanisms
- Viral Infectious Diseases and Gene Expression in Insects
- Protein purification and stability
- Electrocatalysts for Energy Conversion
- Glycosylation and Glycoproteins Research
- Protein Structure and Dynamics
- Trace Elements in Health
- Fungal and yeast genetics research
- Amino Acid Enzymes and Metabolism
- Cancer, Hypoxia, and Metabolism
- Protein Kinase Regulation and GTPase Signaling
- Lysosomal Storage Disorders Research
- Porphyrin Metabolism and Disorders
- Metabolism, Diabetes, and Cancer
- Redox biology and oxidative stress
- Fermentation and Sensory Analysis
- Genomics and Phylogenetic Studies
- Blood disorders and treatments
- RNA and protein synthesis mechanisms
- Enzyme function and inhibition
- Bacterial Genetics and Biotechnology
- Electrochemical sensors and biosensors
Regeneron (United States)
2016-2020
Thunder Bay Regional Research Institute
2015
University of Sussex
1995-2005
John Innes Centre
1999-2001
Daresbury Laboratory
1999-2001
Carl von Ossietzky Universität Oldenburg
1999
Saarland University
1999
The University of Queensland
1999
Newcastle University
1980-1986
There is strong interest in the design of bispecific monoclonal antibodies (bsAbs) that can simultaneously bind 2 distinct targets or epitopes to achieve novel mechanisms action and efficacy. Multiple formats have been proposed are currently under development. Regeneron's technology based upon a standard fully human IgG antibody order minimize immunogenicity improve pharmacokinetic profile. A single common light chain heavy chains combine form molecule. One contains chimeric Fc sequence...
Much is unknown concerning the role of thiolate ligands molybdenum in molybdopterin enzymes. It has been suggested that dissociation from part catalytic mechanism bis-molybdopterin enzymes dimethyl sulfoxide reductase (DMSOR) family. For DMSOR Rhodobacter capsulatus, therefore investigated crystallographically, by UV/visible spectroscopy, and enzyme assays. When crystallized sodium citrate, all four thiolates are within bonding distance Mo, but after extended exposure to Na+-Hepes, a pair...
Analysis of the reversible unfolding yeast phosphoglycerate kinase leads to conclusion that two lobes are capable folding independently, consistent with presence intermediates on pathway a single domain folded. The domains have different free energies stabilisation. Immunological cross‐reactivity, circular dichroism and thiol reactivity provide evidence for cyanogen bromide peptide 1–173, which comprises five‐sixths N‐terminal domain, containing sufficient information refold into native‐like...
Improved assays for the molybdenum enzyme dimethylsulfoxide reductase (DMSOR) with dimethyl sulfoxide (DMSO) and sulfide (DMS) as substrates are described. Maximum activity was observed at pH 6.5 below 8.3, respectively. Rapid-scan stopped-flow spectrophotometry has been used to investigate reduction of by DMS a species previously characterized its UV−visible spectrum [McAlpine, A. S., McEwan, G., Bailey, S. (1998) J. Mol. Biol. 275, 613−623], subsequent reoxidation DMSO. Both these...
<italic>N</italic>-Octyl conduritol aziridine is a potent and specific covalent inactivator of β-glucocerebrosidase (GBA1) inside live human cells.
The bis-molybdopterin enzyme dimethylsulfoxide reductase (DMSOR) from Rhodobacter capsulatus catalyzes the conversion of dimethyl sulfoxide (DMSO) to sulfide (DMS), reversibly, in presence suitable e(-)-donors or e(-)-acceptors. catalytically significant intermediate formed by reaction DMSOR with DMS ('the species') and a damaged form derived latter O(2) (DMS-modified enzyme, DMSOR(mod)D) have been investigated. Evidence is presented that Mo species not, as widely assumed, Mo(IV). Formation...
For isoquinoline 1-oxidoreductase (IsoOr), the reaction mechanism under turnover conditions was studied by EPR spectroscopy using rapid-freeze methods. IsoOr displays several EPR-active Mo(V) species including "very rapid" component found also in xanthine oxidase (XanOx). IsoOr, unlike XanOx or quinoline 2-oxidoreductase (QuinOr), this is stable for about 1 h absence of an oxidizing substrate [Canne, C., Stephan, I., Finsterbusch, J., Lingens, F., Kappl, R., Fetzner, S., and Hüttermann, J....
Recent crystal structures of xanthine dehydrogenase, oxidase and related enzymes have paved the way for a detailed structural functional analysis these enzymes. One problem encountered when working with proteins, especially recombinant protein, is that preparations tend to be heterogeneous, only fraction enzyme molecules being active. This due incompleteness post-translational modification, which this protein complex, incompletely understood, process involving incorporation Mo Fe/S centres....
L-Aspartate aminotransferase, a member of the α-family PLP mediated enzymes, which normally catalyses transamination, has been used to catalyse β-substitution reaction stereospecifically labelled samples enzyme inhibitor β-chloro-L-alanine with 2-mercaptoethanol; stereochemistry products was assigned by independent synthesis, showing that abnormal substitution proceeds overall retention stereochemistry, usual stereochemical consequence reactions catalysed enzymes β-family have low homology α-family.
Two members of the α-family PLP-dependent enzymes, L-aspartate aminotransferase and D-amino acid aminotransferase, have been shown to catalyse β-substitution L- D-β-chloroalanine respectively with β-mercaptoethanol, reactions typical β-family enzymes. The reaction catalysed by has occur retention stereochemistry, a outcome for There are also indications that may involve stereochemistry. Both enzymes exchange at C-3 when appropriate enantiomer β-chloroalanine is substrate.
A hinge‐bending mechanism has been proposed for phosphoglycerate kinase, in which the two domains bend about connecting “swaist& rsquo; region. In partially denaturing concentrations of guanidinium chloride substrate 3‐phosphoglycerate stabilises one domain against denaturation and destabilises other. The reduction mutual stabilisation on binding indicates a freeing hinge to allow protein take up other states rather than directive mechanism. both at higher ATP enzyme is inhibited supports this
Recent crystal structures of xanthine dehydrogenase, oxidase and related enzymes have paved the way for a detailed structural functional analysis these enzymes. One problem encountered when working with proteins, especially recombinant protein, is that preparations tend to be heterogeneous, only fraction enzyme molecules being active. This due incompleteness post-translational modification, which this protein complex, incompletely understood, process involving incorporation Mo Fe/S centres....
Treatment of yeast phosphoglycerate kinase (PGK) with trypsin results in a fourfold increase the V max this enzyme, without affecting Km. This activation is shown to be due removal C‐terminal lysine residue. The sequence folds back over N‐terminal domain and contacts extreme which onto domain, thus making many inter‐domain two protein. Previous studies have that region important mediating conformational changes required during catalysis by PGK. Observation three‐dimensional structure enzyme...
Abstract The stereochemistry of a variety pyridoxal phosphate-mediated enzymic reactions has been studied using enzyme inhibitors that are stereospecifically labeled in the β-position with deuterium. A versatile synthesis developed to prepare wide d- and l-amino acids inhibitors. Investigation "turnover" β-chloro-d-alanine l-serine-O-sulfate by d-amino acid aminotransferase l-aspartate respectively shown reaction within active site former occurs retention stereochemistry. Although is an...
U.K.; *School of Biology and Biochemistry, University Bath, BA2 7AY, JInstituto de Tecnologia Quimica e BioMgica, 2780 Oeiras, Portugal; 4Max-Planck-Institut flit Biochemie, D-82 152 Planegg-Martinsried, Germany; 51nstitut Gtnttique et Microbiologie, Universitt Paris-Sud, 91405 Orsay Cedex, France. DOYLE, 'ROBERT C. BRAY, 294MATTHEW RYAN, The recent availability the 3-dimensional structure
Conference Article| December 01 1980 Native-like dimer formed by the N-terminal cyanogen bromide fragment of yeast phosphoglycerate kinase BENJAMIN ADAMS; ADAMS 1Department Biochemistry, University Newcastle upon Tyne, NE1 7RU, U.K. Search for other works this author on: This Site PubMed Google Scholar ROGER H. PAIN Biochem Soc Trans (1980) 8 (6): 730. https://doi.org/10.1042/bst0080730 Views Icon Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Facebook...