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Production of Propane and Other Short-Chain Alkanes by Structure-Based Engineering of Ligand Specificity in Aldehyde-Deformylating Oxygenase
- B. Khara, N. Menon, N. Scrutton
- Engineering, BiologyChembiochem : a European journal of chemical…
- 11 June 2013
Biocatalytic propane production: structure-based engineering of aldehyde-deformylating oxygenase improves specificity for short- and medium-chain-length aldehydes and enhances the propane generation…
Structures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activity
- M. Funk, Evan T. Judd, E. Marsh, S. Elliott, C. Drennan
- Chemistry, BiologyProceedings of the National Academy of Sciences
- 30 June 2014
The structure of benzylsuccinate synthase reveals the architecture of an enzyme capable of removing aromatic hydrocarbons from polluted environments and illustrates a strategy for controlling the generation and utilization of radicals by glycyl radical enzymes through the use of accessory subunits.
Identification of a monooxygenase from Streptomyces coelicolor A3(2) involved in biosynthesis of actinorhodin: purification and characterization of the recombinant enzyme
Site-directed mutagenesis was used to investigate the role of histidine residues thought to be important in the reaction; mutants lacking His-52 displayed much-reduced activity, consistent with the proposed mechanistic hypothesis that this histidine acts as a general base during catalysis.
Role of zinc in human islet amyloid polypeptide aggregation.
The inhibition of the formation of aggregated and toxic forms of hIAPP by zinc provides a possible mechanism between the recent discovery of linkage between deleterious mutations in the SLC30A8 zinc transporter, which transports zinc into the secretory granule, and type II diabetes.
Coenzyme B12 (cobalamin)-dependent enzymes.
- E. Marsh
- Chemistry, BiologyEssays in biochemistry
- 1 November 1999
The structures of two cobalamin-dependent enzymes, methionine synthase and methylmalonyl-CoA mutase, have been solved and the cobalt is co-ordinated by a histidine ligand from the protein.
Oxygen-independent decarbonylation of aldehydes by cyanobacterial aldehyde decarbonylase: a new reaction of diiron enzymes.
- Debasis Das, B. Eser, Jaehong Han, Aaron Sciore, E. Marsh
- Chemistry, BiologyAngewandte Chemie
- 25 July 2011
An enzymes involved in hydrocarbon biosynthesis, which catalyzes the decarbonylation of long-chain fatty aldehydes to the corresponding alkanes, are of interest both for applications in biofuels production and for the unusual and chemically difficult reactions they catalyze.
Substrate-bound Structures of Benzylsuccinate Synthase Reveal How Toluene Is Activated in Anaerobic Hydrocarbon Degradation*
Background: Benzylsuccinate synthase (BSS) catalyzes the formation of a C—C bond between toluene and fumarate by a radical mechanism. Results: BSS binds substrates in a buried active site and uses…
Aldehyde‐forming fatty acyl‐CoA reductase from cyanobacteria: expression, purification and characterization of the recombinant enzyme
Stearoyl‐CoA was the most effective substrate, being reduced more rapidly than either longer or shorter chain acyl‐CoAs and steady state kinetic analysis indicates that the enzyme operates by a ‘ping‐pong’ mechanism.
Insights into Substrate and Metal Binding from the Crystal Structure of Cyanobacterial Aldehyde Deformylating Oxygenase with Substrate Bound
- B. Buer, Bishwajit Paul, Debasis Das, J. Stuckey, E. Marsh
- ChemistryACS Chemical Biology
- 15 September 2014
The nonheme diiron enzyme cyanobacterial aldehyde deformylating oxygenase, cADO, catalyzes the highly unusual deformylation of aliphatic aldehydes to alkanes and formate. We have determined crystal…
Identification of a Flavin:NADH Oxidoreductase Involved in the Biosynthesis of Actinorhodin
- S. Kendrew, S. Harding, D. Hopwood, E. Marsh
- Biology, ChemistryThe Journal of Biological Chemistry
- 21 July 1995
The subunit structure of the enzyme was investigated by analytical ultracentrifugation, which showed the protein to exist in rapid equilibrium between monomer and dimer forms, and the possible role of this oxidoreductase in the oxidative chemistry of actinorhodin biosynthesis is discussed.