Cloning of a potential cytochrome P450 from the Archaeon Sulfolobus solfataricus

  title={Cloning of a potential cytochrome P450 from the Archaeon Sulfolobus solfataricus},
  author={Ruth L Wright and Katherine Harris and Barbara Thurston Solow and R. H. White and Peter J. Kennelly},
  journal={FEBS Letters},
Characterization of the Peroxidase Activity of CYP119, a Thermostable P450 From Sulfolobus acidocaldarius
The cloning, expression, and purification of CYP119, a thermostable enzyme previously thought to derive from Sulfolobus solfataricus, are reported and the peroxidase activity of this enzyme is reported on and the optimization of the associated reaction parameters are reported on.
Crystal Structure of a Thermophilic Cytochrome P450 from the Archaeon Sulfolobus solfataricus *
An extensive clustering of aromatic residues may provide the structural basis for the enhanced thermal stability of CYP119, which has an unprecedented rearrangement of the active site to adapt to the different size and shape of ligands bound to the heme iron.
Preliminary Characterization and Crystal Structure of a Thermostable Cytochrome P450 from Thermus thermophilus *
The second structure of a thermophile cytochrome P450, CYP175A1 from the thermophilic bacterium Thermus thermophilus HB27, has been solved to 1.8-Å resolution and remains conserved despite the low sequence identity between the various P450s.
A novel electron transport system for thermostable CYP175A1 from Thermus thermophilus HB27
CYP175A1 from Thermus thermophilus is a thermophilic cytochrome P450 and has great potential for industrial applications. However, a native electron transport system for CYP175A1 has not been
A Novel Thermostable Cytochrome P450 from Sequence-Based Metagenomics of Binh Chau Hot Spring as a Promising Catalyst for Testosterone Conversion
Redox partner screening revealed that P450-T3 was reduced well by the mammalian AdR-Adx4-108 and the yeast Arh1-Etp1 redox partners.
Isolation of Cytochrome P-450cam from Alkaliphilic bacteriaKocuria sp. DL
Cytochrome P-450 is a terminal oxidase, involved in biotransformation of endogenous and exogenous substances. Cytochrome P-450cam is isozyme present in various bacteria. CYP-450cam was purified from
The Active Site of the Thermophilic CYP119 from Sulfolobus solfataricus *
Protein melting curves indicate that the thermal stability of CYP119 does not depend on the iron spin state or the active site architecture defined by the threonine residues, and independence of thermal stability from active site structural factors should facilitate the engineering of novel thermostable catalysts.
Protein engineering of cytochromes P-450.


Isolation and cloning of a protein-serine/threonine phosphatase from an archaeon
The great degree of sequence conservation between molecules from two distinct phylogenetic domains implies that the members of this enzyme superfamily had evolved as specialized, dedicated protein phosphatases prior to the divergence of members of the Archaea and Eucarya from one another.
The fas operon of Rhodococcus fascians encodes new genes required for efficient fasciation of host plants
Three virulence loci (fas, att, and hyp) of Rhodococcus fascians D188 have been identified on a 200-kb conjugative linear plasmid and genetic analysis revealed at least two new genes that are involved in fasciation development, one of which is only required on older tobacco plants.
Gene structure, organization, and expression in archaebacteria.
The structure of protein and stable RNA-encoding genes cloned and sequenced from each of the major classes of archaebacteria: the methanogens, extreme halophiles, and acid thermophiles are compared.
P450 gene nomenclature based on evolution.
Transcription termination in the archaebacterium Sulfolobus: signal structures and linkage to transcription initiation.
The precise map positions were determined for the 3'-termini of five transcripts of the Sulfolobus virus-like particle SSV1 suggesting that transcription termination can be linked to the re-initiation of RNA synthesis.