Words similar to bifunctional
Example sentences for: bifunctional
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I have demonstrated that a gene coding for a bifunctional catalase-peroxidase is likely a transfer from archaea to a variety of pathogenic bacteria, including E. coli O157:H7 [ 9 ] . Although not yet directly implicated in O157:H7 as a virulence factor, this enzyme has been implicated as a virulence factor in Mycobacterium tuberculosis [ 24 26 ] , and in Legionella pneumophila [ 25 ] . Furthermore, this E. coli O157:H7 catalase-peroxidase has been associated with enterohaemorrhagic hemolysin in a variety of shiga-like toxin-producing (verotoxin-producing) E. coli [ 30 31 ] . This correlation of the presence of the catalase-peroxidase in many virulent but not in avirulent strains suggests a direct role in the virulence of enterohemorrhagic E. coli .
When two paralogs of such a bifunctional gene are produced by duplication, each may be driven by positive selection to specialize in one of these functions, which it performs more efficiently than the ancestor gene, leading to the creation of two indispensable genes with distinct functions [ 11].
D. discoideum enzymes, MHCK-B [ 17 ] and MHCK-C (GenBank accession AAC31918, and [ 18 ] ). Several enzymes present in mammalian systems are now recognized as having the same conserved catalytic domain, including the eEF-2 kinases [ 19 ] [ 20 ] and TRP-PLIK, a bifunctional protein with kinase and ion channel activities [ 21 ] . Biochemical analysis with MHCK-B has confirmed that this enzyme phosphorylates D. discoideum myosin II in vitro [ 17 22 ] ). Analysis reported here confirms that MHCK-C also readily phosphorylates D. discoideum myosin II in vitro, supporting a possible direct role for this enzyme in myosin II localization control in vivo.
Although the three capping reactions are universal in eukaryotes, there is a surprising diversity in the genetic organization of the capping enzymes as well as a complete divergence in the structure and catalytic mechanism of the RNA triphosphatase component in "lower" versus "higher" eukaryotic species [ 1 ] . Metazoans and plants have a two-component capping system consisting of a bifunctional triphosphatase-guanylyltransferase polypeptide and a separate methyltransferase polypeptide, whereas fungi contain a three-component system consisting of separate triphosphatase, guanylyltransferase, and methyltransferase gene products.
Rabbit anti-PKA RIα was prepared by synthesizing the N-terminal 18 residues of human RIα protein and conjugating this peptide (MESGSTAASEEARSLREC) to keyhole limpet haemocyanin (KLH) via the bifunctional reagent, m-maleimidobenzoyl-N-hydroxysuccinimide ester (MES).
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