Words similar to bifunctional
Example sentences for: bifunctional
How can you use “bifunctional” in a sentence? Here are some example sentences to help you improve your vocabulary:
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.
In C. elegans , two genes each encode unusual bifunctional enzymes containing both isocitrate lyase and malate synthase domains [ 49 ] . Since the isocitrate lyase domain lies within the amino-terminal half of the C. elegans bifunctional enzyme and none of the Meloidogyne EST reads stretches across both domains, further sequencing of the 3' end of cDNA clones from the M. hapla or M. javanica isocitrate lyase ESTs will be necessary to determine whether the Meloidogyne genus contains a bifunctional glyoxylate enzyme homolog similar to that of
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 .
Examples are the bifunctional proteins ThrA (aspartokinase I and homoserine dehydrogenase I) and MetL (aspartokinase II and homoserine dehydrogenase II) where only the amino-terminal modules representing the kinase activities have been identified on the basis of their sequence similarity to the E. coli unimodular aspartokinase III (LysC).
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].
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