Words similar to bifunctional
Example sentences for: bifunctional
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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).
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 .
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.
GSPS is a bifunctional enzyme: its synthase domain carries out the ATP-dependent fusion of two glutathione moieties to the polyamine spermidine to form the antioxidant metabolite GSP, while its amidase domain hydrolyzes the amide linkage to release glutathione and spermidine [ 26, 55, 56].
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