Words similar to cyclases
Example sentences for: cyclases
How can you use “cyclases” in a sentence? Here are some example sentences to help you improve your vocabulary:
They are likely to function as sensors of diffusible gaseous ligands that activate at least three distinct, downstream signaling pathways: namely phosphotransfer through the two-component systems, methyl ester-dependent chemotactic response and cyclic nucleotide signaling through the diguanylate cyclases/phosphodiesterases.
Classic adenylyl and guanylyl cyclases show a far more sporadic distribution, and are often present in multiple copies fused to a variety of signaling domains such as the cyclic nucleotide binding domains [ 24 ] . Cyclic nucleotide generating activity is not known to exist in a subset of the archaea [ 25 ] , though most of them contain a well-conserved copy of the CYTH domain.
Using sequence profile searches we identify two conserved domains in the N-terminal extensions of the soluble guanylyl cyclases from animals.
These include enzymatic domains such as nucleotide cyclases, histidine and serine/threonine kinases, cNMP phosphodiesterases, receiver domains and several different kinds of ATPases [ 3 4 ] . Non-catalytic domains, like DNA- or RNA-binding modules (eg.
The RDRPs of RNA viruses define one major lineage of nucleic acid polymerases, which additionally includes reverse transcriptases, archaeo-eukaryotic DNA polymerases, and nucleotide cyclases [ 8 9 10 11 12 13 ] . The DNA-dependent RNA polymerase of certain bacteriophages, such as T7, and the archaeo-eukaryotic primase (also detected in some bacteria) are divergent derivatives of the same fold [ 11 14 ] . The core catalytic domain of all these enzymes, the so-called "palm" domain, has an RNA-recognition motif (RRM)-like fold with strategically placed metal-coordinating residues, which form the active site [ 11 15 16 ] . In contrast, bacterial DnaG-type primases (also present in archaea and some eukaryotes) contain a polymerase domain of the Rossmann-like TOPRIM fold, which is shared with topoisomerases and OLD-family nucleases [ 17 18 19 ] . The recently solved structures of the DDRPs from yeast and the thermophilic bacterium Thermus thermophilus indicate that the β' subunit (according to the subunit nomenclature of Escherichia coli DDRP, which we hereinafter employ to designate all orthologs of the respective E. coli subunits) of these enzymes defines another distinct catalytic scaffold, which is unrelated to any of the above template-dependent RNA polymerases [ 20 21 22 23 24 ] . Additionally, the structural and evolutionary affinities of two other template-dependent RNA polymerases, namely RDRPs involved in PTGS [ 25 26 27 ] and primases of herpesviruses [ 28 ] , remain obscure.