Example sentences for: cyclases

How can you use “cyclases” in a sentence? Here are some example sentences to help you improve your vocabulary:

  • We postulate that these enzymes are likely to chelate 2 divalent cations and are likely follow a bimetal reaction mechanism similar to what has been proposed for nucleotide cyclases, nucleic acid polymerases, or certain phosphoesterases such as those of the HD and DHH superfamilies.

  • PSI-BLAST searches initiated with the C-terminal part of the SGC-specific extension (the region in between the above-detected N-terminal-most domain, and the C-terminal cyclase domain; human SGC1β, region: 200-370) recovered homologous regions from all other animal soluble guanylyl cyclases, and, additionally, N-terminal regions of histidine kinases from Nostoc and Anabaena species (eg.

  • The majority of previously known nucleotide cyclases belong to two major folds.

  • Thus, the HNOB and HNOBA domains resemble functionally similar CACHE and CHASE domains, which have also been acquired by certain eukaryotic lineages via lateral transfer from bacteria [ 14 36 37 ] . A phylogenetic analysis of the guanylyl cyclase domains of the animal SGCs shows that their closest relatives are cyclases from various bacteria such cyanobacteria, and Leptospira (data not shown).

  • 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.


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