Words similar to rossmann
Example sentences for: rossmann
How can you use “rossmann” in a sentence? Here are some example sentences to help you improve your vocabulary:
Whereas both these enzymes are derived versions of the Rossmann fold and bind a dinucleotide cofactor, the SWIRM amino oxidase proteins do not possess equivalents of the unique inserts with residues that allow the SIR2-like proteins to catalyze the deacetylation reaction.
Organic phosphate compounds are the central metabolites of all biological systems [ 1 2 ] . Some are the basic building blocks of nucleic acids, some like ATP and GTP, are additionally, cellular energy stores, others like cAMP or cGMP are messengers in signal transduction, and, yet others, such as FAD, NAD, thiamine phosphates and pyridoxal phosphate are cofactors for a range of enzymes [ 1 2 ] . Protein domains belonging to a relatively small set of structural folds are known to bind or catalyze reactions that utilize these organic phosphate compounds (see SCOP database: http://scop.mrc-lmb.cam.ac.uk/scop/) [ 3 4 ] . Several of these folds trace back to some of the earliest phases of the evolution of the protein world, and participate in a wide range of disparate biological functions in extant proteins [ 4 5 ] . Some folds, such as the P-loop fold, the Rossmann fold and the Hsp70-like fold, have been well studied, and comprise mainly of dedicated nucleotide binding or hydrolyzing proteins [ 6 7 8 9 ] . Others, such as the palm-domain, which is found in adenylyl cyclases and various nucleic acid polymerases, belong to more generalized protein folds that contain representatives with diverse biochemical activities [ 4 10 11 ] . Current availability of extensive genome sequence data, allows one to identify less numerous, nevertheless biological important organic phosphate-binding domains that may have previous eluded detection.
These include the glycine-rich loop bounded by a β-strand and an a helix that is typical of Rossmann fold nucleotide-binding proteins, a conserved glutamate specific to the amino oxidase family, that interacts with ribose in FAD and other residues of the substrate and cofactor-binding site.
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