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Phosphorylation, one of the more recognizable post-translational modifications, is catalyzed by kinases while the reverse reaction is carried out by phosphatases.
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Histone modifications are catalyzed by a number of enzyme complexes, including the NuRD/Mi2 complex [4].
These modifications are catalyzed by small nucleolar ribonucleoparticles (snoRNPs) through specific base-paring between their RNA component (snoRNA) with the surrounding of the position to be modified.
These modifications are catalyzed by distinct enzymes.
Most of these modifications are catalyzed by specific enzymes that have evolved for their respective tasks.
The snoRNA-dependent modifications are catalyzed by small nucleolar ribonucleoprotein particles (snoRNPs).
Histone modifications are catalyzed by many enzymes such as histone acetyltransferases (HATs), histone deacetylases (HDACs), histone methyltransferases (HMTs), and histone demethylases (HDMs).
The key steps in carotenoid biosynthetic pathway predominantly targeted for transgenic modifications are catalyzed by enzymes such as PSY, PDS and LCY-B.
NAD+-dependent post-translational protein modifications are catalyzed by several enzyme families, including PARPs and the sirtuin family of NAD+-dependent class III histone deacetylases (SIRTs) [ 8, 65, 66].
This modification is catalyzed by poly(ADP-ribose) polymerase (PARP) family of enzymes.
It is recognized that histone modification is catalyzed by several enzymes which modulate the histone markers.
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