Literature summary for 2.1.1.37 extracted from

Mondal, M.; Yang, Y.; Yang, L.; Yang, W.; Gao, Y.Q.
Role of conformational fluctuations of protein toward methylation in DNA by cytosine-5-methyltransferase (2018), J. Chem. Theory Comput., 14, 6679-6689 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulations. The free energy profiles for the flipping of target cytosine into the enzyme active site support the major groove base eversion pathway. The closed state of enzyme increases the free energy barrier, whereas the open state reduces it. The interactions of the key loop residues of protein with cognate DNA alter the protein motions, and modulation of protein fluctuations relates to the closed catalytic complex formation. Methylation of cytosine in the active site of the closed complex destabilizes the interactions of catalytic loop residues with cognate DNA and reduces the stability of the closed state	Haemophilus parahaemolyticus

Crystallization (Comment)

Organism

molecular dynamics simulations. The free energy profiles for the flipping of target cytosine into the enzyme active site support the major groove base eversion pathway. The closed state of enzyme increases the free energy barrier, whereas the open state reduces it. The interactions of the key loop residues of protein with cognate DNA alter the protein motions, and modulation of protein fluctuations relates to the closed catalytic complex formation. Methylation of cytosine in the active site of the closed complex destabilizes the interactions of catalytic loop residues with cognate DNA and reduces the stability of the closed state

Haemophilus parahaemolyticus

Organism

Organism	UniProt	Comment	Textmining
Haemophilus parahaemolyticus	P05102	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)