Literature summary for 3.1.21.5 extracted from

Bist, P.; Sistla, S.; Krishnamurthy, V.; Acharya, A.; Chandrakala, B.; Rao, D.N.
S-adenosyl-L-methionine is required for DNA cleavage by type III restriction enzymes (2001), J. Mol. Biol., 310, 93-109.

Search for more literature for 3.1.21.5

Activating Compound

Activating Compound	Comment	Organism	Structure
N4-adenosyl-N4-methyl-2,4-diaminobutanoic acid	may substitute for S-adenosyl-L-methionine	Escherichia coli
S6-methyl-6-deaminosinefungin	may substitute for S-adenosyl-L-methionine	Escherichia coli
sinefungin	may substitute for S-adenosyl-L-methionine	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
G448S	mutant of Mod subunit, not able to bind S-adenosyl-L-methionine, no DNA cleavage	Escherichia coli
additional information	mutant c2-134, unable to cleave DNA, mutant c2-440, poor ability to cleave DNA	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	enzyme EcoP15I	-

Renatured (Commentary)

Renatured (Comment)	Organism
reconstitution of separated Res and Mod subunits leads to an inactive apoenzyme lacking S-adenosyl-L-methionine, reconstitution in presence of S-adenosyl L-methionine was not successful	Escherichia coli

Subunits

Subunits	Comment	Organism
More	separation of Res and Mod subunits by gel filtration in presence of 2 M NaCl	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	endogenously bound, absolutely required	Escherichia coli

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Release 2023.1 (January 2023)