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Literature summary for 2.1.1.184 extracted from

  • Zhong, P.; Pratt, S.D.; Edalji, R.P.; Walter, K.A.; Holzman, T.F.; Shivakumar, A.G.; Katz, L.
    Substrate requirements for ErmC' methyltransferase activity (1995), J. Bacteriol., 177, 4327-4332.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.184

Cloned(Commentary)

Cloned (Comment) Organism
expressed to a high level in Escherichia coli Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0000344
-
 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA Bacillus subtilis
0.0000375
-
 23S rRNA pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA Bacillus subtilis
0.000144
-
 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA Bacillus subtilis
0.00091
-
 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA Bacillus subtilis ErmC is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalyzing the methylation of 23S rRNA at a specific adenine residue (A2085 in Bacillus subtilis) 2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P13956
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA = 2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA a model of RNA-ErmC interaction involving multiple binding sites is proposed from the kinetic data Bacillus subtilis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA ErmC is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalyzing the methylation of 23S rRNA at a specific adenine residue (A2085 in Bacillus subtilis) Bacillus subtilis 2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
 ?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA the specificity of methylation on adenine2085 is confirmed by site-directed mutagenesis. All three mutated domain V fragments, A2085T, A2085G, and A2085C, are methylated to less than 10% of the level observed with the correct domain V RNA fragment. The G2084A change reduces the methylation of the resultant domain V fragment to ca. 12% of the level of the wild-type domain V fragment Bacillus subtilis 2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
 ?
2 S-adenosyl-L-methionine + adenine2085 in a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA can be utilized efficiently as a substrate for methylation at adenine2085 Bacillus subtilis 2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
-
 ?
2 S-adenosyl-L-methionine + adenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
-
 Bacillus subtilis 2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
-
 ?
2 S-adenosyl-L-methionine + adenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T the A2086T change is methylated to ca. 50% of the level of wild-type domain V Bacillus subtilis 2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T
-
 ?
S-adenosyl-L-methionine + 23S rRNA
-
 Bacillus subtilis S-adenosyl-L-homocysteine + 23S rRNA containing N6-dimethyladenine
-
 ?
S-adenosyl-L-methionine + 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
-
 Bacillus subtilis S-adenosyl-L-homocysteine + 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA containing N6-dimethyladenine
-
 ?
S-adenosyl-L-methionine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
-
 Bacillus subtilis S-adenosyl-L-homocysteine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA containing N6-dimethyladenine
-
 ?
S-adenosyl-L-methionine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T
-
 Bacillus subtilis S-adenosyl-L-homocysteine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T containing N6-dimethyladenine
-
 ?

Synonyms

Synonyms Comment Organism
ErmC' methyltransferase
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Bacillus subtilis

General Information

General Information Comment Organism
physiological function ErmC is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalyzing the methylation of 23S rRNA at a specific adenine residue (A2085 in Bacillus subtilis) Bacillus subtilis