Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.80 extracted from

  • Ullah, A.H.J.; Ordal, G.W.
    Purification and characterization of methyl-accepting chemotaxis protein methyltransferase I in Bacillus subtilis (1981), Biochem. J., 199, 795-805.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.80

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ MCP methyltransferase I Bacillus subtilis
S-adenosyl-L-homocysteine
-
 Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
 gel filtration Bacillus subtilis
44000
-
 MCP methyltransferase I Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.000076
-
-
 Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + protein L-glutamate methyltransferase I is unable to methylate E. coli membranes Bacillus subtilis S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
 ?
S-adenosyl-L-methionine + protein L-glutamate membrane protein involved in chemotaxis Bacillus subtilis S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 44000, MCP methyltransferase I, SDS-PAGE Bacillus subtilis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000065
-
 Ca2+
-
 Bacillus subtilis
0.0002
-
 S-adenosyl-L-homocysteine
-
 Bacillus subtilis