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

BRENDA support

Literature summary for 2.1.1.179 extracted from

  • Savic, M.; Ilic-Tomic, T.; Macmaster, R.; Vasiljevic, B.; Conn, G.L.
    Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm (2008), J. Bacteriol., 190, 5855-5861.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Micromonospora zionensis

Protein Variants

Protein Variants Comment Organism
D156A no binding of S-adenosyl-L-methionine Micromonospora zionensis
D182A no binding of S-adenosyl-L-methionine Micromonospora zionensis
E205A mutant retains S-adenosyl-L-methionine binding Micromonospora zionensis
E267A mutant retains S-adenosyl-L-methionine binding Micromonospora zionensis
G135A no binding of S-adenosyl-L-methionine Micromonospora zionensis
K199A mutant retains S-adenosyl-L-methionine binding Micromonospora zionensis
R236A mutant retains S-adenosyl-L-methionine binding Micromonospora zionensis

Organism

Organism UniProt Comment Textmining
Micromonospora zionensis Q7M0R2
-
-

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
assay at Micromonospora zionensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45 50 Sgm is fully stable up to 45 to 50°C, after which point the spectra become progressively more like those of an unstructured random coil. No further change is observed beyond 65°C, where all secondary structure appears to be lost Micromonospora zionensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Micromonospora zionensis