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Literature summary for 2.1.1.190 extracted from

  • Lee, T.T.; Agarwalla, S.; Stroud, R.M.
    A unique RNA fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function (2005), Cell, 120, 599-611.
    View publication on PubMed
Search for more literature for 2.1.1.190

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, the structure of a ternary complex containing RumA, S-adenosylhomocysteine and a covalently bound 23S rRNA fragment(1932–1968) with 5-fluoro-uridine at position 1939 is determined by molecular replacement methods Escherichia coli

Protein Variants

Protein Variants Comment Organism
D265A the specific activity of the mutant enzyme is 830fold lower than that of the wild-type enzyme Escherichia coli
D265E mutant enzyme has no activity Escherichia coli
D363A mutation results in complete loss of activity Escherichia coli
D363N the specific activity of the mutant enzyme is 2fold lower than that of the wild-type enzyme Escherichia coli
E424Q the mutant enzyme displays a biphasic reaction profile with an initial burst phase followed by a slow second phase, mutation results in at least 350fold reduction in the rate of proton abstraction Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0092
-
 uracil1939 in 23S rRNA the enzymatic activity of RumA is measured for a 37-mer RNA (1932–1968) segment lacking the 3' hairpin Escherichia coli
0.034
-
 uracil1939 in 23S rRNA the enzymatic activity of RumA is measured for a 12-mer 5' RNA segment (1932–1943) lacking the 3' hairpin Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the enzyme contains an [Fe4S4] cluster, the iron-sulfur cluster of RumA may have an important role in stabilizing the structure of the central domain Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P55135
-
-

Purification (Commentary)

Purification (Comment) Organism
(His)6-tag enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + uracil1939 in 23S rRNA the enzymatic activity of RumA is measured for a 37-mer 23 RNA segment (1932–1968) and for a 12-mer 5' segment (1932–1943) lacking the 3' hairpin Escherichia coli S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
-
 ?

Synonyms

Synonyms Comment Organism
RumA
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.006
-
 uracil1939 in 23S rRNA the enzymatic activity of RumA is measured for a 12-mer 5' RNA segment (1932–1943) lacking the 3' hairpin Escherichia coli
0.18
-
 uracil1939 in 23S rRNA the enzymatic activity of RumA is measured for a 37-mer RNA (1932–1968) segment lacking the 3' hairpin Escherichia coli