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Information on EC 2.1.1.177 - 23S rRNA (pseudouridine1915-N3)-methyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A8I8

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IUBMB Comments
YbeA does not methylate uridine at position 1915 .
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This record set is specific for:
Escherichia coli
UNIPROT: P0A8I8
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
pseudouridine methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
m3Psi methyltransferase
-
pseudouridine methyltransferase
-
Psi1915-specific methyltransferase
-
rRNA large subunit methyltransferase H
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA = S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
show the reaction diagram
mechanism: the enzyme docks into the ribosomal A site without encroaching into the P site. YbeA makes extensive interface contacts with both the 30S and 50S subunits to align its active site cofactor adjacent to nucleotide C1915
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (pseudouridine1915-N3)-methyltransferase
YbeA does not methylate uridine at position 1915 [1].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA
S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA
S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003 - 0.006
pseudouridine1915 in 23S rRNA
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017 - 0.04
pseudouridine1915 in 23S rRNA
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 0.09
pseudouridine1915 in 23S rRNA
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
methylation by YbeA possibly functions as a stamp of approval signifying that the 50S subunit has engaged in translational initiation
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36800
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of RlmH bound to S-adenosyl-methionine (SAM) and the inhibitor sinefungin. In the dimer, one monomer provides the SAM-binding site, whereas the conserved C-terminal tail of the second monomer provides residues essential for catalysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E138A
loss of activity, equilibrium dissociation constants for the first SAM binding site in the RlmH dimer is similar to wild-type
E138Q
loss of activity, equilibrium dissociation constants for the first SAM binding site in the RlmH dimer is similar to wild-type
H129A
about 17% of wild-type activity
H153F
loss of activity, equilibrium dissociation constants for the first SAM binding site in the RlmH dimer is similar to wild-type
R142A
about 3% of wild-type activity
R154A
loss of activity, equilibrium dissociation constants for the first SAM binding site in the RlmH dimer is similar to wild-type
Y152F
loss of activity, equilibrium dissociation constants for the first SAM binding site in the RlmH dimer is similar to wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminal His6-tagged YbeA
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mallam, A.L.; Jackson, S.E.
A comparison of the folding of two knotted proteins: YbeA and YibK
J. Mol. Biol.
366
650-665
2007
Escherichia coli (P0A8I8)
Manually annotated by BRENDA team
Ero, R.; Peil, L.; Liiv, A.; Remme, J.
Identification of pseudouridine methyltransferase in Escherichia coli
RNA
14
2223-2233
2008
Escherichia coli (P0A8I8), Escherichia coli
Manually annotated by BRENDA team
Purta, E.; Kaminska, K.H.; Kasprzak, J.M.; Bujnicki, J.M.; Douthwaite, S.
YbeA is the m3Psi methyltransferase RlmH that targets nucleotide 1915 in 23S rRNA
RNA
14
2234-2244
2008
Escherichia coli (P0A8I8), Escherichia coli
Manually annotated by BRENDA team
Koh, C.S.; Madireddy, R.; Beane, T.J.; Zamore, P.D.; Korostelev, A.A.
Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine
Sci. Rep.
7
969
2017
Escherichia coli (P0A8I8)
Manually annotated by BRENDA team