Information on EC 2.1.1.297 - peptide chain release factor N5-glutamine methyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.1.1.297
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RECOMMENDED NAME
GeneOntology No.
peptide chain release factor N5-glutamine methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[peptide chain release factor 1 or 2]-L-glutamine (N5-glutamine)-methyltransferase
Modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
serovar L2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
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 + [peptide chain release factor 1 or 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
show the reaction diagram
S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
show the reaction diagram
S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + [peptide chain release factor 1 or 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
show the reaction diagram
S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
show the reaction diagram
S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
abundant mRNA expression; abundant mRNA expression
Manually annotated by BRENDA team
abundant mRNA expression in embryonic stem cells, weak expression in differentiated embryonic stem cells, proein is most abundant in undifferentiated embryonic stem cells; abundant mRNA expression in embryonic stem cells, weak expression in differentiated embryonic stem cells, protein is most abundant in undifferentiated embryonic stem cells
Manually annotated by BRENDA team
weak mRNA expression; weak mRNA expression
Manually annotated by BRENDA team
abundant mRNA expression; abundant mRNA expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
isoform HemK1 is detected mainly in the nucleus of COS7 cell lines after 24 h post-transfection; isoform HemK1 is detected mainly in the nucleus of COS7 cell lines after 24 h post-transfection
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
analysis of the crystal structure of the HemK N-terminal domain, PDB ID 1T43
molecular replacement based on the data of Thermotoga maritima enzyme, in complex with the methyl-donor product S-adenosyl-L-homocysteine. Enzyme HemK contains two domains: a putative substrate binding domain at the N-terminus consisting of a five helix bundle and a seven-stranded catalytic domain at the C-terminus that harbors the binding site for S-adenosyl-L-homocysteine. The two domains are linked by a beta-hairpin. The apparent hinge mobility of the two domains may reflect functional importance during the reaction cycle
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crystallized in the presence of S-adenosylmethionine at 223C using ammonium sulfate as the precipitant. X-ray diffraction data are collected to 2.5 A resolution from a native crystal. The crystal is orthorhombic, belonging to the space group I222 (or I2(1)2(1)2(1)), with unit-cell parameters of a = 104.24, b = 118.73, and c = 146.62 A. Two (or three) monomers of recombinant HemK are likely to be present in the crystallographic asymmetric unit
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to 2.2 A resolution. The C-terminal domain of PrmC adopts the canonical S-adenosyl-L-methionine-dependent methyltransferase fold and shares structural similarity with the nucleotide N-methyltransferases in the active site, including use of a conserved (D/N)PPY motif to select and position the glutamine substrate. Residues of the PrmC 197NPPY200 motif form hydrogen bonds that position the planar Gln side chain such that the lone-pair electrons on the nitrogen nucleophile are oriented toward the methyl group of S-adenosyl-Lmethionine. In the product complex, the methyl group remains pointing toward the sulfur, consistent with either an sp3-hybridized, positively charged Gln nitrogen, or a neutral sp2-hybridized nitrogen in a strained conformation. Due to steric overlap within the active site, proton loss and formation of the neutral planar methylamide product are likely to occur during or after product release
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
the isolated N-terminal domain with even a single Ala mutation is almost completely unfolded at 37C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli C41(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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