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Information on EC 2.1.1.297 - peptide chain release factor N5-glutamine methyltransferase and Organism(s) Thermotoga maritima and UniProt Accession Q9WYV8

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IUBMB Comments
Modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity.
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Thermotoga maritima
UNIPROT: Q9WYV8
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The taxonomic range for the selected organisms is: Thermotoga maritima
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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
+
[peptide chain release factor 1 or 2]-L-glutamine
=
+
[peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
Synonyms
hemk2, hemk1, n5-glutamine methyltransferase, prmc/hemk, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N5-glutamine MTase
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N5-glutamine S-adenosyl-L-methionine dependent methyltransferase
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release factor glutamine methyltransferase
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TM0488
locus name
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.
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
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-
-
?
additional information
?
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the catalytic methyl transfer by methyltransferase HemK is an energy-favored process with an activation barrier of 15.7 kcal/mol and an exothermicity of 12.0 kcal/mol, while the coenzyme-modified HemK is unable to catalyze the methyl transfer because of a substantial barrier of 20.6 kcal/mol and instability of the product intermediate. Therefore the nitrogen analogue of the SAM coenzyme should be a practicable inhibitor for the catalytic methyl transfer by HemK. The protein environment, especially the residues Asn197 and Pro198 in the active site, plays a pivotal role in stabilizing the transition state and regulating the positioning of reactive groups
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-
?
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 + [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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized in the presence of S-adenosylmethionine at 223°C 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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli C41(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoon, H.J.; Kang, K.Y.; Ahn, H.J.; Shim, S.M.; Ha, J.Y.; Lee, S.K.; Mikami, B.; Suh, S.W.
X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-glutamine methyltransferase
Mol. Cells
16
266-269
2003
Thermotoga maritima (Q9WYV8), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9WYV8)
Manually annotated by BRENDA team
Schubert, H.L.; Phillips, J.D.; Hill, C.P.
Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase
Biochemistry
42
5592-5599
2003
Thermotoga maritima (Q9WYV8), Thermotoga maritima DSM 3109 (Q9WYV8)
Manually annotated by BRENDA team
Wu, R.; Cao, Z.
QM/MM study of catalytic methyl transfer by the N5-glutamine SAM-dependent methyltransferase and its inhibition by the nitrogen analogue of coenzyme
J. Comput. Chem.
29
350-357
2008
Thermotoga maritima (Q9WYV8), Thermotoga maritima DSM 3109 (Q9WYV8)
Manually annotated by BRENDA team