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Information on EC 2.1.1.297 - peptide chain release factor N5-glutamine methyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9Y5R4

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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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Homo sapiens
UNIPROT: Q9Y5R4
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
[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 methyltransferase
-
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.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
stopped-flow kinetics, linear kinetic model
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HEMK1_HUMAN
338
0
38231
Swiss-Prot
Mitochondrion (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L27A/L28A
site-directed mutagenesis
L28A
site-directed mutagenesis, the L28A mutation reduces the in vitro denaturation temperature of HemK-N-terminal domain from 50°C to 30°C
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene HEMK1, recombinant expression of isolated N-terminal domain and of truncated mutants in Escherichia coli, cotranslational folding of the HemK N-terminal domain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mercier, E.; Rodnina, M.
Co-translational folding trajectory of the HemK helical domain
Biochemistry
57
3460-3464
2018
Homo sapiens (Q9Y5R4)
Manually annotated by BRENDA team
Kemp, G.; Kudva, R.; de la Rosa, A.; von Heijne, G.
Force-profile analysis of the cotranslational folding of HemK and filamin domains comparison of biochemical and biophysical folding assays
J. Mol. Biol.
431
1308-1314
2019
Homo sapiens (Q9Y5R4)
-
Manually annotated by BRENDA team