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Literature summary for 2.1.1.297 extracted from

  • Mercier, E.; Rodnina, M.
    Co-translational folding trajectory of the HemK helical domain (2018), Biochemistry, 57, 3460-3464 .
    View publication on PubMed
Search for more literature for 2.1.1.297

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information stopped-flow kinetics, linear kinetic model Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y5R4
-
-

Synonyms

Synonyms Comment Organism
HemK
-
 Homo sapiens
Hemk1
-
 Homo sapiens
N5-glutamine methyltransferase
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Homo sapiens

General Information

General Information Comment Organism
additional information the N-terminal alpha-helical domain of the universally conserved N5-glutamine methyltransferase HemK is compacted within the exit tunnel and rearranges into the native fold upon emerging from the ribosome. Analysis of the rapid kinetics of translation and folding monitored by fluorescence resonance energy transfer and photoinduced electron transfer using global fitting to a model for synthesis of the 112-amino acid HemK fragment. The co-translational folding trajectory of HemK starts within the tunnel and passes through four kinetically distinct folding intermediates that may represent sequential docking of helices to a growing compact core. The kinetics of the process is defined entirely by translation Homo sapiens