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Literature summary for 2.7.13.3 extracted from

  • McCleary, W.R.; Zusman, D.R.
    Purification and characterization of the Myxococcus xanthus FrzE protein shows that it has autophosphorylation activity (1990), J. Bacteriol., 172, 6661-6668.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Myxococcus xanthus

Organism

Organism UniProt Comment Textmining
Myxococcus xanthus P18769
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein autophosphorylation Myxococcus xanthus

Purification (Commentary)

Purification (Comment) Organism
recombinant FrzE protein is overproduced in Escherichia coli and purified from inclusion bodies Myxococcus xanthus

Source Tissue

Source Tissue Comment Organism Textmining
additional information FrzE is clearly present during vegetative growth and at much lower levels during development Myxococcus xanthus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protein + ATP autophosphorylation Myxococcus xanthus ?
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?
protein + ATP a model of the mechanism of FrzE phosphorylation: autophosphorylation initially occurs at a conserved His residue within the "CheA" domain and then, via an intramolecular transphosphorylation, is transferred to a conserved aspartate residue within the "CheY" domain Myxococcus xanthus ?
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?

Synonyms

Synonyms Comment Organism
FrzE
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Myxococcus xanthus
gliding motility regulatory protein
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Myxococcus xanthus