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Literature summary for 3.4.21.53 extracted from

  • Arends, J.; Griego, M.; Thomanek, N.; Lindemann, C.; Kutscher, B.; Meyer, H.E.; Narberhaus, F.
    An integrated proteomic approach uncovers novel substrates and functions of the Lon protease in Escherichia coli (2018), Proteomics, 18, e1800080 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene lon, functional recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain CH1019 Escherichia coli

Protein Variants

Protein Variants Comment Organism
S679A site-directed mutagenesis, the Lon trapping variant is able to translocate substrates but unable to degrade them, it is established and used for substrate determinations by mass spectrometry Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CysB + H2O Escherichia coli a positive cysDNC operon transcription regulator ?
-
?
CysD + H2O Escherichia coli a subunit of the sulfate adenylyltransferase, low activity ?
-
?
GlyA + H2O Escherichia coli a protein of the MetR regulon ?
-
?
MetR + H2O Escherichia coli a protein of the MetR regulon, transcriptional regulator of metE expression ?
-
?
additional information Escherichia coli a quantitative Super-SILAC (stable isotope labeling with amino acids in cell culture) mass spectrometry approach and analysis of proteomes of a lon mutant and a strain producing the protease are employed to determine substrate specificity and Lon-dependent physiological functions. The recognition mechanisms of known Lon substrates are highly diverse. Misfolded proteins are mainly recognized by short, hydrophobic stretches normally buried in the core of natively folded proteins. In contrast, recognition of SulA occurs via its C-terminus with a critical histidine and tyrosine at its very end ?
-
?
SulA + H2O Escherichia coli a cell division inhibitor ?
-
?
ZntR + H2O Escherichia coli
-
?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9M0
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain CH1019 by nickel affinity chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CysB + H2O a positive cysDNC operon transcription regulator Escherichia coli ?
-
?
CysD + H2O a subunit of the sulfate adenylyltransferase, low activity Escherichia coli ?
-
?
GlyA + H2O a protein of the MetR regulon Escherichia coli ?
-
?
MetR + H2O a protein of the MetR regulon Escherichia coli ?
-
?
MetR + H2O a protein of the MetR regulon, transcriptional regulator of metE expression Escherichia coli ?
-
?
additional information a quantitative Super-SILAC (stable isotope labeling with amino acids in cell culture) mass spectrometry approach and analysis of proteomes of a lon mutant and a strain producing the protease are employed to determine substrate specificity and Lon-dependent physiological functions. The recognition mechanisms of known Lon substrates are highly diverse. Misfolded proteins are mainly recognized by short, hydrophobic stretches normally buried in the core of natively folded proteins. In contrast, recognition of SulA occurs via its C-terminus with a critical histidine and tyrosine at its very end Escherichia coli ?
-
?
SulA + H2O
-
Escherichia coli ?
-
?
SulA + H2O a cell division inhibitor Escherichia coli ?
-
?
ZntR + H2O
-
Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
ATP-dependent lon protease
-
Escherichia coli

General Information

General Information Comment Organism
malfunction a Lon trapping variant, which is able to translocate substrates but unable to degrade them, is established and used for substrate determinations by mass spectrometry Escherichia coli
physiological function a quantitative Super-SILAC (stable isotope labeling with amino acids in cell culture) mass spectrometry approach and analysis of proteomes of a lon mutant and a strain producing the protease are employed to determine substrate specificity and Lon-dependent physiological functions, Lon affected proteins, overview. Fundamental functions of Lon in sulfur assimilation, nucleotide biosynthesis, amino acid and central energy metabolism, besides the superoxide stress response function. Lon protease affects the MetR regulon and function of proteins MetE and MetR Escherichia coli