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Literature summary for 3.4.11.1 extracted from

  • Nguyen Le Minh, P.; Nadal, M.; Charlier, D.
    The trigger enzyme PepA (aminopeptidase A) of Escherichia coli, a transcriptional repressor that generates positive supercoiling (2016), FEBS Lett., 590, 1816-1825 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene pepA, recombinant overexpression in Escherichia coli strain JM101 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P68767
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PepA-induced DNA deformations revealed by DNase I footprinting and AFM imaging of 1:1 stoichiometric PepA-DNA complexes Escherichia coli ?
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?

Synonyms

Synonyms Comment Organism
aminopeptidase A
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Escherichia coli
PepA
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Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Escherichia coli

General Information

General Information Comment Organism
physiological function trigger enzymes combine metabolic function with regulation of gene expression. Escherichia coli aminopeptidase A (PepA) is a trigger enzyme endowed with catalytic activity and DNA-binding properties prominent in transcriptional regulation and site-specific DNA recombination. PepA is a repressor in its own right, capable of specifically inhibiting transcription initiation at promoter P1 of the carAB operon, encoding carbamoylphosphate synthase. Furthermore, PepA binding constrains a single positive supercoil in the carP1 control region. Such a topological event is understood to constitute an impediment to transcription initiation and may serve as a mechanism to regulate gene expression. The observed inhibitory effect of PepA at carP1 is specific Escherichia coli