Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.13.21 extracted from

  • Yadav, P.; Goyal, V.D.; Gaur, N.K.; Kumar, A.; Gokhale, S.M.; Makde, R.D.
    Structure of Asp-bound peptidase E from Salmonella enterica Active site at dimer interface illuminates Asp recognition (2018), FEBS Lett., 592, 3346-3354.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
aspartate-bound structure at 1.83 A resolution. The enzyme forms a dimer, and the active site is located at the dimer interface. The stringent aspartate specificity of the enzyme is due to electrostatics and molecular complementarity in the active site Salmonella enterica subsp. enterica serovar Typhimurium

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium P36936
-
-

Synonyms

Synonyms Comment Organism
PepE
-
Salmonella enterica subsp. enterica serovar Typhimurium