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

BRENDA support

Literature summary for 3.4.21.105 extracted from

  • Wu, Z.; Yan, N.; Feng, L.; Oberstein, A.; Yan, H.; Baker, R.P.; Gu, L.; Jeffrey, P.D.; Urban, S.; Shi, Y.
    Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry (2006), Nat. Struct. Mol. Biol., 13, 1084-1091.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the intramembrane enzyme contains six transmembrane helices Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli intramembrane proteolysis regulates diverse biological processes ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains active site structure and catalytic mechanism, structure-function realationship Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information intramembrane proteolysis regulates diverse biological processes Escherichia coli ?
-
?
additional information structural analysis of the enzyme reveals a gating mechanism for substrate entry, cleavage of substrate peptide bonds within the membrane bilayer, the catalytic Ser201 is located at the N terminus of helix alpha4 approximately 10 A below the membrane surface, structure-function realationship, overview Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the rhomboid intramembrane protease family Escherichia coli