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Literature summary for 3.4.15.1 extracted from

  • Hooper, N.M.; Turner, A.J.
    Characterization of angiotensin-converting enzyme from pig brain (1986), Biochem. Soc. Trans., 14, 1249-1250.
No PubMed abstract available
Search for more literature for 3.4.15.1

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
170000
-
 x * 170000, one enzyme form from striatum, SDS-PAGE Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification glycoprotein Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
brain striatum, 2 enzyme forms: MW 170000 Da and MW 180000 Da Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O primary cleavage at the Phe8-Gly9 bond followed by succesive dipeptide cleavages from the newly formed C-terminus, cleavage of the Gly9-Leu10 bond is relatively minor Sus scrofa Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
 ?

Subunits

Subunits Comment Organism
? x * 170000, one enzyme form from striatum, SDS-PAGE Sus scrofa