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

BRENDA support

Literature summary for 3.4.15.1 extracted from

  • Oshima, G.; Nagasawa, K.; Kato, J.
    Renal angiotensin I-converting enzyme as a mixture of sialo- and asialo-enzyme, and a rapid purification method (1976), J. Biochem., 80, 477-483.
    View publication on PubMed
Search for more literature for 3.4.15.1

Activating Compound

Activating Compound Comment Organism Structure
Cl- activates Sus scrofa

General Stability

General Stability Organism
resistant to inactivation by trypsin and chymotrypsin Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
KBr activation is lower than with NaCl Sus scrofa
KI activation is lower than with NaCl Sus scrofa
NaF activation is lower than with NaCl Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
 hog
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification the purified enzyme is a mixture of sialo- and asialo-enzyme. Sialic acid residues do not contribute to the catalytic activity of the enzyme Sus scrofa

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney cortex Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
31
-
-
 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoyl-Gly-Gly-Gly + H2O
-
 Sus scrofa benzoyl-Gly + Gly-Gly
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 relatively stable below, with or without Cl- Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
-
-
 Sus scrofa
8.6
-
 asialo-enzyme, hydrolysis of benzoyl-Gly-Gly-Gly Sus scrofa