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Literature summary extracted from

  • Velletri, P.A.; Billingsley, M.L.; Lovenberg, W.
    Thermal denaturation of rat pulmonary and testicular angiotensin-converting enzyme isozymes. Effects of chelators and CoCl2 (1985), Biochim. Biophys. Acta, 839, 71-82.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.4.15.1 zinc may contribute to the structural integrity and thermal stability of angiotensin-converting enzyme in each tissue Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.15.1 1,10-phenanthroline
-
 Rattus norvegicus
3.4.15.1 captopril
-
 Rattus norvegicus
3.4.15.1 Co2+ testicular enzyme is inhibited, lung enzyme not Rattus norvegicus
3.4.15.1 EDTA
-
 Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.15.1 NaCl
-
 Rattus norvegicus
3.4.15.1 Zinc 0.3 mM ZnCl2 completely reverses the inhibition caused by 0.1 mM EDTA Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.4.15.1 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.15.1 side-chain modification glycoprotein Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.15.1 lung
-
 Rattus norvegicus
-
3.4.15.1 testis
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.15.1 hippuryl-His-Leu + H2O
-
 Rattus norvegicus hippuric acid + His-Leu
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.15.1 additional information
-
 chelators and Co2+ markedly potentiate the thermal denaturation Rattus norvegicus
3.4.15.1 55
-
 lung enzyme looses 50% of the activity after 1.5 min, testicular enzyme looses 50% loss of activity Rattus norvegicus