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Literature summary for 3.4.15.1 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
Search for more literature for 3.4.15.1

General Stability

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

Inhibitors

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification glycoprotein Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
lung
-
 Rattus norvegicus
-
testis
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

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

Temperature Stability [°C]

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