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Literature summary extracted from

  • Mojallal-Tabatabei, Z.; Asoodeh, A.; Housaindokht, M.R.; Chamani, J.
    Purification and biochemical characterization of angiotensin I-converting enzyme (ACE) from ostrich lung the effect of 2,2,2-trifluoroethanol on ACEconformation and activity (2013), Process Biochem., 48, 1091-1098 .
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.15.1 cetyltrimethylammonium bromide CTAB, activates at 0.1-1.0 mM Struthio camelus australis
3.4.15.1 SDS activates at 0.1 mM Struthio camelus australis
3.4.15.1 Triton X-100 activates at 0.01%, inhibits at 1.0-10.0% Struthio camelus australis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.15.1 Ca2+ inhibitory at concentrations above 1 mM Struthio camelus australis
3.4.15.1 captopril
-
 Struthio camelus australis
3.4.15.1 Co2+ inhibitory at concentrations above 1 mM Struthio camelus australis
3.4.15.1 EDTA complete inhibition at 0.01 mM Struthio camelus australis
3.4.15.1 Mg2+ inhibitory at concentrations above 1 mM Struthio camelus australis
3.4.15.1 additional information PMSF has no effect on the ACE activity Struthio camelus australis
3.4.15.1 o-phenanthroline complete inhibition at 0.35 mM Struthio camelus australis
3.4.15.1 trifluoroethanol TFE, stabilizes ACE at low concentrations, while acts as a denaturant at higher concentration (20%). Secondary and tertiary structure and activity of ACE in the absence and presence of TFE are investigated using circular dichroism, fluorescence quenching, and UV-visible spectroscopy, respectively Struthio camelus australis
3.4.15.1 Triton X-100 activates at 0.01%, inhibits at 1.0-10.0% Struthio camelus australis
3.4.15.1 Zn2+ inhibitory at concentrations above 1 mM Struthio camelus australis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.15.1 0.08
-
 N-(3-[2-furyl]acryloyl)-L-phenylalanylglycylglycine pH 7.5, 22°C Struthio camelus australis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.15.1 Co2+ activates, but to a lesser extent than Zn2+ Struthio camelus australis
3.4.15.1 Mn2+ activates, but to a lesser extent than Zn2+ Struthio camelus australis
3.4.15.1 Zn2+ required, activates Struthio camelus australis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.15.1 200000
-
 gel filtration Struthio camelus australis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.15.1 angiotensin I + H2O Struthio camelus australis
-
 angiotensin II + His-Leu
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.15.1 Struthio camelus australis A0A093HJH8
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.15.1 glycoprotein ACE is highly glycosylated Struthio camelus australis

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.15.1 native enzyme 447fold from lung by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography, followed by ultrafiltration Struthio camelus australis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.15.1 lung
-
 Struthio camelus australis
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.15.1 147.52
-
 purified native enzyme, pH 7.5, 22°C, substrate N-(3-[2-furyl]acryloyl)-L-phenylalanylglycylglycine Struthio camelus australis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.15.1 angiotensin I + H2O
-
 Struthio camelus australis angiotensin II + His-Leu
-
 ?
3.4.15.1 N-(3-[2-furyl]acryloyl)-L-phenylalanylglycylglycine + H2O
-
 Struthio camelus australis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.15.1 ACE
-
 Struthio camelus australis
3.4.15.1 angiotensin I-converting enzyme
-
 Struthio camelus australis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.15.1 22
-
 assay at room temperature Struthio camelus australis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.15.1 35
-
 purified native enzyme, 30 min, completely stable up to Struthio camelus australis
3.4.15.1 55
-
 purified native enzyme, 30 min, 90% activity reamining Struthio camelus australis
3.4.15.1 60
-
 purified native enzyme, 30 min, inactivation Struthio camelus australis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.15.1 987.3
-
 N-(3-[2-furyl]acryloyl)-L-phenylalanylglycylglycine pH 7.5, 22°C Struthio camelus australis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.15.1 7.5
-
-
 Struthio camelus australis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.15.1 6.5 10.5 activity range, inactive below pH 6.5 and above pH 10.5 Struthio camelus australis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.15.1 0.0000166
-
 captopril pH 7.5, 22°C Struthio camelus australis

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.4.15.1 0.0000365
-
 pH 7.5, 22°C Struthio camelus australis captopril

General Information

EC Number General Information Comment Organism
3.4.15.1 additional information secondary and tertiary structure and activity of ACE is investigated using circular dichroism, fluorescence quenching, and UV-visible spectroscopy, respectively Struthio camelus australis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.4.15.1 123417
-
 N-(3-[2-furyl]acryloyl)-L-phenylalanylglycylglycine pH 7.5, 22°C Struthio camelus australis