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

BRENDA support

Literature summary for 3.4.15.1 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
Search for more literature for 3.4.15.1

Activating Compound

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

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ inhibitory at concentrations above 1 mM Struthio camelus australis
captopril
-
 Struthio camelus australis
Co2+ inhibitory at concentrations above 1 mM Struthio camelus australis
EDTA complete inhibition at 0.01 mM Struthio camelus australis
Mg2+ inhibitory at concentrations above 1 mM Struthio camelus australis
additional information PMSF has no effect on the ACE activity Struthio camelus australis
o-phenanthroline complete inhibition at 0.35 mM Struthio camelus australis
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
Triton X-100 activates at 0.01%, inhibits at 1.0-10.0% Struthio camelus australis
Zn2+ inhibitory at concentrations above 1 mM Struthio camelus australis

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Struthio camelus australis A0A093HJH8
-
-

Posttranslational Modification

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

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
lung
-
 Struthio camelus australis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Struthio camelus australis

pH Range

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

Ki Value [mM]

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

IC50 Value

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

General Information

General Information Comment Organism
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]

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