EC 3.4.15.1

Base Information

• Chemical Name: EC 3.4.15.1
• CAS No.: 9015-82-1
• Molecular Formula: C2H5NO
• Molecular Weight: 59.0672
• Mol file: 9015-82-1.mol

Synonyms:ACE; ACE(enzyme); Angiotensin I-converting enzyme; Angiotensin-1 converting enzyme;Angiotensin-converting enzyme; Angiotensin-converting enzyme I;Angiotension-converting enzyme; Carboxycathepsin; Carboxypeptidase Zace2;Dipeptidyl carboxypeptidase; Dipeptidyl carboxypeptidase A; Dipeptidylcarboxypeptidase I; Dipeptidyl serine carboxypeptidase; E.C. 3.4.15.1; EC3.4.15.1; Endothelial cell peptidyl dipeptidase; Kininase II; Peptidase P;Peptidyl dipeptidase; Peptidyl dipeptidase A; Peptidyl dipeptidase-4;Peptidyldipeptide hydrolase A; Vasopeptidase; Zinc metallopeptidase Zace1

Chemical Property of EC 3.4.15.1

Chemical Property:

• PSA: 0.00000
• LogP: 0.00000
• Storage Temp.: −20°C

Purity/Quality:

98%,99%, ^*data from raw suppliers

Angiotensin Converting Enzyme ^*data from reagent suppliers

Safty Information:

• Pictogram(s):  
• Hazard Codes: 

MSDS Files:

SDS file from LookChem

Total 1 MSDS from other Authors

Useful:

• Biological functions: The well-known function of ACE is the conversion of Ang I to Ang II and the degradation of BK, which plays an important role in controlling the blood pressure. ACE also acts on other natural substrates, including encephalin, neurotensin, and substance P. Besides being involved in blood pressure control, ACE possesses widespread functions including renal development, male fertility, hematopoiesis, erythropoiesis, myelopoiesis, and immune responses. ACE2 can convert Ang II to Ang1–7, thereby reducing the concentration of Ang II and increasing that of Ang1–7. ACE2 can also convert Ang I to Ang1–9, which is subsequently converted into Ang1–7 by ACE. The high expression of ACE2 favors the balance of Ang1–7 over Ang II, which accounts for the cardioprotective role of ACE2 via the Ang1–7/Mas signaling pathway.
• Description: ACE possesses dual actions to convert Ang I to Ang II, and degrade bradykinin. The development of an ACE inhibitor was the first effective drug for hypertension caused by high renin activity. ACE2 was identified as the receptor for the SARS (severe acute respiratory syndrome) coronavirus, which caused an epidemic in 2002–2003. ACE was discovered in the mid-1950s through the observation that the dialysis of plasma and kidney extract with water and saline before incubation produced two separate pressor substances, Ang I and Ang II, respectively. It was discovered for a second time in 1966 during the characterization of a bradykinin (BK)-degrading enzyme from the kidney. This was named kininase II, which later was found to be the same enzyme as ACE. ACE2 was discovered in 2000 when two independent research groups cloned homologous ACE that could convert Ang I to Ang1–9 and yet also be captopril-insensitive.
• Uses: Angiotensin converting enzyme from rabbit lung has been used:for measuring inhibitory effect of egg white protein hydrolysates on ACE activity by high performance liquid chromatography (HPLC)to measure the ACE inhibition by litchi pericarp and cooked chicken breast using hippuryl-L-histidyl-L-leucine (HHL) as substrate by reverse phase-HPLC (RP-HPLC)3 and HPLC respectively in releasing GPI anchored protein in vitro in few cell lines like HeLa, HEK293 and in vivo in mice sperm.
• Clinical Use: ACE has been the target of hypertension control since the 1970s. ACE inhibitors are prescribed as the sole or combinational treatment for high blood pressure, for its dual effects of lowering Ang II and slowing down BK degradation. In human hypertensive patients, ACE2 levels are lower in both the kidney and heart compared to normotensive volunteers.