A2580

Sigma-Aldrich

Angiotensin Converting Enzyme from porcine kidney

lyophilized powder, ≥10 units/mg protein (Bradford)

Synonym(s):
ACE, Peptidyl-dipeptidase A
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.32

form

lyophilized powder

Quality Level

specific activity

≥10 units/mg protein (Bradford)

shipped in

dry ice

storage temp.

−20°C

Gene Information

pig ... ACE(613133)

General description

ACE is a monomer with molecular weight of ~170 kDa
pH range for activity: 7-8.5
Temperature optimum: 37 °C
Zinc is required for activity
Inhibitors: captopril, enalaprilat, lisinopril etc. (1-10 μM)
Angiotensin converting enzyme (ACE) is encoded by the gene, mRNA-decapping enzyme subunit 1 (DCP1). It is a zinc metalloprotease, which belongs to the M2 family.

Application

Angiotensin converting enzyme from porcine kidney has been used in in vitro angiotensin-converting enzyme (ACE) inhibition assay.

Biochem/physiol Actions

Angiotensin converting enzyme (ACE) catalyzes the conversion of angiotensin I to angiotensin II, which regulates the fluid-electrolyte balance and systemic blood pressure. ACE inhibits the vasodilator, bradykinin. ACE inhibitors are used to treat high blood pressure.
Removes C-terminal dipeptides from susceptible substrates, e.g., angiotensin I and bradykinin.

Unit Definition

One unit will produce 1.0 ·μmole of hippuric acid from Hippuryl-His-Leu per min in 50 mM HEPES and 300 mM NaCl at pH 8.3 at 37 °C.

Physical form

Lyophilized powder containing Tris buffer salts.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Sequence variation in the human angiotensin converting enzyme
Rieder MJ, et al.
Nature Genetics, 22(1), 59-59 (1999)
Effect of angiotensin-converting-enzyme inhibition compared with conventional therapy on cardiovascular morbidity and mortality in hypertension: the Captopril Prevention Project (CAPPP) randomised trial
Hansson L, et al.
Lancet, 353(9153), 611-616 (1999)
Prolyl carboxypeptidase: a forgotten kidney angiotensinase. Focus on "Identification of prolyl carboxypeptidase as an alternative enzyme for processing of renal angiotensin II using mass spectrometry".
Juan Carlos Q Velez
American journal of physiology. Cell physiology, 304(10), C939-C940 (2013-04-05)
Rodrigo A Fraga-Silva et al.
Hypertension (Dallas, Tex. : 1979), 61(6), 1233-1238 (2013-04-24)
Diminished release and function of endothelium-derived nitric oxide coupled with increases in reactive oxygen species production is critical in endothelial dysfunction. Recent evidences have shown that activation of the protective axis of the renin-angiotensin system composed by angiotensin-converting enzyme 2...
A Human Homolog of Angiotensin Converting Enzyme-Cloning and Functional Expression As A Captopril Insensitive Carboxypeptidase
Tipnis SR, et al.
The Journal of Biological Chemistry (2000)

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