A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin

Yang, Hongdian; Erdös, Ervin G.; Levin, Yehuda

doi:10.1016/0005-2795(70)90017-6

Cited by 500 publications

(263 citation statements)

References 4 publications

Supporting

Mentioning

256

Contrasting

Unclassified

Order By: Relevance

“…ACE generates the powerful vasoconstrictor angiotensin II that removes the C-terminal dipeptide from the lysate of the precursor decapeptide angiotensin I (Skggs et al, 1954). Furthermore, ACE also inactivates the vasodilator bradykinin (Yang et al, 1970).…”

Section: Introductionmentioning

confidence: 99%

Structure and Activity of Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Alaskan Pollack Skin

Byun¹,

Kim²

2002

BMB Reports

110

View full text Add to dashboard Cite

Angiotensin I that converts the enzyme (ACE) inhibitory peptide, Gly-Pro-Leu, previously purified and identified from the Alaskan pollack skin gelatin hydrolysate, were synthesized. In addition, the peptides Gly-Leu-Pro, LeuGly-Pro, Leu-Pro-Gly, Pro-Gly-Leu, Pro-Leu-Gly, GlyPro, and Pro-Leu, which consisted of glycine, proline, and leucine, were synthesized by the solid-phase method. The IC 50 values of each tripeptide − namely Leu-Gly-Pro, GlyLeu-Pro, Gly-Pro-Leu, Pro-Leu-Gly, Leu-Pro-Gly, and Pro-Gly-Leu − were 0.72, 1.62, 2.65, 4.74, 5.73, and 13.93 µM, respectively. The ACE inhibitory activity of these tripeptides was higher than that of dipeptides, such as GlyPro and Pro-Leu with IC 50 values of 252.6 and 337.3 µM, respectively. Among the tripeptides, Leu-Gly-Pro and GlyLeu-Pro had higher inhibitory activity than Gly-Pro-Leu that was isolated from the Alaskan pollack skin gelatin hydrolysate. Among the different types of tripeptides that were examined, the highest ACE inhibitory activity was observed for Leu-Gly-Pro. It had the leucine residue at the N-terminal and proline residue at the C-terminal.

show abstract

Section: Introductionmentioning

confidence: 99%

Structure and Activity of Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Alaskan Pollack Skin

Byun¹,

Kim²

2002

BMB Reports

110

View full text Add to dashboard Cite

show abstract

“…In the present study we showed that LH-RH, which also contains a blocked COOH-terminal amino acid, was cleaved by human ACE at the bond between Leu-7 and Arg-8 to release the COOH- 8 9 10 terminal tripeptide, Arg-Pro-Gly-NH2, similar to the results found with substance P. ACE also hydrolyzed the bond between Trp-3 and Ser-4 to release the NH2-terminal tripeptide, <Glu-His-Trp. This finding was quite unexpected as ACE usually cleaves dipeptides from the COOH terminus of peptide substrates with free COOH-terminal amino acids (8,9) and has not been shown before to cleave at the NH2 terminus. Peptide substrates with free NH2-terminal amino acids are not cleaved at the NH2 terminus by ACE to any significant degree probably because of the positively charged free amino group, which would be repelled by the positively charged arginine in the active center (11,29).…”

Section: Discussionmentioning

confidence: 92%

“…The enzyme was originally named for its ability to convert angiotensin I to angiotensin 11 (5) or to inactivate bradykinin (6,7). After extensive studies with a variety of peptide substrates, it was concluded that ACE cleaves mainly COOH-terminal dipeptides from oligopeptides with a free COOH terminus (8,9). Thus, it was named dipeptidyl carboxypeptidase, or, more correctly, peptidyldipeptide hydrolase (EC 3.4.15.1).…”

mentioning

confidence: 99%

Novel activity of human angiotensin I converting enzyme: release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone.

Skidgel¹,

Erdös²

1985

Proc. Natl. Acad. Sci. U.S.A.

112

View full text Add to dashboard Cite

Angiotensin I converting enzyme (ACE; kininase II; peptidyldipeptide hydrolase, EC 3.4.15.1) cleaves COOH-terminal dipeptides from active peptides containing a free COOH terminus. We investigated the hydrolysis of luteinizing hormone-releasing hormone (LH-RH) by homogeneous human ACE. Although this decapeptide is blocked at both the NH2 and COOH termini, it was metabolized to several peptides, which were separated by HPLC and identified by amino acid analysis. A major product was the NH2-terminal tripep-tide,

show abstract

“…CE has been shown to be identical with kininase II (2). Therefore, its inhibition may lead to reduction in both generation of angiotensin (ANG) II and degradation of kinins.…”

mentioning

confidence: 99%

Effects of Enalapril and Captopril on Urinary Excretion of Kinins and Electrolytes in Stroke-Prone Spontaneously Hypertensive Rats

Kawashima¹,

Kimura²,

Watanabe

et al. 1985

Japanese Journal of Pharmacology

View full text Add to dashboard Cite

Abstract-Urinary excretion of kinins in stroke-prone spontaneously hypertensive (SHRSP) rats was unchanged during oral enalapril (10 mg/kg) or captopril (30 mg/kg) treatment once a day for 8 days compared to vehicle treatment.However, a significant decrease in urinary kinin excretion was observed on the 5th and 7th day compared to the pretreatment value in rats treated with enalapril.Both enalapril and captopril produced a significant reduction in blood pressure when compared to the vehicle.These findings provide no positive evidence to support the hypothesis of possible involvement of renal kinins in the antihypertensive effect of converting enzyme inhibitors in SHRSP rats.

show abstract

A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin

Cited by 500 publications

References 4 publications

Structure and Activity of Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Alaskan Pollack Skin

Structure and Activity of Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Alaskan Pollack Skin

Novel activity of human angiotensin I converting enzyme: release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone.

Effects of Enalapril and Captopril on Urinary Excretion of Kinins and Electrolytes in Stroke-Prone Spontaneously Hypertensive Rats

Contact Info

Product

Resources

About