Literature summary for 3.4.15.1 extracted from

Wijesekara, I.; Kim, S.K.
Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: prospects in the pharmaceutical industry (2010), Mar. Drugs, 8, 1080-1093.

Search for more literature for 3.4.15.1

Application

Application	Comment	Organism
drug development	marine-derived ACE inhibitors as therapeutic drug candidates to treat hypertension	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
alcacepril	synthetic ACE inhibitor and antihypertensive drug	Homo sapiens
aminoethyl-chitin	with 10%, 50%, and 90% deacetylation	Rattus norvegicus
captopril	synthetic ACE inhibitor and antihypertensive drug	Homo sapiens
captopril	synthetic ACE inhibitor and antihypertensive drug	Rattus norvegicus
chitooligosaccharide derivatives	i.e. COS, chitosan derivatives, polycationic polymers comprised principally of glucosamine units, generated via either chemical or enzymatic hydrolysis of chitosan. ACE inhibitory activity of hetero-COS, derived from crab chitin, is dependent on the degree of deacetylation of chitosan	Homo sapiens
chitooligosaccharide derivatives	i.e. COS, chitosan derivatives, polycationic polymers comprised principally of glucosamine units, generated via either chemical or enzymatic hydrolysis of chitosan. ACE inhibitory activity of hetero-COS, derived from crab chitin, is dependent on the degree of deacetylation of chitosan	Rattus norvegicus
chitosan trimer	effective in lowering blood pressure	Rattus norvegicus
dieckol	deribed from Ecklonia stolonifera	Homo sapiens
dieckol	deribed from Ecklonia stolonifera	Rattus norvegicus
eckol	derived from Ecklonia stolonifera	Homo sapiens
eckol	derived from Ecklonia stolonifera	Rattus norvegicus
enalapril	synthetic ACE inhibitor and antihypertensive drug	Homo sapiens
lisinopril	synthetic ACE inhibitor and antihypertensive drug	Homo sapiens
additional information	nutrient sources of ACE inhibitory peptides derived from marine organisms, enzymes used for hydrolysis, and IC50 values, overview. Tryptophan, tyrosine, proline or phenylalanine at the C-terminal and branched-chain aliphatic amino acids at the N-terminal is suitable for peptides to act as competitive inhibitors by binding with ACE, some peptides also show a non-competitive mechanism. Hydrophobicity of the N-terminus, which is one of the common features of ACE inhibitory peptides, may contribute to the inhibitory activity. The peptides exhibit antihypertensive activity in vivo rather than in vitro. Polyphenolic compounds inhibit ACE activity through sequestration of the enzyme metal factor, Zn2+ ion	Homo sapiens
additional information	ACE inhibitory peptides derived from marine organisms show a strong suppressive effect on systolic blood pressure of spontaneously hypertensive rats, and this antihypertensive activity is similar with captopril, a commercial antihypertensive drug. Hydrophobicity of the N-terminus is one of the common features of ACE inhibitory peptides, and may contribute to the inhibitory activity. No side effect observed on rats after administration of antihypertensive peptides. The peptides exhibit antihypertensive activity in vivo rather than in vitro. An antihypertensive peptide isolated from bonito fish hydrolysate product, is hydrolyzed by ACE to produce a smaller peptide than the initial one, which has 8fold increased ACE inhibitory activity compared with the initial peptide. Polyphenolic compounds inhibit ACE activity through sequestration of the enzyme metal factor, Zn2+ ion	Rattus norvegicus
phlorofucofuroeckol A	derived from Ecklonia stolonifera	Homo sapiens
phlorofucofuroeckol A	derived from Ecklonia stolonifera	Rattus norvegicus
phlorotannins	e.g. from Ahnfeltiopsis flabelliformis, Ecklonia cava, Ecklonia stolonifera, Pelvetia siliqousa, and Undaria pinnatifida, phenolic compounds formed by the polymerization of phloroglucinol or defined as 1,3,5-trihydroxybenzene monomer units and biosynthesized through the acetate-malonate pathway. They are highly hydrophilic components with a wide range of molecular sizes ranging between 126-650 kDa. A closed ring dibenzo-1,4-dioxin moiety may be crucial for ACE inhibitory effects	Homo sapiens
phlorotannins	e.g. from Ahnfeltiopsis flabelliformis, Ecklonia cava, Ecklonia stolonifera, Pelvetia siliqousa, and Undaria pinnatifida, phenolic compounds formed by the polymerization of phloroglucinol or defined as 1,3,5-trihydroxybenzene monomer units and biosynthesized through the acetate-malonate pathway. They are highly hydrophilic components with a wide range of molecular sizes ranging between 126-650 kDa. A closed ring dibenzo-1,4-dioxin moiety may be crucial for ACE inhibitory effects	Rattus norvegicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	required	Homo sapiens
Zn2+	required	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Rattus norvegicus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	ACE is a dipeptidyl carboxypeptidase	Homo sapiens	?	-	?
additional information	ACE is a dipeptidyl carboxypeptidase	Rattus norvegicus	?	-	?

Synonyms

Synonyms	Comment	Organism
ACE	-	Homo sapiens
ACE	-	Rattus norvegicus
angiotensin-converting enzyme	-	Homo sapiens
angiotensin-converting enzyme	-	Rattus norvegicus

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
additional information	-	nutrient sources of ACE inhibitory peptides derived from marine organisms, enzymes used for hydrolysis, and IC50 values, overview	Homo sapiens	additional information
0.0000001	-	-	Rattus norvegicus	captopril
0.000038	-	with 50% deacetylation	Rattus norvegicus	aminoethyl-chitin
0.000064	-	with 10% deacetylation	Rattus norvegicus	aminoethyl-chitin
0.000103	-	with 90% deacetylation	Rattus norvegicus	aminoethyl-chitin
0.0009	-	-	Rattus norvegicus	chitosan trimer
0.0127	-	-	Rattus norvegicus	phlorofucofuroeckol A

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Release 2023.1 (January 2023)