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

BRENDA support

Literature summary extracted from

  • Iturrioz, X.; Reaux-Le Goazigo, A.; Llorens-Cortes, C.
    Aminopeptidase inhibitors as anti-hypertensive drugs (2004), Aminopetidases in Biology and Disease (Hooper, N. M. ; Lendaechel, U. , eds. ) Springer, 2, 229-250.
No PubMed abstract available

Application

EC Number Application Comment Organism
3.4.11.7 drug development the enzyme is a target for design of specific inhibitors Mus musculus
3.4.11.7 drug development the enzyme is a target for design of specific inhibitors Homo sapiens
3.4.11.7 drug development the enzyme is a target for design of specific inhibitors Rattus norvegicus
3.4.11.7 drug development the enzyme is a target for design of specific inhibitors Sus scrofa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.7 gene APA, DNA and amino acid sequence determination and analysis Homo sapiens
3.4.11.7 gene APA, DNA and amino acid sequence determination and analysis Rattus norvegicus
3.4.11.7 gene APA, DNA and amino acid sequence determination and analysis Sus scrofa
3.4.11.7 gene APA, DNA and amino acid sequence determination and analysis, genetic organization and structure Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
3.4.11.7 additional information construction of active site residue mutants Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.7 amastatin inhibits the enzyme and blocks the metabolism of brain angiotensin II and III Homo sapiens
3.4.11.7 amastatin inhibits the enzyme and blocks the metabolism of brain angiotensin II and III Mus musculus
3.4.11.7 amastatin inhibits the enzyme and blocks the metabolism of brain angiotensin II and III Rattus norvegicus
3.4.11.7 amastatin inhibits the enzyme and blocks the metabolism of brain angiotensin II and III Sus scrofa
3.4.11.7 bestatin inhibits the enzyme and blocks the metabolism of brain angiotensin II and III Homo sapiens
3.4.11.7 bestatin inhibits the enzyme and blocks the metabolism of brain angiotensin II and III Mus musculus
3.4.11.7 bestatin inhibits the enzyme and blocks the metabolism of brain angiotensin II and III Rattus norvegicus
3.4.11.7 bestatin inhibits the enzyme and blocks the metabolism of brain angiotensin II and III Sus scrofa
3.4.11.7 Ca2+ substrate-specific inhibition, overview Homo sapiens
3.4.11.7 Ca2+ substrate-specific inhibition, overview Mus musculus
3.4.11.7 Ca2+ substrate-specific inhibition, overview Rattus norvegicus
3.4.11.7 Ca2+ substrate-specific inhibition, overview Sus scrofa
3.4.11.7 Cd2+
-
Homo sapiens
3.4.11.7 Cd2+
-
Mus musculus
3.4.11.7 Cd2+
-
Rattus norvegicus
3.4.11.7 Cd2+
-
Sus scrofa
3.4.11.7 Cu2+
-
Homo sapiens
3.4.11.7 Cu2+
-
Mus musculus
3.4.11.7 Cu2+
-
Rattus norvegicus
3.4.11.7 Cu2+
-
Sus scrofa
3.4.11.7 EC33 highly selective APA inhibitor Homo sapiens
3.4.11.7 EC33 highly selective APA inhibitor Mus musculus
3.4.11.7 EC33 highly selective APA inhibitor Rattus norvegicus
3.4.11.7 EC33 highly selective APA inhibitor Sus scrofa
3.4.11.7 Hg2+
-
Homo sapiens
3.4.11.7 Hg2+
-
Mus musculus
3.4.11.7 Hg2+
-
Rattus norvegicus
3.4.11.7 Hg2+
-
Sus scrofa
3.4.11.7 Ni2+
-
Homo sapiens
3.4.11.7 Ni2+
-
Mus musculus
3.4.11.7 Ni2+
-
Rattus norvegicus
3.4.11.7 Ni2+
-
Sus scrofa
3.4.11.7 Zn2+
-
Homo sapiens
3.4.11.7 Zn2+
-
Mus musculus
3.4.11.7 Zn2+
-
Rattus norvegicus
3.4.11.7 Zn2+
-
Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.11.7 membrane bound, type II integral membrane protein, the enzyme contains an ectodomain Mus musculus 16020
-
3.4.11.7 membrane bound, type II integral membrane protein, the enzyme contains an ectodomain Homo sapiens 16020
-
3.4.11.7 membrane bound, type II integral membrane protein, the enzyme contains an ectodomain Rattus norvegicus 16020
-
3.4.11.7 membrane bound, type II integral membrane protein, the enzyme contains an ectodomain Sus scrofa 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.7 Ca2+ activates, best at 1 mM, substrate-specific activation Mus musculus
3.4.11.7 Ca2+ activates, best at 1 mM, substrate-specific activation Homo sapiens
3.4.11.7 Ca2+ activates, best at 1 mM, substrate-specific activation Rattus norvegicus
3.4.11.7 Ca2+ activates, best at 1 mM, substrate-specific activation Sus scrofa
3.4.11.7 Zn2+ zinc-metallopeptidase, the enzyme contains the zinc-binding motif HEXXH Homo sapiens
3.4.11.7 Zn2+ zinc-metallopeptidase, the enzyme contains the zinc-binding motif HEXXH Rattus norvegicus
3.4.11.7 Zn2+ zinc-metallopeptidase, the enzyme contains the zinc-binding motif HEXXH Sus scrofa
3.4.11.7 Zn2+ zinc-metallopeptidase, the enzyme contains the zinc-binding motif HEXXH residues 385-389 with catalytically important Glu386 Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.7 250000 300000
-
Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.11.7 angiotensin III + H2O Mus musculus the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension angiotensin IV + Arg
-
ir
3.4.11.7 angiotensin III + H2O Homo sapiens the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension angiotensin IV + Arg
-
ir
3.4.11.7 angiotensin III + H2O Rattus norvegicus the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension angiotensin IV + Arg
-
ir
3.4.11.7 angiotensin III + H2O Sus scrofa the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension angiotensin IV + Arg
-
ir
3.4.11.7 additional information Mus musculus the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview ?
-
?
3.4.11.7 additional information Homo sapiens the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview ?
-
?
3.4.11.7 additional information Rattus norvegicus the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview ?
-
?
3.4.11.7 additional information Sus scrofa the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.7 Homo sapiens
-
-
-
3.4.11.7 Mus musculus
-
-
-
3.4.11.7 Rattus norvegicus
-
-
-
3.4.11.7 Rattus norvegicus
-
WKY rats
-
3.4.11.7 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.11.7 glycoprotein N-linked glycans Mus musculus
3.4.11.7 glycoprotein N-linked glycans Homo sapiens
3.4.11.7 glycoprotein N-linked glycans Rattus norvegicus
3.4.11.7 glycoprotein N-linked glycans Sus scrofa

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.11.7 release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide active site structure and organization Homo sapiens
3.4.11.7 release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide active site structure and organization Rattus norvegicus
3.4.11.7 release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide active site structure and organization Sus scrofa
3.4.11.7 release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide active site structure and organization, modeling, residues Glu352, Glu386, Tyr471, and Glu408 are important in catalysis Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.11.7 adrenal gland
-
Homo sapiens
-
3.4.11.7 B-lymphocyte immature B-lineage cell Mus musculus
-
3.4.11.7 B-lymphocyte immature B-lineage cell Homo sapiens
-
3.4.11.7 B-lymphocyte immature B-lineage cell Rattus norvegicus
-
3.4.11.7 B-lymphocyte immature B-lineage cell Sus scrofa
-
3.4.11.7 bile duct
-
Homo sapiens
-
3.4.11.7 bone marrow
-
Mus musculus
-
3.4.11.7 bone marrow
-
Homo sapiens
-
3.4.11.7 bone marrow
-
Rattus norvegicus
-
3.4.11.7 bone marrow
-
Sus scrofa
-
3.4.11.7 brain pericyte Mus musculus
-
3.4.11.7 brain pericyte Homo sapiens
-
3.4.11.7 brain pericyte Rattus norvegicus
-
3.4.11.7 brain pericyte Sus scrofa
-
3.4.11.7 brain pericyte and almost all structures, hyperactive in RAS and SHR, distribution overview Rattus norvegicus
-
3.4.11.7 epididymis basement membrane Homo sapiens
-
3.4.11.7 epithelium
-
Homo sapiens
-
3.4.11.7 gall bladder epithelium
-
Homo sapiens
-
3.4.11.7 heart
-
Homo sapiens
-
3.4.11.7 hepatocyte
-
Homo sapiens
-
3.4.11.7 liver bile canaliculi Homo sapiens
-
3.4.11.7 lung
-
Homo sapiens
-
3.4.11.7 ovary theca interna Homo sapiens
-
3.4.11.7 pancreas interlobular ducts Homo sapiens
-
3.4.11.7 pericyte brain Mus musculus
-
3.4.11.7 pericyte brain Homo sapiens
-
3.4.11.7 pericyte brain Rattus norvegicus
-
3.4.11.7 pericyte brain Sus scrofa
-
3.4.11.7 placenta syncytiotrophoblast cells Homo sapiens
-
3.4.11.7 syncytiotrophoblast
-
Homo sapiens
-
3.4.11.7 thymus stromal cells of the cortex Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.7 angiotensin I + H2O cleavage only in vitro Mus musculus ?
-
?
3.4.11.7 angiotensin I + H2O cleavage only in vitro Homo sapiens ?
-
?
3.4.11.7 angiotensin I + H2O cleavage only in vitro Rattus norvegicus ?
-
?
3.4.11.7 angiotensin I + H2O cleavage only in vitro Sus scrofa ?
-
?
3.4.11.7 angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Mus musculus Asp + angiotensin III i.e. Arg-Val-Tyr-Ile-His-Pro-Phe ir
3.4.11.7 angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Homo sapiens Asp + angiotensin III i.e. Arg-Val-Tyr-Ile-His-Pro-Phe ir
3.4.11.7 angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Rattus norvegicus Asp + angiotensin III i.e. Arg-Val-Tyr-Ile-His-Pro-Phe ir
3.4.11.7 angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Sus scrofa Asp + angiotensin III i.e. Arg-Val-Tyr-Ile-His-Pro-Phe ir
3.4.11.7 angiotensin III + H2O the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension Mus musculus angiotensin IV + Arg
-
ir
3.4.11.7 angiotensin III + H2O the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension Homo sapiens angiotensin IV + Arg
-
ir
3.4.11.7 angiotensin III + H2O the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension Rattus norvegicus angiotensin IV + Arg
-
ir
3.4.11.7 angiotensin III + H2O the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension Sus scrofa angiotensin IV + Arg
-
ir
3.4.11.7 cholecystokinin-8 + H2O cleavage only in vitro Mus musculus ?
-
?
3.4.11.7 cholecystokinin-8 + H2O cleavage only in vitro Homo sapiens ?
-
?
3.4.11.7 cholecystokinin-8 + H2O cleavage only in vitro Rattus norvegicus ?
-
?
3.4.11.7 cholecystokinin-8 + H2O cleavage only in vitro Sus scrofa ?
-
?
3.4.11.7 additional information the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview Mus musculus ?
-
?
3.4.11.7 additional information the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview Homo sapiens ?
-
?
3.4.11.7 additional information the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview Rattus norvegicus ?
-
?
3.4.11.7 additional information the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview Sus scrofa ?
-
?
3.4.11.7 additional information substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides Mus musculus ?
-
?
3.4.11.7 additional information substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides Homo sapiens ?
-
?
3.4.11.7 additional information substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides Rattus norvegicus ?
-
?
3.4.11.7 additional information substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides Sus scrofa ?
-
?
3.4.11.7 N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O
-
Mus musculus ?
-
?
3.4.11.7 N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O
-
Homo sapiens ?
-
?
3.4.11.7 N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O
-
Rattus norvegicus ?
-
?
3.4.11.7 N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O
-
Sus scrofa ?
-
?
3.4.11.7 N-(alpha-L-aspartylyl)-2-naphthylamide + H2O
-
Mus musculus L-aspartic acid + 2-naphthylamine
-
?
3.4.11.7 N-(alpha-L-aspartylyl)-2-naphthylamide + H2O
-
Homo sapiens L-aspartic acid + 2-naphthylamine
-
?
3.4.11.7 N-(alpha-L-aspartylyl)-2-naphthylamide + H2O
-
Rattus norvegicus L-aspartic acid + 2-naphthylamine
-
?
3.4.11.7 N-(alpha-L-aspartylyl)-2-naphthylamide + H2O
-
Sus scrofa L-aspartic acid + 2-naphthylamine
-
?
3.4.11.7 N-(alpha-L-glutamyl)-2-naphthylamide + H2O
-
Mus musculus L-glutamic acid + 2-naphthylamine
-
?
3.4.11.7 N-(alpha-L-glutamyl)-2-naphthylamide + H2O
-
Homo sapiens L-glutamic acid + 2-naphthylamine
-
?
3.4.11.7 N-(alpha-L-glutamyl)-2-naphthylamide + H2O
-
Rattus norvegicus L-glutamic acid + 2-naphthylamine
-
?
3.4.11.7 N-(alpha-L-glutamyl)-2-naphthylamide + H2O
-
Sus scrofa L-glutamic acid + 2-naphthylamine
-
?

Subunits

EC Number Subunits Comment Organism
3.4.11.7 dimer 2 * 120000-185000, SDS-PAGE Mus musculus
3.4.11.7 dimer 2 * 120000-185000, SDS-PAGE Homo sapiens
3.4.11.7 dimer 2 * 120000-185000, SDS-PAGE Sus scrofa
3.4.11.7 dimer three-dimensional structure determination and analysis, modeling Rattus norvegicus
3.4.11.7 monomer three-dimensional structure determination and analysis, modeling Rattus norvegicus
3.4.11.7 More three-dimensional structure determination and analysis, modeling Homo sapiens
3.4.11.7 More three-dimensional structure determination and analysis, modeling Sus scrofa
3.4.11.7 More three-dimensional structure determination and analysis, modeling, the enzyme contains a short N-terminal cytoplasmic domain of 17 amino acid residues, a transmembrane domain of 22 amino acid residues, and a large extracellular domain of 906 amino acid residues in cluding the active and the zinc-binding site Mus musculus

Synonyms

EC Number Synonyms Comment Organism
3.4.11.7 aminopeptidase A
-
Mus musculus
3.4.11.7 aminopeptidase A
-
Homo sapiens
3.4.11.7 aminopeptidase A
-
Rattus norvegicus
3.4.11.7 aminopeptidase A
-
Sus scrofa
3.4.11.7 APA
-
Mus musculus
3.4.11.7 APA
-
Homo sapiens
3.4.11.7 APA
-
Rattus norvegicus
3.4.11.7 APA
-
Sus scrofa
3.4.11.7 BP1/6C3
-
Mus musculus
3.4.11.7 BP1/6C3
-
Homo sapiens
3.4.11.7 BP1/6C3
-
Rattus norvegicus
3.4.11.7 BP1/6C3
-
Sus scrofa
3.4.11.7 More the enzyme belongs to the zinc-metallopeptidase family of zincins Mus musculus
3.4.11.7 More the enzyme belongs to the zinc-metallopeptidase family of zincins Homo sapiens
3.4.11.7 More the enzyme belongs to the zinc-metallopeptidase family of zincins Rattus norvegicus
3.4.11.7 More the enzyme belongs to the zinc-metallopeptidase family of zincins Sus scrofa