BRENDA - Enzyme Database
show all sequences of 3.4.17.23

The sweeter side of ACE2: physiological evidence for a role in diabetes

Bindom, S.M.; Lazartigues, E.; Mol. Cell. Endocrinol. 302, 193-202 (2009)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
ACE2 exists as bothmembrane bound and soluble forms, the latter being generated by proteolytic cleavage of the ectodomain by the tumor necrosis factor convertase ADAM17
Homo sapiens
5737
-
membrane
ACE2 exists as bothmembrane bound and soluble forms, the latter being generated by proteolytic cleavage of the ectodomain by the tumor necrosis factor convertase ADAM17
Homo sapiens
16020
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
zinc metalloprotease
Homo sapiens
Zn2+
zinc metalloprotease
Rattus norvegicus
Organism
Organism
UniProt
Commentary
Textmining
Homo sapiens
Q9BYF1
-
-
Rattus norvegicus
Q5EGZ1
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
adipose tissue
-
Rattus norvegicus
-
brain
-
Rattus norvegicus
-
colon
-
Homo sapiens
-
heart
-
Homo sapiens
-
kidney
localization of ACE2 in the podocytes early in the development of diabetes indicates that it may protect against podocyte loss, thus preventing the worsening glomerular injury
Homo sapiens
-
liver
-
Rattus norvegicus
-
lung
-
Rattus norvegicus
-
ovary
-
Homo sapiens
-
pancreas
ACE-mediated inhibition of TGF-beta expression may prevent islet fibrosis and loss of islet function
Rattus norvegicus
-
placenta
-
Homo sapiens
-
retina
-
Homo sapiens
-
retina
-
Rattus norvegicus
-
small intestine
-
Homo sapiens
-
testis
-
Homo sapiens
-
Synonyms
Synonyms
Commentary
Organism
ACE2
-
Rattus norvegicus
ACE2
-
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
ACE2 exists as bothmembrane bound and soluble forms, the latter being generated by proteolytic cleavage of the ectodomain by the tumor necrosis factor convertase ADAM17
Homo sapiens
5737
-
membrane
ACE2 exists as bothmembrane bound and soluble forms, the latter being generated by proteolytic cleavage of the ectodomain by the tumor necrosis factor convertase ADAM17
Homo sapiens
16020
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
zinc metalloprotease
Homo sapiens
Zn2+
zinc metalloprotease
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
adipose tissue
-
Rattus norvegicus
-
brain
-
Rattus norvegicus
-
colon
-
Homo sapiens
-
heart
-
Homo sapiens
-
kidney
localization of ACE2 in the podocytes early in the development of diabetes indicates that it may protect against podocyte loss, thus preventing the worsening glomerular injury
Homo sapiens
-
liver
-
Rattus norvegicus
-
lung
-
Rattus norvegicus
-
ovary
-
Homo sapiens
-
pancreas
ACE-mediated inhibition of TGF-beta expression may prevent islet fibrosis and loss of islet function
Rattus norvegicus
-
placenta
-
Homo sapiens
-
retina
-
Homo sapiens
-
retina
-
Rattus norvegicus
-
small intestine
-
Homo sapiens
-
testis
-
Homo sapiens
-
Other publictions for EC 3.4.17.23
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)