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Literature summary for 3.4.24.79 extracted from

  • Glerup, S.; Kloeverpris, S.; Laursen, L.S.; Dagnaes-Hansen, F.; Thiel, S.; Conover, C.A.; Oxvig, C.
    Cell surface detachment of pregnancy-associated plasma protein-A requires the formation of intermolecular proteinase-inhibitor disulfide bonds and glycosaminoglycan covalently bound to the inhibitor (2007), J. Biol. Chem., 282, 1769-1778.
    View publication on PubMed
Search for more literature for 3.4.24.79

Cloned(Commentary)

Cloned (Comment) Organism
expression of PAPP-A wild-type and mutant E483A in HEK-293T cells, co-expression with inhibitor proMBP Homo sapiens

Protein Variants

Protein Variants Comment Organism
E483A a proteolytically inactive PAPP-A mutant Homo sapiens

General Stability

General Stability Organism
half-life of circulating PAPP-A and proMBP in complex is severalfold higher than both of the uncomplexed proteins Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
proform of eosinophil major basic protein i.e. proMBP, the glycosaminoglycan of proMBP is not required for PAPP-A-proMBP complex formation, while proMBP residues His137, Ser178, Arg179, and Asn181 are important for the recognition of PAPP-A, complex formation increases the half-life of enzyme and inhibitor, the PAPP-A-proMBP complex is formed at the cell surface in vivo rather than in the circulation, the redox potential of the tissue microenvironment controls the process, chondroitin or dermatan sulfate do not have any effect on complex formation Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information PAPP-A-proMBP complex formation kinetics, overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface detachment of pregnancy-associated plasma protein-A requires the formation of intermolecular proteinase-inhibitor disulfide bonds and glycosaminoglycan covalently bound to the inhibitor, mechanism, overview, the PAPP-A-proMBP complex is unable to bind to the cell surface Homo sapiens 9986
-
extracellular
-
 Homo sapiens
-
-
additional information the PAPP-A-proMBP complex is formed at the cell surface in vivo rather than in the circulation, the redox potential of the tissue microenvironment controls the process, chondroitin or dermatan sulfate do not have any effect on complex formation Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the enzyme is a metzincin metalloproteinase Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
IGF-binding protein-4 + H2O Homo sapiens PAPP-A promotes cell growth causing the release of bound insulin-like growth factors ?
-
 ?
IGF-binding protein-5 + H2O Homo sapiens PAPP-A promotes cell growth causing the release of bound insulin-like growth factors ?
-
 ?
additional information Homo sapiens in human pregnancy, the majority of PAPP-A circulates as a disulfide-bonded complex with its inhibitor, the proform of eosinophil major basic protein, i.e. proMBP ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant PAPP-A wild-type and mutant E483A from HEK-293T cells by immunoaffinity chromatography Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
additional information in human pregnancy, the majority of PAPP-A circulates as a disulfide-bonded complex with its inhibitor, the proform of eosinophil major basic protein, i.e. proMBP, the PAPP-A-proMBP complex is unable to bind to the cell surface Homo sapiens
-
placenta cell surface Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
IGF-binding protein-4 + H2O i.e. IGFBP-4 Homo sapiens ?
-
 ?
IGF-binding protein-4 + H2O PAPP-A promotes cell growth causing the release of bound insulin-like growth factors Homo sapiens ?
-
 ?
IGF-binding protein-5 + H2O i.e. IGFBP-5 Homo sapiens ?
-
 ?
IGF-binding protein-5 + H2O PAPP-A promotes cell growth causing the release of bound insulin-like growth factors Homo sapiens ?
-
 ?
additional information in human pregnancy, the majority of PAPP-A circulates as a disulfide-bonded complex with its inhibitor, the proform of eosinophil major basic protein, i.e. proMBP Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
PAPP-A
-
 Homo sapiens
pregnancy-associated plasma protein-A
-
 Homo sapiens