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Literature summary for 3.4.17.3 extracted from

  • Plummer, T.H.; Erdös, E.G.
    Human plasma carboxypeptidase N (1981), Methods Enzymol., 80, 442-449.
    View publication on PubMed
Search for more literature for 3.4.17.3

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
 Homo sapiens
5-amino-n-pentanoic acid
-
 Homo sapiens
6-aminohexanoic acid
-
 Homo sapiens
EDTA
-
 Homo sapiens
Peptide fragments of bradykinin
-
 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0004
-
 bradykinin
-
 Homo sapiens
0.1
-
 benzoyl-Gly-Arg
-
 Homo sapiens
0.3
-
 furylacryloylalanyl-L-Lys
-
 Homo sapiens
1.4
-
 Benzoyl-Gly-Lys
-
 Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates Homo sapiens
Zinc zinc metalloenzyme Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
270000 280000
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification presence of significant amounts of glucosamine, mannose, galactose, fucose, sialic acid Homo sapiens
side-chain modification the carbohydrate is primarily attached to the larger subunit, representing 28% of its weight. Two forms detected in isoelectric focusing with pI of 3.8 and 4.3. The difference is attributed to differences in sialic acid content of the two forms Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
plasma
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
furylacryloyl-Ala-L-Lys + H2O
-
 Homo sapiens furylacryloylalanine-Ala + Lys
-
 ?

Subunits

Subunits Comment Organism
tetramer 2 * 49000-55000 + 2 * 83000-98000. Homo sapiens