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Literature summary for 3.4.15.1 extracted from

  • Woodman, Z.L.; Schwager, S.L.; Redelinghuys, P.; Chubb, A.J.; van der Merwe, E.L.; Ehlers, M.R.; Sturrock, E.D.
    Homologous substitution of ACE C-domain regions with N-domain sequences: effect on processing, shedding, and catalytic properties (2006), Biol. Chem., 387, 1043-1051.
    View publication on PubMed
Search for more literature for 3.4.15.1

Cloned(Commentary)

Cloned (Comment) Organism
regions of the testis ACE sequence are replaced with the corresponding N-domain sequence. The resultant chimeras C1-163Ndom-ACE, C417-579Ndom-ACE, and C583-623Ndom-ACE are processed to the cell surface of transfected Chinese hamster ovary cells, and are cleaved at the identical site as that of tACE Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information regions of the testis ACE sequence are replaced with the corresponding N-domain sequence. The resultant chimeras C1-163Ndom-ACE, C417-579Ndom-ACE, and C583-623Ndom-ACE are processed to the cell surface of transfected Chinese hamster ovary cells, and are cleaved at the identical site as that of tACE. They show acquisition of N-domain-like catalytic properties. Homology modelling of the chimeric proteins reveals structural changes in regions required for tACE-specific catalytic activity. In contrast, C164-416Ndom-ACE and C191-214Ndom-ACE demonstrate defective intracellular processing and are neither enzymatically active nor shed. Therefore, critical elements within region D164–V416 and more specifically I191–T214 are required for the processing, cell-surface targeting, and enzyme activity of tACE, and cannot be substituted for by the homologous N-domain sequence Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.3
-
 benzyloxycarbonyl-Phe-His-Leu 37°C, pH 8.3, chimeric enzyme C583-623Ndom-ACE Homo sapiens
0.3
-
 benzyloxycarbonyl-Phe-His-Leu 37°C, pH 8.3, N-domain of tACE Homo sapiens
0.4
-
 benzyloxycarbonyl-Phe-His-Leu 37°C, pH 8.3, chimeric enzyme C1-163Ndom-ACE Homo sapiens
0.5
-
 hippuryl-His-Leu 37°C, pH 8.3, N-domain of tACE Homo sapiens
1.1
-
 hippuryl-His-Leu 37°C, pH 8.3, chimeric enzyme C1-163Ndom-ACE Homo sapiens
1.1
-
 hippuryl-His-Leu 37°C, pH 8.3, chimeric enzyme C583–623Ndom-ACE Homo sapiens
1.1
-
 hippuryl-His-Leu 37°C, pH 8.3, tACE Homo sapiens
1.2
-
 benzyloxycarbonyl-Phe-His-Leu 37°C, pH 8.3, ACE Homo sapiens
2.7
-
 hippuryl-His-Leu 37°C, pH 8.3, chimeric enzyme C417-579Ndom-ACE Homo sapiens
2.8
-
 benzyloxycarbonyl-Phe-His-Leu 37°C, pH 8.3, chimeric enzyme C417–579Ndom-ACE Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface both isoforms are shed from the cell surface via a sheddase-mediated cleavage, testis ACE is shed much more efficiently than somatic ACE Homo sapiens 9986
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P12821 testis-specific isoform precursor
-

Source Tissue

Source Tissue Comment Organism Textmining
testis
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-Phe-His-Leu + H2O
-
 Homo sapiens ?
-
 ?
hippuryl-His-Leu + H2O
-
 Homo sapiens hippuric acid + His-Leu
-
 ?

Synonyms

Synonyms Comment Organism
TACE
-
 Homo sapiens
testis ACE
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1
-
 benzyloxycarbonyl-Phe-His-Leu 37°C, pH 8.3, ACE Homo sapiens
11.8
-
 hippuryl-His-Leu 37°C, pH 8.3, chimeric enzyme C417-579Ndom-ACE Homo sapiens
12.9
-
 hippuryl-His-Leu 37°C, pH 8.3, chimeric enzyme C583-623Ndom-ACE Homo sapiens
15.1
-
 hippuryl-His-Leu 37°C, pH 8.3, chimeric enzyme C1–163Ndom-ACE Homo sapiens
24.5
-
 hippuryl-His-Leu 37°C, pH 8.3, tACE Homo sapiens
34.4
-
 benzyloxycarbonyl-Phe-His-Leu 37°C, pH 8.3, chimeric enzyme C417-579Ndom-ACE Homo sapiens
36.8
-
 benzyloxycarbonyl-Phe-His-Leu 37°C, pH 8.3, chimeric enzyme C583-623Ndom-ACE Homo sapiens
73.2
-
 benzyloxycarbonyl-Phe-His-Leu 37°C, pH 8.3, ACE Homo sapiens
97.5
-
 benzyloxycarbonyl-Phe-His-Leu 37°C, pH 8.3, chimeric enzyme C1-163Ndom-ACE Homo sapiens
128
-
 benzyloxycarbonyl-Phe-His-Leu 37°C, pH 8.3, N-domain of tACE Homo sapiens
262.5
-
 hippuryl-His-Leu 37°C, pH 8.3, N-domain of tACE Homo sapiens