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

BRENDA support

Literature summary extracted from

  • Sidyelyeva, G.; Fricker, L.D.
    Characterization of Drosophila carboxypeptidase D (2002), J. Biol. Chem., 277, 49613-49620.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.16.6 individual domains of the enzyme are expressed in insect Sf9 cells using the baculovirus expression system. Medium from domain 1B-expressing cells and domain 2-expressing cells shows substantial enzymatic activity, whereas medium from domain 1A-expressing cells is not different from cells infected with wild-type virus. The individual domains 1A, 1B, and 2 are expressed in baculovirus under the polyhedrin promoter and with the signal peptide of the rat enzyme Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
3.4.16.6 E353Q cells infected with the mutant enzyme show considerable carboxypeptidase activity, mutation eliminates the activity of domain 1 Drosophila melanogaster
3.4.16.6 E771Q cells infected with the mutant enzyme show considerable carboxypeptidase activity, mutation eliminates the activity of domain 2 Drosophila melanogaster

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.16.6 4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid
-
 Drosophila melanogaster
3.4.16.6 EDTA
-
 Drosophila melanogaster
3.4.16.6 Guanidinoethylmercaptosuccinic acid domain 1B and domain Drosophila melanogaster
3.4.16.6 PCMB domain 1B and domain Drosophila melanogaster

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.16.6 0.208
-
 dansyl-Phe-Ala-Arg pH 7.4, 37°C, domain 1B Drosophila melanogaster
3.4.16.6 0.246
-
 dansyl-Phe-Ala-Arg pH 5.7, 37°C, domain 2 Drosophila melanogaster

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.16.6 additional information Drosophila melanogaster the enzyme functions in processing of proteins that transit the secretory pathway ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.6 Drosophila melanogaster
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.16.6 domain 1B and 2 expressed in Sf9 cells using baculovirus expression system Drosophila melanogaster

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.16.6 Dansyl-Phe-Ala-Arg + H2O
-
 Drosophila melanogaster Dansyl-Phe-Ala + Arg
-
 ?
3.4.16.6 additional information activity of individual domains of the enzyme. Domain 1B is more active at neutral pH and greatly prefers C-terminal Arg over Lys, whereas domain 2 is more active at pH 5-6 and slightly prefers C-terminal Lys over Arg Drosophila melanogaster ?
-
 ?
3.4.16.6 additional information the enzyme functions in processing of proteins that transit the secretory pathway Drosophila melanogaster ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.16.6 3.86
-
 dansyl-Phe-Ala-Arg pH 5.7, 37°C, domain 2 Drosophila melanogaster
3.4.16.6 32.6
-
 dansyl-Phe-Ala-Arg pH 7.4, 37°C, domain 1B Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.16.6 5 7 wild-type enzyme Drosophila melanogaster
3.4.16.6 5.6
-
 domain 1B Drosophila melanogaster
3.4.16.6 7.4
-
 domain 2 Drosophila melanogaster