Literature summary for 3.4.16.6 extracted from

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

Cloned(Commentary)

Cloned (Comment)	Organism
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

Cloned (Comment)

Organism

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

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

Inhibitors

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	-	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
Dansyl-Phe-Ala-Arg + H2O	-	Drosophila melanogaster	Dansyl-Phe-Ala + Arg	-	?
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	?	-	?
additional information	the enzyme functions in processing of proteins that transit the secretory pathway	Drosophila melanogaster	?	-	?

Turnover Number [1/s]

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

pH Optimum

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