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

BRENDA support

Literature summary for 3.4.17.22 extracted from

  • Novikova, E.G.; Eng, F.J.; Yan, L.; Qian, Y.; Fricker, L.D.
    Characterization of the enzymatic properties of the first and second domains of metallocarboxypeptidase D (1999), J. Biol. Chem., 274, 28887-28892.
    View publication on PubMed
Search for more literature for 3.4.17.22

Cloned(Commentary)

Cloned (Comment) Organism
wild-type enzyme and point mutants are expressed at high levels in Sf9 cells using the baculovirus expression system Anas sp.

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
 Anas sp.
4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid
-
 Anas sp.
EDTA
-
 Anas sp.
EGTA
-
 Anas sp.
Zn2+ ZnCl2 Anas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km-values of domain 1 and 2 Anas sp.
0.0092
-
 Dansyl-Pro-Ala-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
0.016
-
 dansyl-Phe-Phe-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
0.023
-
 dansyl-Phe-Ala-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
0.0305
-
 Tyr-Gly-Gly-Phe-Leu-Lys wild-type enzyme, pH 6.4, 37°C Anas sp.
0.047
-
 dansyl-Phe-Gly-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
0.115
-
 Tyr-Gly-Gly-Phe-Leu-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates Anas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Anas sp. the enzyme plays a role in processing of many proteins that transit the secretory pathway ?
-
 ?

Organism

Organism UniProt Comment Textmining
Anas sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type enzyme and various point mutants expressed in a baculovirus expression system Anas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Dansyl-Phe-Ala-Arg + H2O
-
 Anas sp. Dansyl-Phe-Ala + Arg
-
 ?
Dansyl-Phe-Gly-Arg + H2O
-
 Anas sp. Dansyl-Phe-Gly + Arg
-
 ?
Dansyl-Phe-Phe-Arg + H2O
-
 Anas sp. Dansyl-Phe-Phe + Arg
-
 ?
Dansyl-Pro-Ala-Arg + H2O
-
 Anas sp. Dansyl-Pro-Ala + Arg
-
 ?
additional information the enzyme removes only the C-terminal Lys or Arg from peptides, with the first domain more efficient towards Arg and the second domain more efficient towards Lys. Peptides containing Pro in the penultimate position are poorly cleaved. Cleavage of a peptide with Ala in the penultimate position is most efficient, with the order of decreasing efficiency Ala, Met, Ser, Phe, tyr, Trp, Thr, Gln, Asp, Leu, Gly, Pro. There are only minor differences between the first and the second domains regarding the influence of the penultimate amino acid Anas sp. ?
-
 ?
additional information the enzyme plays a role in processing of many proteins that transit the secretory pathway Anas sp. ?
-
 ?
Tyr-Gly-Gly-Phe-Leu-Arg + H2O
-
 Anas sp. Tyr-Gly-Gly-Phe-Leu + Arg
-
 ?
Tyr-Gly-Gly-Phe-Leu-Lys + H2O
-
 Anas sp. Tyr-Gly-Gly-Phe-Leu + Lys
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information turnover numbers of domain 1 and 2 Anas sp.
2.6
-
 dansyl-Phe-Gly-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
3.07
-
 Tyr-Gly-Gly-Phe-Leu-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
3.7
-
 dansyl-Phe-Phe-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
3.97
-
 Tyr-Gly-Gly-Phe-Leu-Lys wild-type enzyme, pH 6.4, 37°C Anas sp.
6.7
-
 Dansyl-Pro-Ala-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
19
-
 dansyl-Phe-Ala-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.