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Literature summary 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

Cloned(Commentary)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.17.22 2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
 Anas sp.
3.4.17.22 4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid
-
 Anas sp.
3.4.17.22 EDTA
-
 Anas sp.
3.4.17.22 EGTA
-
 Anas sp.
3.4.17.22 Zn2+ ZnCl2 Anas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.17.22 additional information
-
 additional information Km-values of domain 1 and 2 Anas sp.
3.4.17.22 0.0092
-
 Dansyl-Pro-Ala-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
3.4.17.22 0.016
-
 dansyl-Phe-Phe-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
3.4.17.22 0.023
-
 dansyl-Phe-Ala-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
3.4.17.22 0.0305
-
 Tyr-Gly-Gly-Phe-Leu-Lys wild-type enzyme, pH 6.4, 37°C Anas sp.
3.4.17.22 0.047
-
 dansyl-Phe-Gly-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
3.4.17.22 0.115
-
 Tyr-Gly-Gly-Phe-Leu-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.4.17.22 Anas sp.
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.17.22 Dansyl-Phe-Ala-Arg + H2O
-
 Anas sp. Dansyl-Phe-Ala + Arg
-
 ?
3.4.17.22 Dansyl-Phe-Gly-Arg + H2O
-
 Anas sp. Dansyl-Phe-Gly + Arg
-
 ?
3.4.17.22 Dansyl-Phe-Phe-Arg + H2O
-
 Anas sp. Dansyl-Phe-Phe + Arg
-
 ?
3.4.17.22 Dansyl-Pro-Ala-Arg + H2O
-
 Anas sp. Dansyl-Pro-Ala + Arg
-
 ?
3.4.17.22 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. ?
-
 ?
3.4.17.22 additional information the enzyme plays a role in processing of many proteins that transit the secretory pathway Anas sp. ?
-
 ?
3.4.17.22 Tyr-Gly-Gly-Phe-Leu-Arg + H2O
-
 Anas sp. Tyr-Gly-Gly-Phe-Leu + Arg
-
 ?
3.4.17.22 Tyr-Gly-Gly-Phe-Leu-Lys + H2O
-
 Anas sp. Tyr-Gly-Gly-Phe-Leu + Lys
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.17.22 additional information
-
 additional information turnover numbers of domain 1 and 2 Anas sp.
3.4.17.22 2.6
-
 dansyl-Phe-Gly-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
3.4.17.22 3.07
-
 Tyr-Gly-Gly-Phe-Leu-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
3.4.17.22 3.7
-
 dansyl-Phe-Phe-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
3.4.17.22 3.97
-
 Tyr-Gly-Gly-Phe-Leu-Lys wild-type enzyme, pH 6.4, 37°C Anas sp.
3.4.17.22 6.7
-
 Dansyl-Pro-Ala-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.
3.4.17.22 19
-
 dansyl-Phe-Ala-Arg wild-type enzyme, pH 6.4, 37°C Anas sp.