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Literature summary extracted from

  • Beebe, K.D.; Shin, J.N.; Peng, J.; Chaudhury, C.; Khera, J.; Pei, D.H.
    Substrate recognition through a PDZ domain in tail-specific protease (2000), Biochemistry, 39, 3149-3155.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.102 additional information deletion of N-terminal amino acids 206-660, and deletion of C-terminal amino acids 1-334, both peptides are efficiently labelled by a competitive inhibitor of the enzyme marked with photoaffinity lable Escherichia coli
3.4.21.102 V229E increased Km for 2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala Escherichia coli
3.4.21.102 V229Q increased Km for 2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.102 0.0044
-
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala wild-type enzyme Escherichia coli
3.4.21.102 0.0095
-
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala mutant V229Q Escherichia coli
3.4.21.102 0.0111
-
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala mutant V229E Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.102 75000
-
x * 75000-80000, SDS-PAGE, x * 75000, mass spectrometry Escherichia coli
3.4.21.102 75000 80000 the enzyme possesses an N-terminal domain, a PDZ domain and a C-terminal catalytic domain Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.102 Protein + H2O Escherichia coli
-
?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.102 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.102 wild-type and mutant enzyme Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.21.102 the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II substrate recognition site is located between amino acids 206 and 334 where there is also a putative PDZ domain Escherichia coli

Storage Stability

EC Number Storage Stability Organism
3.4.21.102 -80°C, 20 mM Tris-HCl, pH 7.9, 1 M imidazole, 0.5 M NaCl, 33% glycerol Escherichia coli
3.4.21.102 4°C, prolonged storage, proteolytic cleavage into two fragments of 50000 and 25000 Da Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.102 2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala + H2O
-
Escherichia coli 2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala + Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
-
?
3.4.21.102 Protein + H2O
-
Escherichia coli ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.21.102 ? x * 75000-80000, SDS-PAGE, x * 75000, mass spectrometry Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.102 0.05
-
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala wild-type enzyme, mutants V229Q, V229E Escherichia coli