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Literature summary for 2.3.2.5 extracted from

  • Schilling, S.; Hoffmann, T.; Rosche, F.; Manhart, S.; Wasternack, C.; Demuth, H.U.
    Heterologous expression and characterization of human glutaminyl cyclase: evidence for a disulfide bond with importance for catalytic activity (2002), Biochemistry, 41, 10849-10857.
    View publication on PubMed
Search for more literature for 2.3.2.5

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris. In Escherichia coli only 50% of the protein does not contain a disulfide bond that is present in the enzyme expressed in Pichia pastoris Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.051
-
 L-glutaminyl-4-methylcoumarinylamide 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
0.06
-
 L-glutaminyl-2-naphthylamide 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
0.09
-
 Gln-His-Pro-NH2 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
0.101
-
 Gln-Tyr-Ala-OH 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
0.148
-
 Gln-Gln-OH 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
0.153
-
 Gln-Tyr-Ala-OH 37°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
0.409
-
 Gln-NH2 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38795
-
 x * 38795, deglycosylated enzyme, MALDI-TOF mass analysis Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutaminyl-peptide Homo sapiens the N-terminal formation of 5-oxoproline is a common post-translational event during biosynthesis of a number of peptides 5-oxoprolyl-peptide + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein deglycosylation has no effect on enzymatic activity Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
of 6His-tagged enzyme expressed in Pichia pastoris and enzyme expressed in Escherichia coli Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
18.7
-
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gln-Gln
-
 Homo sapiens L-5-oxoprolyl-Gln + NH3
-
 ?
Gln-Gln
-
 Homo sapiens Glp-Gln + NH3
-
 ?
Gln-His-Pro-NH2
-
 Homo sapiens L-5-oxoprolyl-His-Pro-NH2 + NH3
-
 ?
Gln-NH2
-
 Homo sapiens Glp-amide + NH3
-
 ?
Gln-Tyr-Ala-OH
-
 Homo sapiens L-5-oxoprolyl-Tyr-Ala + NH3
-
 ?
L-glutaminyl-2-naphthylamide
-
 Homo sapiens L-5-oxoprolyl-2-naphthylamide + NH3
-
 ?
L-glutaminyl-4-methylcoumarinylamide
-
 Homo sapiens L-5-oxoprolyl-4-methylcoumarinylamide + NH3
-
 ?
L-glutaminyl-peptide the N-terminal formation of 5-oxoproline is a common post-translational event during biosynthesis of a number of peptides Homo sapiens 5-oxoprolyl-peptide + NH3
-
 ?

Subunits

Subunits Comment Organism
? x * 38795, deglycosylated enzyme, MALDI-TOF mass analysis Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.4
-
 L-glutaminyl-4-methylcoumarinylamide 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
12.8
-
 Gln-Gln-OH 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
18.8
-
 L-glutaminyl-2-naphthylamide 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
20.7
-
 Gln-NH2 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
83
-
 Gln-His-Pro-NH2 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
125
-
 Gln-Tyr-Ala-OH 30°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens
220
-
 Gln-Tyr-Ala-OH 37°C, recombinant enzyme, expressed in Pichia pastoris Homo sapiens