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Literature summary extracted from

  • Huang, W.L.; Wang, Y.R.; Ko, T.P.; Chia, C.Y.; Huang, K.F.; Wang, A.H.
    Crystal structure and functional analysis of the glutaminyl cyclase from Xanthomonas campestris (2010), J. Mol. Biol., 401, 374-388.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.5 expressed in Escherichia coli BL21(DE3) cells Xanthomonas campestris

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.2.5 mutant enzyme E89A, hanging drop vapor diffusion method, using 50 mM imidazole and 0.8 M sodium citrate, pH 8.7, at 25°C Xanthomonas campestris

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.5 E45A the mutation leads to a drop in the enzyme activity (1.12% activity compared to the wild type enzyme) Xanthomonas campestris
2.3.2.5 E45Q the mutation increases the enzyme activity by an order of magnitude (1079.68% activity compared to the wild type enzyme) Xanthomonas campestris
2.3.2.5 E89A the mutant exhibits 5.46% activity compared to the wild type enzyme Xanthomonas campestris
2.3.2.5 F43A the mutant exhibits 5.46% activity compared to the wild type enzyme Xanthomonas campestris
2.3.2.5 F87A the mutant exhibits 3.87% activity compared to the wild type enzyme Xanthomonas campestris
2.3.2.5 W103A the mutant exhibits 3.05% activity compared to the wild type enzyme Xanthomonas campestris

General Stability

EC Number General Stability Organism
2.3.2.5 after a 24-h incubation in 1 M guanidine hydrochloride the recombinant enzyme becomes aggregated Xanthomonas campestris

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.5 L-Gln-2-naphthylamide substrate inhibition Xanthomonas campestris

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.5 0.039
-
 L-Gln-2-naphthylamide mutant enzyme E45Q, at pH 7.0 at 25°C Xanthomonas campestris
2.3.2.5 0.121
-
 L-Gln-2-naphthylamide wild type enzyme, at pH 7.0 at 25°C Xanthomonas campestris

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.2.5 Ca2+ contains a calcium ion Xanthomonas campestris

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.5 Xanthomonas campestris Q8P8M4
-
-
2.3.2.5 Xanthomonas campestris ATCC 33913 Q8P8M4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.5 Ni-NTA column chromatography Xanthomonas campestris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.5 L-Gln-2-naphthylamide
-
 Xanthomonas campestris 5-oxoprolyl-2-naphthylamide + NH3
-
 ?
2.3.2.5 L-Gln-2-naphthylamide
-
 Xanthomonas campestris ATCC 33913 5-oxoprolyl-2-naphthylamide + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.5 glutaminyl cyclase
-
 Xanthomonas campestris

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.2.5 20 75 the enzyme is only stable below 40°C and exhibits remarkable instability above 50°C Xanthomonas campestris

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.2.5 1.4
-
 L-Gln-2-naphthylamide wild type enzyme, at pH 7.0 at 25°C Xanthomonas campestris
2.3.2.5 5.8
-
 L-Gln-2-naphthylamide mutant enzyme E45Q, at pH 7.0 at 25°C Xanthomonas campestris

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.3.2.5 3.5 9 the enzyme possesses relatively high activities between pH 5.0 and 7.5, but exhibits significantly decreased activities above pH 8.0 and below pH 5.0 Xanthomonas campestris

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.2.5 1.54
-
 L-Gln-2-naphthylamide wild type enzyme, at pH 7.0 at 25°C Xanthomonas campestris
2.3.2.5 5.06
-
 L-Gln-2-naphthylamide mutant enzyme E45Q, at pH 7.0 at 25°C Xanthomonas campestris

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.2.5 12.6
-
 L-Gln-2-naphthylamide wild type enzyme, at pH 7.0 at 25°C Xanthomonas campestris
2.3.2.5 166.1
-
 L-Gln-2-naphthylamide mutant enzyme E45Q, at pH 7.0 at 25°C Xanthomonas campestris