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Literature summary for 2.3.2.5 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
Search for more literature for 2.3.2.5

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

General Stability

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Xanthomonas campestris Q8P8M4
-
-
Xanthomonas campestris ATCC 33913 Q8P8M4
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
glutaminyl cyclase
-
 Xanthomonas campestris

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Stability

pH Stability pH Stability Maximum Comment Organism
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]

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

kcat/KM [mM/s]

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