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Literature summary for 4.6.1.1 extracted from

  • Gallagher, D.T.; Kim, S.K.; Robinson, H.; Reddy, P.T.
    Active-site structure of class IV adenylyl cyclase and transphyletic mechanism (2011), J. Mol. Biol., 405, 787-803.
    View publication on PubMed
Search for more literature for 4.6.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Yersinia pestis

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzyme D55K Yersinia pestis

Protein Variants

Protein Variants Comment Organism
C83A the mutation results in moderate to sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+ Yersinia pestis
D55K the mutant shows increased Km for Mg2+ compared to the wild type enzyme Yersinia pestis
E10A the mutation results in about 8fold reduction in activity with 20 mM Mg2+ and in a 5fold increase in activity in the presence of 10 mM Mn2+ Yersinia pestis
E10Q the mutation results in about 8fold reduction in activity with 20 mM Mg2+ and in a 5fold increase in activity in the presence of 10 mM Mn2+ Yersinia pestis
E12Q the mutation results in sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+ Yersinia pestis
E136A the mutation results in sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+ Yersinia pestis
F5A the mutant shows increased Km for Mg2+ compared to the wild type enzyme Yersinia pestis
K14A the mutation results in sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+ Yersinia pestis
K76A the mutation results in sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+ Yersinia pestis
L72A the mutant shows about 2fold increased Km for Mg2+ compared to the wild type enzyme Yersinia pestis
M140A the mutation results in moderate to sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+ Yersinia pestis
R113A the mutation results in sharp decreases in activity in the presence of 10 mM Mn2+ and no activity with Mg2+ Yersinia pestis
R63A the mutation results in sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+ Yersinia pestis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.005
-
 ATP mutant enzyme C83A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.011
-
 ATP mutant enzyme R63A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.014
-
 ATP mutant enzyme D55K, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.015
-
 ATP mutant enzyme E12Q, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.02
-
 ATP wild type enzyme, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.03
-
 ATP mutant enzyme F5A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.035
-
 ATP mutant enzyme L72A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.035
-
 ATP mutant enzyme M140A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.046
-
 ATP mutant enzyme K76A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.05
-
 ATP mutant enzyme R113A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.06
-
 ATP mutant enzyme E136A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.09
-
 ATP mutant enzyme K14A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.1
-
 ATP mutant enzyme E10Q, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C Yersinia pestis
0.16
-
 ATP mutant enzyme E136A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis
0.21
-
 ATP mutant enzyme K14A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis
0.21
-
 ATP wild type enzyme, at pH 7.0, in Tris buffer at 37°C Yersinia pestis
0.24
-
 ATP mutant enzyme E10Q, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis
0.34
-
 ATP wild type enzyme, at pH 8.0, in Tris buffer at 37°C Yersinia pestis
0.37
-
 ATP wild type enzyme, at pH 7.5, in Tris buffer at 37°C Yersinia pestis
0.4
-
 ATP mutant enzyme K76A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis
0.43
-
 ATP wild type enzyme, at pH 8.5, in Tris buffer at 37°C Yersinia pestis
0.44
-
 ATP wild type enzyme, at pH 9.0, in Tris buffer at 37°C Yersinia pestis
0.62
-
 ATP mutant enzyme C83A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis
0.69
-
 ATP wild type enzyme, at pH 9.5, in Tris buffer at 37°C Yersinia pestis
0.7
-
 ATP wild type enzyme, at pH 10.0, in Tris buffer at 37°C Yersinia pestis
0.71
-
 ATP wild type enzyme, at pH 10.4, in Tris buffer at 37°C Yersinia pestis
0.75
-
 ATP mutant enzyme R63A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis
0.78
-
 ATP wild type enzyme, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis
0.87
-
 ATP mutant enzyme D55K, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis
1.15
-
 ATP mutant enzyme E12Q, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis
1.19
-
 ATP mutant enzyme M140A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis
1.38
-
 GTP wild type enzyme, pH 8.5, 37°C Yersinia pestis
1.89
-
 ATP mutant enzyme F5A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis
2.29
-
 ATP mutant enzyme L72A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C Yersinia pestis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the wild type enzyme activity is stimulated by Mg2+ Yersinia pestis
Mn2+ the wild type enzyme is about 2.5fold more active with saturating Mg2+ than with saturating Mn2+ Yersinia pestis

Organism

Organism UniProt Comment Textmining
Yersinia pestis Q7CH76
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE cellulose column chromatography, gel filtration Yersinia pestis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP
-
 Yersinia pestis 3',5'-cyclic-AMP + diphosphate
-
 ?
GTP class IV adenylyl cyclase also functions as guanylyl cyclase with about 20% efficiency Yersinia pestis 3',5'-cyclic-GMP + diphosphate
-
 ?
additional information class IV adenylyl cyclase also functions as guanylyl cyclase Yersinia pestis ?
-
 ?

Subunits

Subunits Comment Organism
dimer x-ray crystallography Yersinia pestis

Synonyms

Synonyms Comment Organism
AC-IV
-
 Yersinia pestis
class IV adenylyl cyclase
-
 Yersinia pestis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0057
-
 ATP wild type enzyme, at pH 7.0, in Tris buffer at 37°C Yersinia pestis
0.0349
-
 ATP wild type enzyme, at pH 7.5, in Tris buffer at 37°C Yersinia pestis
0.1002
-
 ATP wild type enzyme, at pH 8.0, in Tris buffer at 37°C Yersinia pestis
0.2519
-
 ATP wild type enzyme, at pH 8.5, in Tris buffer at 37°C Yersinia pestis
0.4943
-
 ATP wild type enzyme, at pH 9.0, in Tris buffer at 37°C Yersinia pestis
0.7449
-
 ATP wild type enzyme, at pH 9.5, in Tris buffer at 37°C Yersinia pestis
0.8368
-
 ATP wild type enzyme, at pH 10.0, in Tris buffer at 37°C Yersinia pestis
0.889
-
 ATP wild type enzyme, at pH 10.4, in Tris buffer at 37°C Yersinia pestis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00027
-
 ATP wild type enzyme, at pH 7.0, in Tris buffer at 37°C Yersinia pestis
0.00094
-
 ATP wild type enzyme, at pH 7.5, in Tris buffer at 37°C Yersinia pestis
0.00294
-
 ATP wild type enzyme, at pH 8.0, in Tris buffer at 37°C Yersinia pestis
0.01079
-
 ATP wild type enzyme, at pH 9.5, in Tris buffer at 37°C Yersinia pestis
0.01124
-
 ATP wild type enzyme, at pH 9.0, in Tris buffer at 37°C Yersinia pestis
0.01195
-
 ATP wild type enzyme, at pH 10.0, in Tris buffer at 37°C Yersinia pestis
0.01252
-
 ATP wild type enzyme, at pH 10.4, in Tris buffer at 37°C Yersinia pestis
586
-
 ATP wild type enzyme, at pH 8.5, in Tris buffer at 37°C Yersinia pestis