Information on EC 4.6.1.1 - adenylate cyclase and Organism(s) Escherichia coli and UniProt Accession P00936

for references in articles please use BRENDA:EC4.6.1.1
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This record set is specific for:
Escherichia coli
UNIPROT: P00936


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria


The taxonomic range for the selected organisms is: Escherichia coli

EC NUMBER
COMMENTARY hide
4.6.1.1
-
RECOMMENDED NAME
GeneOntology No.
adenylate cyclase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P-O bond cleavage
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
purine metabolism
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-
Purine metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
ATP diphosphate-lyase (cyclizing; 3',5'-cyclic-AMP-forming)
Also acts on dATP to form 3',5'-cyclic dAMP. Requires pyruvate. Activated by NAD+ in the presence of EC 2.4.2.31 NAD(P)+---arginine ADP-ribosyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-42-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
class I AC gene
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP
3',5'-cyclic-AMP + diphosphate
show the reaction diagram
ATP
3',5'-cAMP + diphosphate
show the reaction diagram
additional information
?
-
structure-function relationship, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP
3',5'-cyclic-AMP + diphosphate
show the reaction diagram
P00936
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the class I enzyme shows a requirement for free metal ions in addition to the MgATP2- complex, operating with a two-metal-ion mechanism in analogy to class II and calss III enzymes. The native enzyme shows very little activity when the concentration of Mg2+ is much lower than that of ATP, and activity rises strongly when the concentration of Mg2+ exceeds that of ATP
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'(3')-O-(N-methylanthraniloyl)-ADP
slight competitive inhibition
2'(3')-O-(N-methylanthraniloyl)-AMP
slight competitive inhibition
2'(3')-O-(N-methylanthraniloyl)-ATP
competitive
3-[(9-oxo-9H-fluorene-1-carbonyl)-amino]-benzoic acid
-
-
ATP
-
high concentrations
Co2+
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high concentrations
KH2PO4
-
-
Mercuric acetate
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nucleotides
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-
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pyridoxal 5'-phosphate
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-
Ribonucleoside triphosphates
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-
additional information
inhibition of mutant catalytic domains by 2'(3')-O-(N-methylanthraniloyl)-modified nucleotides is reduced compared to the wild-type catalytic domain Cya2-446, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.153 - 4.7
ATP
0.45
ATP
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.67
ATP
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-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
2'(3')-O-(N-methylanthraniloyl)-ATP
pH 8.0, 37C, versus ATP, wild-type catalytic domain Cya2-446
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.281
purified recombinant catalytic domain mutant S106A, 10 mM Mg2+
0.396
purified recombinant catalytic domain mutant K136A, 10 mM Mg2+
0.48
purified recombinant catalytic domain mutant W374A, 10 mM Mg2+
0.513
purified recombinant catalytic domain mutant Y394A, 10 mM Mg2+
0.526
purified recombinant catalytic domain mutant K253A, 10 mM Mg2+
0.614
purified recombinant catalytic domain mutant R19A, 10 mM Mg2+
0.665
purified recombinant catalytic domain, 10 mM Mg2+
0.752
purified recombinant catalytic domain mutant E242A, 10 mM Mg2+
0.778
purified recombinant catalytic domain mutant W249A, 10 mM Mg2+
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9
recombinant catalytic domain Cya2-446
8.5
native holoenzyme
9 - 9.5
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-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.6
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
native holoenzyme
47
recombinant catalytic domain Cya2?446
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 47
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-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
92000 - 110000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
structure-function relationship, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-40
-
more than 5 days
-25
-
5 days
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilized by ATP or at -20C as an ammonium sulfate precipitate or in 50% glycerol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C (NH4)2SO4 precipitate, 50% glycerol, 5 mM ATP, 3 months
-
liquid N2, several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant catalytic domain Cya2-446 from strain BL21(DE3) by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
class I AC gene, overexpression of wild-type and mutant catalytic domain, residues 2-446, i.e. Cya2-446, in strain BL21(DE3)
overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D114A
site-directed mutagenesis, the almost inactive mutant shows highly reduced activity compared to the wild-type enzyme
D116A
site-directed mutagenesis, the almost inactive mutant shows highly reduced activity compared to the wild-type enzyme
D300A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E185A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E242A
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km compared to the wild-type enzyme
K136A
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km compared to the wild-type enzyme
K253A
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km compared to the wild-type enzyme
K260A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K264A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K332A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R19A
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km compared to the wild-type enzyme
S103A
site-directed mutagenesis, the mutant has a 17fold higher Km for ATP compared to the wild-type enzyme, and the mutation causes a marked reduction of discrimination between ATP- and ADP- or AMP-derived inhibitors
S106A
site-directed mutagenesis, the mutation reduces the mutant activity to 25% of the wild-type enzyme activity, kinetic analysis show a 58% reduction of the Vmax and a doubling of the Km compared to the wild-type enzyme
S113A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
T189A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W118A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W200A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W249A
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km compared to the wild-type enzyme
W374A
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km compared to the wild-type enzyme
Y394A
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km compared to the wild-type enzyme
D414B
-
mutant does not show increased cAMP levels
G463D
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mutant does not show increased cAMP levels
R188H
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mutant does not show increased cAMP levels