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

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EC Tree
IUBMB Comments
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.
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Escherichia coli
UNIPROT: P00936
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
adenylate cyclase, adenylyl cyclase, adenyl cyclase, pituitary adenylate cyclase, edema factor, adenylylcyclase, soluble adenylyl cyclase, adenylate cyclase toxin, adcy5, aciii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
class I adenylate cyclase
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3',5'-cyclic AMP synthetase
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-
-
-
AC2
-
-
-
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AC3
-
-
-
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ACTP10
-
-
-
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adenyl cyclase
-
-
-
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Adenylate cyclase, olfactive type
-
-
-
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adenylyl cyclase
Adenylyl cyclase type 10
-
-
-
-
adenylylcyclase
-
-
-
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ATP pyrophosphate-lyase
-
-
-
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Ca(2+)-inhibitable adenylyl cyclase
-
-
-
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Ca(2+)/calmodulin activated adenylyl cyclase
-
-
-
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class I AC
-
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cyclase, adenylate
-
-
-
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Edema factor
-
-
-
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Rutabaga protein
-
-
-
-
xlAC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P-O bond cleavage
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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
-
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
?
-
NATURAL SUBSTRATE
NATURAL 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
-
-
-
?
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
INHIBITOR
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
diphosphate
-
-
KH2PO4
-
-
Mercuric acetate
-
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nucleotides
-
-
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pyridoxal 5'-phosphate
-
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Ribonucleoside triphosphates
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.153 - 4.7
ATP
0.45
ATP
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.67
ATP
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
2'(3')-O-(N-methylanthraniloyl)-ATP
pH 8.0, 37°C, 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
native holoenzyme
8.5 - 9
recombinant catalytic domain Cya2-446
9 - 9.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.6
-
-
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
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
class I AC gene
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
92000 - 110000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
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
-
mutant does not show increased cAMP levels
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-25
-
5 days
-40
-
more than 5 days
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilized by ATP or at -20°C as an ammonium sulfate precipitate or in 50% glycerol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C (NH4)2SO4 precipitate, 50% glycerol, 5 mM ATP, 3 months
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, J.K.; Epstein, W.
Purification and characterization of adenylate cyclase from Escherichia coli K12
J. Biol. Chem.
258
3750-3758
1983
Glutamicibacter nicotianae, Escherichia coli
Manually annotated by BRENDA team
Janecek, J.; Naprstek, J.; Dobrova, Z.; Jiresova, M.; Spizek, J.
Characterization of adenylate cyclase from Escherichia coli
Folia Microbiol. (Praha)
25
361-368
1980
Glutamicibacter nicotianae, Escherichia coli
Manually annotated by BRENDA team
Tao, M.
Preparation and properties of adenylate cyclase from Escherichia coli
Methods Enzymol.
38C
155-160
1974
Glutamicibacter nicotianae, Escherichia coli
Manually annotated by BRENDA team
Ide, M.
Adenyl cyclase of bacteria
Arch. Biochem. Biophys.
144
262-268
1971
Alcaligenes faecalis, Arthrobacter citreus, Arthrobacter globiformis, Glutamicibacter nicotianae, Rhodococcus equi, Escherichia coli, Pectobacterium carotovorum, Micrococcus flavus, Micrococcus luteus, Nocardia erythropolis
-
Manually annotated by BRENDA team
Reddy, P.; Peterkofsky, A.; McKenney, K.
Hyperexpression and purification of Escherichia coli adenylate cyclase using a vector designed for expression of lethal gene products
Nucleic Acids Res.
17
10473-10488
1989
Escherichia coli
Manually annotated by BRENDA team
Crasnier, M.; Danchin, A.
Characterization of Escherichia coli adenylate cyclase mutants with modified regulation
J. Gen. Microbiol.
136
1825-1831
1990
Escherichia coli
Manually annotated by BRENDA team
Linder, J.U.
Class III adenylyl cyclases: molecular mechanisms of catalysis and regulation
Cell. Mol. Life Sci.
63
1736-1751
2006
Bacillus anthracis, Bordetella pertussis, Saccharomyces cerevisiae, Caenorhabditis elegans, Chlamydomonas reinhardtii, Chloroflexus aurantiacus, Dictyostelium discoideum, Drosophila melanogaster, Escherichia coli, Euglena gracilis, Mus musculus, Myxococcus xanthus, Pseudomonas aeruginosa, Rattus norvegicus, Sinorhizobium meliloti, Schizosaccharomyces pombe, Arthrospira platensis, Trypanosoma brucei, Ustilago maydis, Yersinia enterocolitica, Mycobacterium tuberculosis (P9WQ35), Nostoc sp. PCC 7120 = FACHB-418 (Q7A2D9), Nostoc sp. PCC 7120 = FACHB-418 (Q8YMH0), Nostoc sp. PCC 7120 = FACHB-418 (Q8YVS0), Mycobacterium tuberculosis H37Rv (P9WQ35)
Manually annotated by BRENDA team
Linder, J.U.
Structure-function relationships in Escherichia coli adenylate cyclase
Biochem. J.
415
449-454
2008
Escherichia coli (P00936), Escherichia coli
Manually annotated by BRENDA team
Moen, S.T.; Blumentritt, C.A.; Slater, T.M.; Patel, S.D.; Tutt, C.B.; Estrella-Jimenez, M.E.; Pawlik, J.; Sower, L.; Popov, V.L.; Schein, C.H.; Gilbertson, S.R.; Peterson, J.W.; Torres, A.G.
Testing the efficacy and toxicity of adenylyl cyclase inhibitors against enteric pathogens using in vitro and in vivo models of infection
Infect. Immun.
78
1740-1749
2010
Escherichia coli
Manually annotated by BRENDA team