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Information on EC 4.6.1.1 - adenylate cyclase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC4.6.1.1

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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.

The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
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
3',5'-cyclic AMP synthetase
-
-
-
-
AC2
-
-
-
-
AC3
-
-
-
-
ACTP10
-
-
-
-
adenyl cyclase
-
-
-
-
Adenylate cyclase, olfactive type
-
-
-
-
adenylyl cyclase
Adenylyl cyclase type 10
-
-
-
-
adenylylcyclase
-
-
-
-
ATP pyrophosphate-lyase
-
-
-
-
Ca(2+)-inhibitable adenylyl cyclase
-
-
-
-
Ca(2+)/calmodulin activated adenylyl cyclase
-
-
-
-
class III adenylyl cyclase
-
-
class IIIb AC
-
-
cyclase, adenylate
-
-
-
-
Edema factor
-
-
-
-
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
LITERATURE
COMMENTARY hide
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP
3',5'-cAMP + diphosphate
show the reaction diagram
ATP
3',5'-cyclic AMP + diphosphate
show the reaction diagram
Substrates: -
Products: -
?
ATP
3',5'-cyclic-AMP + diphosphate
show the reaction diagram
-
Substrates: -
Products: -
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP
3',5'-cyclic AMP + diphosphate
show the reaction diagram
Substrates: -
Products: -
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
Mn2+
-
required, the enzyme has higher specific activity for Mn2+-ATP versus Mg2+-ATP
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxyestradiol
significant inhibition at 0.1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
-
no detectable stimulation of enzyme activity
crude extract of cytosolic proteins from CHO cells
-
at least 500fold increased adenylate cyclase activity
-
additional information
-
is activated by different host cell factors and is inactive until injected into the host cell
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0667
ATP
-
pH 8.5, 40Ā°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide Go to Organism Search
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide Go to Localization Search
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the N-terminal half of the class IIIb AC consists of a predicted membrane-associated sensor domain
Manually annotated by BRENDA team
Highest Expressing Human Cell Lines
Cell Line Links Gene Links
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A241XW13_PSEAI
951
0
108882
TrEMBL
-
A0A643HYJ2_PSEAI
950
0
108756
TrEMBL
-
A0A8G2S4G3_PSEAI
950
0
108725
TrEMBL
-
A0A8G6VYI7_PSEAI
950
0
108834
TrEMBL
-
A0A6B1YDW2_PSEAI
950
0
108771
TrEMBL
-
A0A8G4TNZ3_PSEAI
950
0
108775
TrEMBL
-
A0A8G7F0D9_PSEAI
950
0
108814
TrEMBL
-
A0A8G7CGD4_PSEAI
950
0
108799
TrEMBL
-
A0A8G6IK29_PSEAI
950
0
108805
TrEMBL
-
A0A509JFF0_PSEAI
950
0
108802
TrEMBL
-
A0A8G4DV43_PSEAI
950
0
108865
TrEMBL
-
A0A8G2NT83_PSEAI
950
0
108763
TrEMBL
-
A0A8B4ZNS4_PSEAI
950
0
108822
TrEMBL
-
A0A8G7PWN3_PSEAI
950
0
108871
TrEMBL
-
A0A7M2ZX67_PSEAI
950
0
108849
TrEMBL
-
A0A8G3DHS8_PSEAI
950
0
108787
TrEMBL
-
A0A8G2TBC8_PSEAI
950
0
108871
TrEMBL
-
A0A5E9WAV8_PSEAI
950
0
108805
TrEMBL
-
A0A8G7BKP3_PSEAI
950
0
108849
TrEMBL
-
A0A2R3IMY9_PSEAI
446
4
49611
TrEMBL
-
A0A8G6I5Y8_PSEAI
950
0
108821
TrEMBL
-
A0A8G2QW07_PSEAI
950
0
108873
TrEMBL
-
A0A8G3QEE6_PSEAI
950
0
108772
TrEMBL
-
A0A8G3SGL9_PSEAI
950
0
108738
TrEMBL
-
A0A659BE75_PSEAI
950
0
108793
TrEMBL
-
A0A8G5T537_PSEAI
950
0
108771
TrEMBL
-
A0A6A9KES9_PSEAI
950
0
108661
TrEMBL
-
A0A8A4F6I7_PSEAI
950
0
108805
TrEMBL
-
A0A8G4HEX8_PSEAI
950
0
108848
TrEMBL
-
A0A3S0L2A2_PSEAI
944
0
107462
TrEMBL
-
A0A8G3YL32_PSEAI
950
0
108747
TrEMBL
-
A0A8H0WX40_PSEAI
950
0
108821
TrEMBL
-
A0A8G6E2K2_PSEAI
950
0
108772
TrEMBL
-
A0A8G4BD06_PSEAI
950
0
108830
TrEMBL
-
A0A8G4K387_PSEAI
950
0
108833
TrEMBL
-
A0A8G4L5P8_PSEAI
950
0
108789
TrEMBL
-
A0A8F9L8W9_PSEAI
950
0
108819
TrEMBL
-
A0A4U6X1V9_PSEAI
950
0
108791
TrEMBL
-
A0A8G6ZC68_PSEAI
950
0
108741
TrEMBL
-
A0A8G3Y9W8_PSEAI
950
0
108844
TrEMBL
-
A0A485FJ83_PSEAI
413
3
45821
TrEMBL
-
A0A8G3PFI8_PSEAI
950
0
108880
TrEMBL
-
A0A8G7H8Q3_PSEAI
950
0
108808
TrEMBL
-
A0A8G3MFR3_PSEAI
950
0
108818
TrEMBL
-
A0A8G3KEU0_PSEAI
950
0
108808
TrEMBL
-
A0A8G4WLL6_PSEAI
950
0
108821
TrEMBL
-
A0A8G4NJT3_PSEAI
950
0
108805
TrEMBL
-
A0A8G3DCD6_PSEAI
950
0
108733
TrEMBL
-
A0A367MCV5_PSEAI
950
0
108755
TrEMBL
-
A0A8G2RSE5_PSEAI
950
0
108763
TrEMBL
-
A0A8G6V8Z9_PSEAI
950
0
108819
TrEMBL
-
A0A8G2WRB4_PSEAI
951
0
108878
TrEMBL
-
A0A8G5V914_PSEAI
950
0
108879
TrEMBL
-
A0A8F9NKC8_PSEAI
950
0
108849
TrEMBL
-
A0A8G6ZRN1_PSEAI
950
0
108830
TrEMBL
-
A0A8G4AMN3_PSEAI
950
0
108762
TrEMBL
-
A0A8G3JF28_PSEAI
950
0
108714
TrEMBL
-
A0A8G5ZD27_PSEAI
950
0
108836
TrEMBL
-
A0A8G3ZJD6_PSEAI
950
0
108794
TrEMBL
-
A0A8G7L8U2_PSEAI
950
0
108767
TrEMBL
-
A0A8F9JRY0_PSEAI
950
0
108681
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
2 * 40000, SDS-PAGE
41670
-
predicted after nucleotide sequence analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using 0.1 M 4-morpholineethanesulfonic acid (pH 6.5) and 12% (w/v) polyethylene glycol 20000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A197T
the mutant shows increased activity compared to the wild type enzyme
D212N
-
mutant with no detectable enzyme activity
D214N
-
mutant with no detectable enzyme activity
E189R
the mutant shows increased activity compared to the wild type enzyme
E377G
the mutant shows increased activity compared to the wild type enzyme
F399H
the mutant shows increased activity compared to the wild type enzyme
F399I
the mutant shows increased activity compared to the wild type enzyme
I352T
the mutant shows increased activity compared to the wild type enzyme
K274A
-
the mutation significantly reduces adenylate cyclase activity
K81M
-
mutant with no detectable enzyme activity
K88I
-
mutant with no detectable enzyme activity
L326P
the mutant shows increased activity compared to the wild type enzyme
r23ExoY
-
mutant with histidine tag at carboxyl-terminal position, detectable enzyme activity
R318W
the mutant shows increased activity compared to the wild type enzyme
R412H
the mutant shows slightly increased activity compared to the wild type enzyme
R456L
the mutant shows strongly increased activity compared to the wild type enzyme
rExoY
-
mutant with histidine tag at amino-terminal position, detectable enzyme activity
T351A
-
the mutation significantly reduces adenylate cyclase activity
additional information
-
disruption of a class IIIb AC gene results in strong attenuation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity resin column chromatography
-
Ni-NTA agarose column chromatography and Superose 12 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli SG13009[pREP4] andM15[pREP4] cells
expression in Escherichia coli
-
the putative catalytic domain (amino acids 217-463) as an N-terminal hexahistidine fusion is expressed in Escherichia coli M15[pREP4] cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
is an exotoxin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yahr, T.L.; Vallis, A.J.; Hancock, M.K.; Barbieri, J.T.; Frank, D.W.
ExoY, an adenylate cyclase secreted by the Pseudomonas aeruginosa type III system
Proc. Natl. Acad. Sci. USA
95
13899-13904
1998
Pseudomonas aeruginosa
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
Sinha, S.C.; Sprang, S.R.
Structure, mechanism, regulation and evolution of class III nucleotidyl cyclases
Rev. Physiol. Biochem. Pharmacol.
157
105-140
2007
Aeromonas hydrophila, Bacillus anthracis, Prevotella ruminicola, Bordetella pertussis, Canis lupus familiaris, Caulobacter vibrioides, Escherichia sp., Haemophilus sp., Mycobacterium tuberculosis, Yersinia pestis, Pseudomonas sp., Pseudomonas aeruginosa, Rattus norvegicus, Rhizobium etli, Sinorhizobium meliloti, Arthrospira platensis, Trypanosoma brucei, Vibrio parahaemolyticus, Yersinia sp.
Manually annotated by BRENDA team
Fulcher, N.B.; Holliday, P.M.; Klem, E.; Cann, M.J.; Wolfgang, M.C.
The Pseudomonas aeruginosa Chp chemosensory system regulates intracellular cAMP levels by modulating adenylate cyclase activity
Mol. Microbiol.
76
889-904
2010
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAK
Manually annotated by BRENDA team
Topal, H.; Fulcher, N.B.; Bitterman, J.; Salazar, E.; Buck, J.; Levin, L.R.; Cann, M.J.; Wolfgang, M.C.; Steegborn, C.
Crystal structure and regulation mechanisms of the CyaB adenylyl cyclase from the human pathogen Pseudomonas aeruginosa
J. Mol. Biol.
416
271-286
2012
Pseudomonas aeruginosa (Q9HZ23), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9HZ23)
Manually annotated by BRENDA team