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Information on EC 4.6.1.1 - adenylate cyclase and Organism(s) Arthrospira platensis and UniProt Accession O32393

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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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Arthrospira platensis
UNIPROT: O32393
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Word Map
The taxonomic range for the selected organisms is: Arthrospira platensis
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 III adenylate cyclase
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3',5'-cyclic AMP synthetase
-
-
-
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AC2
-
-
-
-
AC3
-
-
-
-
ACTP10
-
-
-
-
adenyl cyclase
-
-
-
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Adenylate cyclase, olfactive type
-
-
-
-
adenylyl cyclase
Adenylyl cyclase type 10
-
-
-
-
adenylylcyclase
-
-
-
-
ATP pyrophosphate-lyase
-
-
-
-
Ca(2+)-inhibitable adenylyl cyclase
-
-
-
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Ca(2+)/calmodulin activated adenylyl cyclase
-
-
-
-
class III adenylyl cyclase
-
-
cyclase, adenylate
-
-
-
-
Edema factor
-
-
-
-
Rutabaga protein
-
-
-
-
xlAC
-
-
-
-
additional information
the enzyme belongs to the class III adenylyl cyclase superfamily
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
-
-
-
-
?
ATP
3',5'-cyclic AMP + diphosphate
show the reaction diagram
-
-
?
ATP
cAMP + diphosphate
show the reaction diagram
-
-
-
-
?
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
-
-
-
?
ATP
3',5'-cyclic AMP + diphosphate
show the reaction diagram
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
1 mM, strong activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2,3,4,5,6,7,8,13,13,14,14-dodecachloro-1,4,4a,4b,5,8,8a,12b-octahydro-11-sulfo-1,4:5,8-dimethanotriphenylene-10-carboxylic acid
the compound defines an AC inhibitor scaffold with high affinity for human soluble isozyme and less inhibitory effect on mammalian transmembrane isozymes
1-(bromo(1-naphthyl)methyl)naphthalene
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17beta-estra-1(10),2,4-triene-2,3,17-triol
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2,3,6,23-tetrahydroxyurs-12-en-28-oic acid
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2,3-dibromo-1-(4-(hydroxy(oxido)amino)phenyl)-3-(4-quinolinyl)-1-propanone
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3,20-dioxopregn-4-en-21-yl 4-bromobenzenesulfonate
4,5,6,7-tetrachloro-3,3-bis(6-hydroxy[1,1'-biphenyl]-3-yl)-2-benzofuran-1(3H)-one
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5'-benzyl-12'-hydroxy-2'-methyl-3',6',18-trioxoergotaman
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2-hydroxyestradiol
-
IC50 of about 2 microM
4-hydroxyestradiol
-
-
catechol
-
noncompetetive inhibitor
additional information
structure-based development of adenylyl cyclase inhibitors, compounds exploiting the catechol estrogen binding site can produce potent, isoform discriminating adenylyl cyclase inhibitors, inhibitory potency of compounds, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bicarbonate
additional information
-
2-4fold enhancement of adenylate cyclase activity by the histidine kinase-receiver system, histidine kinase domain autophosphorylates on His572, subsequently the phosphate is transferred to the second receiver domain Asp895, which is adjacent to the CHD domain
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005
1,2,3,4,5,6,7,8,13,13,14,14-dodecachloro-1,4,4a,4b,5,8,8a,12b-octahydro-11-sulfo-1,4:5,8-dimethanotriphenylene-10-carboxylic acid
Arthrospira platensis
-
0.2
1-(bromo(1-naphthyl)methyl)naphthalene
Arthrospira platensis
about
0.001
17beta-estra-1(10),2,4-triene-2,3,17-triol
Arthrospira platensis
-
0.1
2,3,6,23-tetrahydroxyurs-12-en-28-oic acid
Arthrospira platensis
about
0.1
2,3-dibromo-1-(4-(hydroxy(oxido)amino)phenyl)-3-(4-quinolinyl)-1-propanone
Arthrospira platensis
about
0.015
3,20-dioxopregn-4-en-21-yl 4-bromobenzenesulfonate
Arthrospira platensis
-
0.1
4,5,6,7-tetrachloro-3,3-bis(6-hydroxy[1,1'-biphenyl]-3-yl)-2-benzofuran-1(3H)-one
Arthrospira platensis
about
0.07
5'-benzyl-12'-hydroxy-2'-methyl-3',6',18-trioxoergotaman
Arthrospira platensis
about
0.002
2-hydroxyestradiol
Arthrospira platensis
-
IC50 of about 2 microM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00036
in the presence of 1 mM Mg2+, recombinant C-terminal CyaG domain
0.011
in the presence of 1 mM Mn2+, recombinant C-terminal CyaG domain
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cyaC
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O32393_ARTPT
1202
0
133924
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
complex with 2-hydroxyestradiol and alpha/beta-methylene-ATP, 20-3 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K533E
no activity
K533E/I603R/D605C
mutant lose adenylyl cyclase activity but obtains significant guanylyl cyclase activity
additional information
-
mutation of either His572 or Asp895 greatly reduces AC activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminal domain
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the N-terminally His-tagged catalytic domain of CyaC
expression of C-terminal domain as GST-fusion protein in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kasahara, M.; Unno, T.; Yashiro, K.; Ohmori, M.
CyaG, a novel cyanobacterial adenylyl cyclase and a possible ancestor of mammalian guanylyl cyclases
J. Biol. Chem.
276
10564-10569
2001
Arthrospira platensis (Q9EXQ2), Arthrospira platensis
Manually annotated by BRENDA team
Steegborn, C.; Litvin, T.N.; Hess, K.C.; Capper, A.B.; Taussig, R.; Buck, J.; Levin, L.R.; Wu, H.
A novel mechanism for adenylyl cyclase inhibition from the crystal structure of its complex with catechol estrogen
J. Biol. Chem.
280
31754-31759
2005
Homo sapiens, Arthrospira platensis
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
Schlicker, C.; Rauch, A.; Hess, K.C.; Kachholz, B.; Levin, L.R.; Buck, J.; Steegborn, C.
Structure-based development of novel adenylyl cyclase inhibitors
J. Med. Chem.
51
4456-4464
2008
Rattus norvegicus, Arthrospira platensis (O32393), Homo sapiens (Q96PN6), Homo sapiens
Manually annotated by BRENDA team