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Information on EC 4.6.1.1 - adenylate cyclase and Organism(s) Bos taurus and UniProt Accession P19754

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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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Bos taurus
UNIPROT: P19754
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
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
-
-
-
-
AC1
-
-
AC4
-
-
AC5
-
-
AC6
-
-
AC7
-
-
AC8
-
-
AC9
-
-
ACTP10
-
-
-
-
adenyl cyclase
-
-
-
-
Adenylate cyclase, olfactive type
-
-
-
-
adenylate cyclases I
-
-
adenylate cyclases IV
-
-
adenylate cyclases VI
-
-
adenylyl cyclase
-
-
-
-
Adenylyl cyclase type 10
-
-
-
-
adenylylcyclase
-
-
-
-
ATP pyrophosphate-lyase
-
-
-
-
Ca(2+)-inhibitable adenylyl cyclase
-
-
-
-
Ca(2+)/calmodulin activated adenylyl cyclase
-
-
-
-
cyclase, adenylate
-
-
-
-
Edema factor
-
-
-
-
Rutabaga protein
-
-
-
-
sAC
-
-
soluble adenylyl cyclase
-
-
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'-cAMP + diphosphate
show the reaction diagram
-
-
-
?
ATP
3',5'-cAMP + diphosphate
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
-
activation
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
-
F-
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',5'-dideoxyadenosine
-
inhibitor significantly inhibits heparin-induced capacitation of sperm cells
beta, gamma subunit of the guanine-nucleotide binding regulatory protein
-
-
-
Ca2+
-
-
Chloropromazine
-
-
Dextran sulfate
-
-
-
Polyvinyl sulfate
-
-
Trifluoperazine
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
forskolin
-
Galphas
-
-
Gbetagamma
a second isoform- and regulator-specific contact site in C2 is necessary to render enzyme activity susceptible to Gbetagamma modulation. In addition to the PFAHL-motif in C1b of ACII, Gbetagamma contacts the KF-loop in C2
-
5'-guanylimidodiphosphate
-
activation
alpha subunit of the guanine-nucleotide binding regulatory protein
-
activation
-
BIM-1
-
specific protein-kinase C inhibitor, significantly increases cumulus cell cAMP concentrations
clonidine
-
slight stimulatory effect on cAMP concentrations
EGTA
-
significantly increases cumulus cell cAMP concentrations
forskolin
glucagon
-
activation
guanosine 5'-(beta,gamma-imido)triphosphate
-
activation
H89
-
specific inhibitor of protein-kinase A, significantly increases cumulus cell cAMP concentrations at 0.0001 and 0.03 mM
ionomycin
-
increases intracellular Ca2+ concentrations, significantly increases cumulus cell cAMP concentrations
NaF
-
activation
pertussis toxin
-
catalyses ADP-ribosylation of a cysteine residue on GalphaI, causing the G-protein complex to become uncoupled from the receptor, significantly increases cAMP concentrations
-
staurosporine
-
non-specific protein-kinase C inhibitor, significantly increases cumulus cell cAMP concentrations
thapsigargin
-
increases intracellular Ca2+ concentrations, significantly increases cumulus cell cAMP concentrations
additional information
-
cholera toxin, KN-62, phorbol-12-myristate-13-acetate and BAPTA-am or a combination of 3 mM EGTA plus BAPTA-am have no effect on cAMP concentrations
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07 - 5
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.33
ATP
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100 - 150
-
-
2.7
-
-
46
-
forskolin-eluted
6.35
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
-
7.8
-
membrane-bound
8.3
-
solubilized enzyme
8.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
AC isoforms 3, 4, 6, 8, and 9
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
sAC
Manually annotated by BRENDA team
additional information
-
AC isoforms 1, 3, 4, 6, and 9 in cumulus cells. AC1, AC4 and AC6 predominate
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
hyaluronic acid and heparin are physiological glycosaminoglycans capable of inducing in vitro capacitation in cryopreserved bull sperm, stimulating different enzymatic pathways and intracellular signals modulated by a membrane-associated adenylate cyclase. Hyaluronic acid induces sperm capacitation involving LDH and CK activities, thereby reducing oxidative metabolism, and this process is mediated by membrane-associated adenylate cyclase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADCY1_BOVIN
1134
11
123979
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
115000
-
catalytic unit, SDS-PAGE
135000
-
SDS-PAGE
150000
358000
-
sucrose density gradient centrifugation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V1027A/L1031A
is not catalytically active under basal, Galphas- or forskolin-stimulated conditions
additional information
ACI-deletion mutants ACI.lambda1057 with reduced catalytic activity and ACI.lambda1094, which like mutant ACIlambda1057 is active and stimulated by Ca/CaM as well as ACI. Mutant ACII.lambda928 is catalytically inactive, mutant ACII.AA930 shows diminished activity, mutants ACII.AA925 or ACII.AA932 show no significant change in Gbetagamma-regulation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-80
-
1 month
4
-
1 week
45
-
up to
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 12 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
different methods
-
partial
-
recombinant adenylyl cyclase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Sf9 cells
expression in HEK 293 cells
-
expression in Sf9 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
isoform Adcy1 catalytic activity can be delicately adjusted by mediating calmodulin activation of Adcy1 by reversible Met oxidation in calmodulin
medicine
-
cumulus cells possess multiple active isoforms of adenylyl cyclase, each isoform may have a specific role at a specific time during oocyte growth and maturation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shattuck, R.L.; Oldenburg, D.J.; Storm, D.R.
Purification and characterization of a calmodulin-sensitive adenylate cyclase from Bordetella pertussis
Biochemistry
24
6356-6362
1985
Bordetella pertussis, Bos taurus
Manually annotated by BRENDA team
Yeager, R.E.; Heideman, W.; Rosenberg, G.B.; Storm, D.R.
Purification of the calmodulin-sensitive adenylate cyclase from bovine cerebral cortex
Biochemistry
24
3776-3783
1985
Bos taurus
Manually annotated by BRENDA team
Wolff, J.; Cook, G.H.
Microtubule-associated adenylate cyclase
Biochim. Biophys. Acta
844
34-41
1985
Bos taurus
Manually annotated by BRENDA team
Asbury, R.F.; Cook, G.H.; Wolff, J.
Soluble adenylate cyclase from thyroid membranes
J. Biol. Chem.
253
5286-5292
1978
Bos taurus
Manually annotated by BRENDA team
Herman, C.A.; Zahler, W.L.; Doak, G.A.; Campbell, B.J.
Bull sperm adenylate cyclase: localization and partial characterization
Arch. Biochem. Biophys.
177
622-629
1976
Bos taurus
Manually annotated by BRENDA team
Tang, W.J.; Krupinski, J.; Gilman, A.G.
Expression and characterization of calmodulin-activated (type I) adenylylcyclase
J. Biol. Chem.
266
8595-8603
1991
Bos taurus
Manually annotated by BRENDA team
Moos Jr., M.; Morris, D.I.; Robbins, J.; Appel, L.; Seamon, K.B.
Purification of bovine brain adenylyl cyclase with a novel derivative of forskolin: evidence for a high specific activity form of the enzyme
Prep. Biochem. Biotechnol.
26
155-167
1996
Bos taurus
Manually annotated by BRENDA team
Wang, P.; Storm, D.R.
Purification and characterization of calmodulin-sensitive adenylyl cyclase from bovine brain
Methods Enzymol.
195
65-82
1991
Bos taurus
Manually annotated by BRENDA team
Diel, S.; Beyermann, M.; Navarro Llorens, J.M.; Wittig, B.; Kleuss, C.
Two Interaction Sites on Mammalian Adenylyl Cyclase Type I and II: modulation by calmodulin and Gbetagamma
Biochem. J.
411
449-456
2008
Bos taurus (P19754)
Manually annotated by BRENDA team
Lastro, M.; Collins, S.; Currie, W.B.
Adenylyl cyclases in oocyte maturation: a characterization of AC isoforms in bovine cumulus cells
Mol. Reprod. Dev.
73
1202-1210
2006
Bos taurus
Manually annotated by BRENDA team
Fernandez, S.; Cordoba, M.
A membrane-associated adenylate cyclase modulates lactate dehydrogenase and creatine kinase activities required for bull sperm capacitation induced by hyaluronic acid
Anim. Reprod. Sci.
179
80-87
2017
Bos taurus
Manually annotated by BRENDA team
Luebker, C.; Urbauer, R.; Moskovitz, J.; Dove, S.; Weisemann, J.; Fedorova, M.; Urbauer, J.; Seifert, R.
Membranous adenylyl cyclase 1 activation is regulated by oxidation of N- and C-terminal methionine residues in calmodulin
Biochem. Pharmacol.
93
196-209
2015
Bos taurus (P19754)
Manually annotated by BRENDA team