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4.6.1.1: adenylate cyclase

This is an abbreviated version!
For detailed information about adenylate cyclase, go to the full flat file.

Word Map on EC 4.6.1.1

Reaction

ATP
=
3',5'-cyclic AMP
+
diphosphate

Synonyms

3',5'-cyclic AMP synthetase, AC, AC 1, AC 2, AC 3, AC 4, AC 5, AC 7, AC 8, AC 9, AC Rv1625c, AC toxin, AC-IV, AC-V, AC-VI, AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8, AC9, ACA, ACB, ACbeta, ACG, ACI, ACII, ACIII, ACT, ACTP10, ACV, ACVI, ADCY10, Adcy5, adenyl cyclase, adenylate cyclase, adenylate cyclase 1, adenylate cyclase 10, adenylate cyclase 5, adenylate cyclase 6, adenylate cyclase toxin, adenylate cyclase type 10, adenylate cyclase type 5, adenylate cyclase [ATP pyrophosphate-lyase (cyclizing)], Adenylate cyclase, olfactive type, adenylate cyclases I, adenylate cyclases IV, adenylate cyclases VI, adenylyl cyclase, adenylyl cyclase 1, adenylyl cyclase 2, adenylyl cyclase 5, adenylyl cyclase 6, adenylyl cyclase 8, adenylyl cyclase 9, adenylyl cyclase toxin, adenylyl cyclase type 1, Adenylyl cyclase type 10, adenylyl cyclase type 5, adenylyl cyclase type 6, adenylyl cyclase type 8, adenylyl cyclase type V, adenylyl cyclase type VI, adenylyl cyclase VI, adenylyl cyclase VII, adenylyl cyclase, type-V, adenylyl cyclase, type-VI, adenylyl cyclase-5, adenylyl cyclase-beta, adenylyl cyclase-V, adenylyl cyclases 1, adenylyl cyclases 8, adenylylcyclase, Amac3, ATP pyrophosphate-lyase, ATP-diphosphate-lyase cyclizing, ATP-pyrophosphate lyase cyclizing, bacterial photoactivated adenylyl cyclase, BGP_1043, bPAC, Ca(2+)-inhibitable adenylyl cyclase, Ca(2+)/calmodulin activated adenylyl cyclase, Ca(II)- and calmodulin-dependent adenylyl cyclase edema factor, Ca-stimulated type 8 adenylyl cyclase, Ca2+-calmodulin stimulated adenylyl cyclase type 8, Ca2+-dependent adenylyl cyclase, Ca2+/calmodulin-stimulated adenylyl cyclase 1, calcium-sensitive adenylyl cyclase, calcium-stimulated adenylyl cyclase, class I AC, class I adenylate cyclase, class II AC, class III AC, class III adenylate cyclase, class III adenylyl cyclase, class IIIb AC, class IV AC, class IV adenylyl cyclase, class IVadenylyl cyclase, class V AC, class VI AC, Cya, Cya1, CyaA, CyaA toxin, CyaB, cyaB1, CyaB1 adenylyl cyclase, CyaB2, cyaC, CyaG, cyclase, adenylate, Cyr1p, Edema factor, ExoY, G protein-regulated adenylyl cyclase, GRESAG 4.1, GRESAG 4.3, GRESAG4.1, group 1 adenylyl cyclase, IIC2, ion-channel adenylyl cyclase, Ma1120, mAC, MAP0426c, MAP1279c, MAP1318c, MAP1357, MAP2079, MAP2250c, MAP2440, MAP2507c, MAP2672, MAP2695c, MAP3844, MAP4266, membrane adenylyl cyclase, ML1399, MM0123, MM0157, MM0286, MM0666, MM0730, MM0935, MM1414, MM2428, MM2454, MM2550, MM2962, MM3042, MM3043, MM3257, MM3505, MM3522, MM3640, MM3755, MM3757, MM3795, MM4078, MM4079, MM4080, MM4120, MM4173, MM4340, MM4370, MM4438, MM5137, MM5254, MM5257, More, MSMEG0218, MSMEG0536, MSMEG3253, MSMEG3579, MSMEG3786, MSMEG4282, MSMEG4472, MSMEG4909, MSMEG5003, MSMEG6117, Oscil6304_3613, PAC, particulate adenylyl cyclase, PfACalpha, pituitary adenylate cyclase, PleD, Rutabaga protein, Rv0386, Rv0891c, Rv1120c, Rv1264, Rv1318c, Rv1319c, Rv1320c, Rv1358, Rv1359, Rv1625c, Rv1647, Rv1900c, Rv2212, Rv2435c, Rv2488c, Rv3645, Ry1625c, sAC, sACI/II, SACY, Slr1991 adenylyl cyclase, soluble AC, soluble adenylate cyclase, soluble adenylyl cyclase, TczAC, tmAC, transmembrane adenylyl cyclase, transmembrane adenylyl cyclase type 1, transmembrane adenylyl cyclase type 3, transmembrane adenylyl cyclase type 8, type 1 AC, type 1 adenylyl cyclase, type 1 Ca2+/calmodulin-stimulated adenylyl cyclase, type 3 adenylyl cyclase, type 5 adenylyl cyclase, type 6 adenylyl cyclase, type 8 AC, type 8 adenylyl cyclase, type I adenylate cyclase, type II AC, type III adenylyl cyclase, type V AC, type V adenylate cyclase, type V adenylyl cyclase, type VI adenylyl cyclase, type VIII adenylyl cyclase, VC1, xlAC

ECTree

     4 Lyases
         4.6 Phosphorus-oxygen lyases
             4.6.1 Phosphorus-oxygen lyases (only sub-subclass identified to date)
                4.6.1.1 adenylate cyclase

Engineering

Engineering on EC 4.6.1.1 - adenylate cyclase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D650A
mutation in cyaB1-595-859 catalytical domain, no activity
L259V
affinity for cAMP is at least 11fold higher than for cGMP
more |
replacement of the entire beta1-beta3 region, Ile250 to Ile283, of the cyaB1 GAF B subdomain with Asn411 to Tyr443 of GAF B from rat phosphodiesterase 2, is stimulated by cGMP 10.5fold similar to wild-type cyaB1, whereas activation by cAMP is eliminated, thus switched specificity of the cyaB1 tandem GAF domain from cAMP to cGMP. Swapping of the anterior part, Ile250 to Gly267, in cyaB1 GAF B with Asn411 to Asn426 of rat phosphodiesterase 2, which is stimulated by neither cAMP nor cGMP up to 10 mM. Swapping the C-terminal W270 to I283 section of cyaB1 for Val429 to Tyr443 from rat phosphodiesterase 2 yields a protein that is highly stimulated by both cAMP and cGMP, i.e. purine specificity is lost. Elongation of the swapped stretch of amino acids towards the N-terminal, e.g. when Thr258/Leu259 are included in the domain swapping and replaced by Ser and Val cNMP, specificity is inverted, i.e. the efficacy of cAMP is almost lost, whereas cGMP stimulates cyaB1 AC potently
N728A
mutation in cyaB1-595-859 catalytical domain, no activity
T258S
preference for cGMP over cAMP is 35fold, affinity for both cyclic nucleotides is enhanced
T258S/L259V
response to cGMP is highly diminished
K533E
no activity
K533E/I603R/D605C
mutant lose adenylyl cyclase activity but obtains significant guanylyl cyclase activity
H351A
-
mutant with no enzyme activity
H351F
-
mutant with 40fold decreased enzyme activity
H351N
-
mutant with 34fold decreased enzyme activity
K372A
-
mutant with 30fold reduced catalytic rate constant and 3fold increased Km value for ATP
A225C
a CyaA 1-373 mutant
A94C
a CyaA 1-373 mutant
N347A
-
the mutant shows an enzymatic activity that is reduced by about half as well as 5fold reduced affinity for calmodulin
Q260A/R262A
a CyaA 1-373 mutant, the mutant shows reduced calmodulin-dependent activation of CyaA compared to the wild-type CyaA
Q260C
the mutant shows about 1000fold reduced potency to be activated by calmodulin compared to the wild-type CyaA
R338A/D360A
-
the mutant shows no affected catalytic efficiency but 6fold reduced affinity for calmodulin
R338A/N347A/D360A
-
the mutant shows 15% of wild type turnover and exhibits 200fold reduced affinity for calmodulin
V1027A/L1031A
is not catalytically active under basal, Galphas- or forskolin-stimulated conditions
E497K/C566D
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
D414B
-
mutant does not show increased cAMP levels
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
G463D
-
mutant does not show increased cAMP levels
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
R188H
-
mutant does not show increased cAMP levels
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
F1078S
-
isoform VI, mutation within the GALPHAS binding pocket
N1090D
-
isoform V, mutation within the GALPHAS binding pocket
N955A
-
mutation prevents glycosylation
N964A
-
mutation prevents glycosylation
Y1082L
-
mutation in AC9 confers both binding and activation by forskolin
D147A
Rv1647 mutant, mutation of first metal-binding residue, barely active
D241C
Rv1647 mutant, mutation of C1-like substrate specifying residues, barely active, does not lead to a gain in guanylyl cyclase activity
D256A
Rv1625c mutant, mutation of the metal-binding residue, leads to significant decrease in adenylyl cyclase activity, can not reconstitute activity with C1 or C2 domains of the mammalian adenylyl cyclase isoforms or with Rv1647
D256A/D300A
mixture of artificial C2-like mutants of Rv1625c, reconstitutes an active enzyme
D300A
Rv1625c mutant, mutation of the metal-binding residue, leads to significant decrease in adenylyl cyclase activity, can heterodimerize and reconstitute activity with the Paramaecium guanylyl cyclase C1-like domain, can not reconstitute activity with C1 or C2 domains of the mammalian adenylyl cyclase isoforms or with Rv1647
D365A
Rv1625c mutant, mutation of the substrate specifying residue, leads to significant decrease in adenylyl cyclase activity, can not reconstitute activity with C1 or C2 domains of the mammalian adenylyl cyclase isoforms or with Rv1647
D365C
E136A
shift of the pH optimum by about 0.5 unit to acidic pH
E136R
shift of the pH optimum by about 0.5 unit to acidic pH
E195A
mutation with partially relieved inhibition and 4fold increased enzyme activity at pH 8.0, pH optimum shifted from 5.8 to 6.5
F363R
H103A
pH regulation is barely affected, not involved in pH-regulation
H140A
pH regulation is barely affected, not involved in pH-regulation, shift of the pH optimum by about 0.5 unit to acidic pH
H140R
inhibition is relaxed slightly, with a shift of the pH optimum toward more basic values
H192A
mutant with wild-type phenotype at pH 8.0, the slope of activation is shifted by 0.5 pH units towards the acidic pH. 10fold higher enzyme activity at pH 8.0 than the wild type
H58A
pH regulation is barely affected, not involved in pH-regulation
K187E
Rv1647 mutant, mutation of C1-like substrate specifying residues, barely active, does not lead to a gain in guanylyl cyclase activity
K187E/D241C
Rv1647 mutant, mixture of artificial C1-like mutants, reconstitutes high adenylyl cyclase activity, does not lead to a gain in guanylyl cyclase activity
K296A
Rv1625c mutant, mutation of the substrate specifying residue, leads to significant decrease in adenylyl cyclase activity, can not reconstitute activity with C1 or C2 domains of the mammalian adenylyl cyclase isoforms or with Rv1647
K296A/D365A/R376A
mixture of artificial C1-like mutants of Rv1625c, reconstitutes an active enzyme
K296E
K296E/D365C
K296E/F363R/D365C
R132A
shift of the pH optimum by about 0.5 unit to acidic pH
R132E
results in a biphasic pH activity curve with a minimum at pH 6.5 and higher activity at basic pH values
R18A
88% of wild-type activity, in the presence of 2 mM Mn2+
R18A/R19G
67% of wild-type activity, in the presence of 2 mM Mn2+
R19G
78% of wild-type activity, in the presence of 2 mM Mn2+
R27A
78% of wild-type activity, in the presence of 2 mM Mn2+
R309A
mutation renders holoenzyme active and unregulated
R31G
118% of wild-type activity, in the presence of 2 mM Mn2+
R376A
Rv1625c mutant, mutation of the transition state stabilizing residue, leads to significant decrease in adenylyl cyclase activity
R43A
61% of wild-type activity, in the presence of 2 mM Mn2+
R43A/R44G
R43K
77% of wild-type activity, in the presence of 2 mM Mn2+
R43K/R44K
39% of wild-type activity, in the presence of 2 mM Mn2+
R44G
41% of wild-type activity, in the presence of 2 mM Mn2+
R44K
116% of wild-type activity, in the presence of 2 mM Mn2+
R46A
85% of wild-type activity, in the presence of 2 mM Mn2+
R46K
135% of wild-type activity, in the presence of 2 mM Mn2+
R4G
77% of wild-type activity, in the presence of 2 mM Mn2+
D147A
-
Rv1647 mutant, mutation of first metal-binding residue, barely active
-
D241C
-
Rv1647 mutant, mutation of C1-like substrate specifying residues, barely active, does not lead to a gain in guanylyl cyclase activity
-
D256A
-
Rv1625c mutant, mutation of the metal-binding residue, leads to significant decrease in adenylyl cyclase activity, can not reconstitute activity with C1 or C2 domains of the mammalian adenylyl cyclase isoforms or with Rv1647
-
D365A
-
Rv1625c mutant, mutation of the substrate specifying residue, leads to significant decrease in adenylyl cyclase activity, can not reconstitute activity with C1 or C2 domains of the mammalian adenylyl cyclase isoforms or with Rv1647
-
D365C
-
Rv1625c mutant, does not result in a gain of guanylyl cyclase activity, but leads to severely compromised adenylyl cyclase activity
-
E136A
-
shift of the pH optimum by about 0.5 unit to acidic pH
-
E195A
-
mutation with partially relieved inhibition and 4fold increased enzyme activity at pH 8.0, pH optimum shifted from 5.8 to 6.5
-
F363R
-
mutant with poor adenylate cyclase acitivity
-
H140A
-
pH regulation is barely affected, not involved in pH-regulation, shift of the pH optimum by about 0.5 unit to acidic pH
-
H140R
-
inhibition is relaxed slightly, with a shift of the pH optimum toward more basic values
-
H192A
-
mutant with wild-type phenotype at pH 8.0, the slope of activation is shifted by 0.5 pH units towards the acidic pH. 10fold higher enzyme activity at pH 8.0 than the wild type
-
K187E
-
Rv1647 mutant, mutation of C1-like substrate specifying residues, barely active, does not lead to a gain in guanylyl cyclase activity
-
K187E/D241C
-
Rv1647 mutant, mixture of artificial C1-like mutants, reconstitutes high adenylyl cyclase activity, does not lead to a gain in guanylyl cyclase activity
-
K296E
K296E/D365C
-
double mutant with severely compromised enzyme activity
-
K296E/F363R/D365C
-
triple mutant with severely compromised enzyme activity
-
Q57K/N106D
-
Rv0386 mutant, abolishes activity
-
R132A
-
shift of the pH optimum by about 0.5 unit to acidic pH
-
R18A
-
88% of wild-type activity, in the presence of 2 mM Mn2+
-
R19G
-
78% of wild-type activity, in the presence of 2 mM Mn2+
-
R27A
-
78% of wild-type activity, in the presence of 2 mM Mn2+
-
R309A
-
mutation renders holoenzyme active and unregulated
-
R43A/R44G
-
1.3% of wild-type activity, in the presence of 2 mM Mn2+
-
R4G
-
77% of wild-type activity, in the presence of 2 mM Mn2+
-
D200N
mutant shows no activation on light exposure
F197S
mutant shows no activation on light exposure
L111A/L115A
mutant shows no activation on light exposure
N256A
mutant shows no activation on light exposure
Y125A
mutant shows no activation on light exposure
D200N
-
mutant shows no activation on light exposure
-
F197S
-
mutant shows no activation on light exposure
-
L111A/L115A
-
mutant shows no activation on light exposure
-
N256A
-
mutant shows no activation on light exposure
-
Y125A
-
mutant shows no activation on light exposure
-
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
E189R
-
the mutant shows increased activity compared to the wild type enzyme
-
E377G
-
the mutant shows increased activity compared to the wild type enzyme
-
F399I
-
the mutant shows increased activity compared to the wild type enzyme
-
L326P
-
the mutant shows increased activity compared to the wild type enzyme
-
R318W
-
the mutant shows increased activity compared to the wild type enzyme
-
K274A
-
the mutation significantly reduces adenylate cyclase activity
-
T351A
-
the mutation significantly reduces adenylate cyclase activity
-
D396A
-
almost no activity
D396A/D440A
-
no activity
D396A/D440N
-
no activity
D396N
-
almost no activity
D396N/D440A
-
no activity
D396N/D440N
-
no activity
D425A
-
catalytically inactive mutant of isoform AC6, the expression of the mutant is associated with marked reduction in cAMP production
D440A
-
almost no activity
D440N
-
almost no activity
K1876M
-
large decrease in cAMP signalling
C83A
Q7CH76
the mutation results in moderate to sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+
D143A
-
does not crystallize
D55K
Q7CH76
the mutant shows increased Km for Mg2+ compared to the wild type enzyme
E10Q
Q7CH76
the mutation results in about 8fold reduction in activity with 20 mM Mg2+ and in a 5fold increase in activity in the presence of 10 mM Mn2+
E12Q
Q7CH76
the mutation results in sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+
E136A
E84A
-
gives crystals that are unsuitable owing to poor crystal growth or poor diffraction
F5A
Q7CH76
the mutant shows increased Km for Mg2+ compared to the wild type enzyme
K14A
Q7CH76
the mutation results in sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+
K76A
Q7CH76
the mutation results in sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+
L72A
Q7CH76
the mutant shows about 2fold increased Km for Mg2+ compared to the wild type enzyme
M140A
Q7CH76
the mutation results in moderate to sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+
R113A
Q7CH76
the mutation results in sharp decreases in activity in the presence of 10 mM Mn2+ and no activity with Mg2+
R63A
Q7CH76
the mutation results in sharp decreases in activity in the presence of 10 mM Mn2+ or 20 mM Mg2+
additional information