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Ligand Calmodulin

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.60

S-adenosyl-L-methionine + calmodulin L-lysine = S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine

734999, 735078, 735212, 441314, 441316, 734893, 757976

-

2.3.2.B11

n ATP + calmodulin + n ubiquitin = ?

648927, 648928, 648937, 648930, 648934

-

Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Substrate (8 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.4.11

calmodulin + thioredoxin disulfide + H2O = ?

725066

-

2.1.1.60

S-adenosyl-L-methionine + calmodulin L-lysine = S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine

441320, 734999, 735078, 735212, 441319, 441314, 441315, 441313, 441317, 441316, 734893, 757976

-

2.1.1.60

S-adenosyl-L-methionine + calmodulin L-lysine-115 = S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine-115

720536

-

2.1.1.60

2 entries

2.1.1.77

S-adenosyl-L-methionine + calmodulin = S-adenosyl-L-homocysteine + ?

485611, 485617

-

2.3.2.B11

n ATP + calmodulin + n ubiquitin = ?

648927, 648928, 648937, 648930, 648934

-

2.7.11.1

ATP + calmodulin = ADP + phosphorylated calmodulin

722389

-

2.7.11.13

ATP + calmodulin = ADP + phosphorylated calmodulin

662054

-

3.4.21.4

calmodulin + H2O = ?

699817

-

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.1.61

methylated calmodulin + H2O = calmodulin + methanol

-

-

Enzyme Cofactor/Cosubstrate (103 results)

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Show Cofactor (103 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.39

-

685095, 440236, 696643, 440205, 440215, 696110, 697713, 698461, 440202, 440203, 440230, 675257, 698484, 698852, 700433, 701000, 701194

-

1.14.13.39

15fold stimulation of cytochrome c reduction of wild-type and mutants C415A and C415H

440234

-

1.14.13.39

30 nM

697412

-

1.14.13.39

activation, potent stimulator of purified, not crude, enzyme preparation

440191

-

1.14.13.39

Ca2+/calmodulin is required for superoxide formation in absence of tetrahydropterin

440218

-

1.14.13.39

Ca2+/calmodulin stimulates cytochrome c reductase activity

440234, 440214

-

1.14.13.39

dependent on

685094, 687697

-

1.14.13.39

dependent on, endothelial enzyme

440216, 440235

-

1.14.13.39

enzyme-bound is required, supplemented stimulates

440240

-

1.14.13.39

enzyme-bound, the binding sequence links the two enzyme domains

671709

-

1.14.13.39

in the absence of calmodulin, the wild type enzyme activity is less than 15% of the maximum calmodulin-dependent values

698884

-

1.14.13.39

maximum calmodulin-dependent activity is measured at 1.5 mM CaCl2, phosphorylation within an autoinhibitory domain in endothelial nitric oxide synthase reduces the Ca2+ concentrations required for calmodulin to bind and activate the enzyme

696280

-

1.14.13.39

murine macrophage enzyme is Ca2+/calmodulin independent

440200, 440201

-

1.14.13.39

NADPH-diaphorase activity of the enzyme is Ca2+/calmodulin independent

440196

-

1.14.13.39

no stimulation with exogenous calmodulin, inducible isoform from liver

440237

-

1.14.13.39

rat neutrophil enzyme is calmodulin independent

440208, 440213

-

1.14.13.39

required

440221, 440223, 440225, 440228, 440227, 440231, 440224

-

1.14.13.39

the enzyme bears a Ca2+/calmodulin dependent FAD and FMN containing reductase domain which transfers electrons from NADPH to a variety of acceptors

440199

-

2.7.1.127

1.5fold activation by Ca2+/calmodulin

640749

-

2.7.1.127

17fold stimulation by Ca2+/calmodulin at saturating calmodulin and 0.01 mM free Ca2+

640733

-

2.7.1.127

3-6fold stimulation by Ca2+/calmodulin

640737

-

2.7.1.127

6-7fold stimulation by Ca2+/calmodulin

640741

-

2.7.1.127

activation by Ca2+/calmodulin

640744, 640745, 640752, 640733, 640734, 640751, 640755, 640756, 640758, 640735, 640736, 640737, 640738, 640739, 640749, 640753, 640757, 640759, 640761, 640742, 640743, 640740, 640741, 640750, 640754, 640747

-

2.7.1.127

Ca2+/calmodulin-dependent, 10fold stimulation, reversed upon chelation of Ca2+ by EGTA

640734

-

2.7.1.127

effects of Ca2+/calmodulin on enzyme activity

640743

-

2.7.1.127

isoform C is strongly activated by Ca2+/calmodulin in a substrate concentration-dependent manner

640761

-

2.7.1.127

isoforms A and B are differentially regulated by Ca2+/calmodulin, isoform A: 2.5fold stimulation, isoform B: 20fold stimulation

640759

-

2.7.1.127

maximal at 50 nM calmodulin, reversed by EGTA, interaction between the Ca2+-calmodulin complex and enzyme

640750

-

2.7.1.127

maximally 5fold stimulation by 0.01 mM Ca2+/calmodulin, reversible

640739

-

2.7.1.127

mechanism of activation

640734, 640741

-

2.7.1.127

mediates activation by Ca2+

640754

-

2.7.1.127

phosphorylation of isoenzyme B has no effect on the sensitivity to the Ca2+/calmodulin complex

640758

-

2.7.1.127

phosphorylation of Thr-311 of isoenzyme A by CaM kinase II results in a 25fold increase in sensitivity to the Ca2+/calmodulin complex, maximally 2-2.5fold stimulation by the Ca2+/calmodulin complex

640756

-

2.7.1.127

the 3 isoenzymes A, B and C can be distinguished by their sensitivity to Ca2+/calmodulin

640755

-

2.7.1.127

The binding domain is present in all IP3K isoforms

687650

-

2.7.1.127

The binding domain is present in all IP3K isoforms, involved in inhibitor binding.

687650

-

2.7.1.127

up to 30fold stimulation by Ca2+/calmodulin

640740

-

1.14.13.39

18 entries

2.7.1.127

19 entries

2.7.11.1

-

738584

-

2.7.11.17

a ubiquitous Ca2+-sensing protein called calmodulin (CaM), which contains four EF-hand Ca2+-binding motifs, undergoes conformational change upon Ca2+-binding, and the resulting Ca2+/CaM complex regulates a number of effector proteins including Ca2+/CaM-dependent protein kinases (Ca2+/CaMKs)

739960

-

2.7.11.17

after autophosphorylation, the enzyme is active in the absence of Ca2+/calmodulin and even in the presence of EGTA

640689

-

2.7.11.17

binding required for activity

490797, 490800, 490796, 490801

-

2.7.11.17

calcium-calmodulin dependent signalling via Ca2+ leads to activation of CAMKIV autoinhibition

740003

-

2.7.11.17

CaV2.1(1848–1964) contains an IQ-like motif as part of a bipartite regulatory site that is important for CaM-induced facilitation and inactivation of CaV2.1 channels. IQ-like motifs bind CaM. CaM is not required for CaMKII binding to Ca2+channels

740718

-

2.7.11.17

dependent on

691978, 694382, 693760, 693764, 694154, 694372, 694396, 691539, 691719, 693128, 693725, 694887, 690363, 691668, 692227, 690372, 691560, 691673, 690822, 693767, 694403, 690926, 691837, 692345, 692226, 694370, 691612

-

2.7.11.17

dependent on, 2 mM CaCl2 plus 0.001 mM calmodulin induce 69.2% activation of CaMKIV activity

693204

-

2.7.11.17

each kinase subunit is activated separately by direct binding of Ca2+/CaM, which can also induce intra-holoenzyme inter-subunit Thr286 autophosphorylation

740722

-

2.7.11.17

not

490758

-

2.7.11.17

required

740328

-

2.7.11.17

required, calcium-dependent CaM binding overrides the effects of autophosphorylation and activates the protein

741158

-

2.7.11.17

requirement

640685, 640686, 640687, 640689, 490757, 490759

-

2.7.11.17

substrate activation, but not autophosphorylation is dependent on calmodulin

693768

-

2.7.11.18

-

640652, 640655, 661664, 708823, 709148, 709692, 662502, 662503, 662504, 663446, 710379, 660858, 640659, 640660

-

2.7.11.18

1:1 stoichiometric complex in the presence of Ca2+

640635, 640645

-

2.7.11.18

aged enzyme loses Ca2+/calmodulin sensitivity by proteolysis

640619

-

2.7.11.18

binding site I at residue 1002-1022, binding site II at residues 26-42, complex formation with Ca2+

660857

-

2.7.11.18

calmodulin in presence of Ca2+ abolishes the inhibition of actin-myosin interaction

640648, 640649, 640650

-

2.7.11.18

dependent on

661665, 661729, 709858, 708142

-

2.7.11.18

lower affinity for Ca2+/caldesmon after phosphorylation by cAMP-dependent protein kinase, Ka: 0.0000006 mM

640627

-

2.7.11.18

not

491266

-

2.7.11.18

only active as ternary complex of calmodulin, Ca2+ and kinase: activation is initiated by binding of Ca2+ to calmodulin

640621

-

2.7.11.18

optimal ratio of enzyme to calmodulin for telokin phosphorylation is 1:4

640651

-

2.7.11.18

requirement

491268, 640620, 640624, 640629, 640633, 640634, 640635, 640639, 640640, 640643, 640644, 640645, 640626, 640630, 640631, 640632, 640638, 640641, 640642, 640618, 640628, 640627, 640619, 640621, 640622, 640623, 640625, 640615, 640637

-

2.7.11.18

trypsin or chymotrypsin digested smooth muscle enzyme is independent of Ca2+/calmodulin

640634, 640635, 640645, 640632

-

2.7.11.19

activation of nonactivated enzyme and alphagammadelta subunit complex

492114

-

2.7.11.19

activation of recombinant gamma subunit at pH 6.8, slightly at pH 8.2

492148

-

2.7.11.19

additional activation

492132, 492148, 492122

-

2.7.11.19

allosteric effector

492101

-

2.7.11.19

Ca2+-dependent binding, identical with the delta subunit

661075

-

2.7.11.19

calmodulin containing enzyme i.e. tightly bound delta subunit

492101, 492110, 492114, 492120

-

2.7.11.19

calmodulin containing enzyme in the absence of Ca2+

492120

-

2.7.11.19

encoded by 3 different genes CALM1-3

661654

-

2.7.11.19

identical with the delta subunit

662844, 663335, 663347

-

2.7.11.19

in the presence of Ca2+ phosphorylase kinase binds a second molecule calmodulin (i.e. delta' subunit) producing additional activation

492110

-

2.7.11.19

in the presence of Ca2+: 1 mol extrinsic calmodulin per mol alphabetagammadelta rabbit enzyme

492101

-

2.7.11.19

interacts with alpha subunit

492114

-

2.7.11.19

mediates Ca2+-sensitivity of the enzyme, calmodulin is identical with the delta-subunit

650575

-

2.7.11.19

no activation of bovine red skeletal muscle or rabbit cardiac enzymes

492101

-

2.7.11.19

no activation of phosphorylated or proteolytically modified enzyme by delta'-subunit

492122

-

2.7.11.19

no additional activation

492121

-

2.7.11.19

requirement

492101, 492110, 492114, 492120

-

2.7.11.19

the delta subunit

741081

-

2.7.11.19

tightly bound molecule interacts with additional calmodulin in the presence of Ca2+

492120

-

2.7.11.17

13 entries

2.7.11.18

12 entries

2.7.11.19

19 entries

2.7.11.31

requirement, Ca2+/calmodulin dependent kinase, no phosphorylation of substrate observed in absence

644958

-

2.7.11.4

activation

349073

-

3.1.3.16

-

690925, 691077, 691081, 691177, 692085, 657391, 690834

-

3.1.3.16

activation, dependent on Ca2+

134595, 134598, 134632

-

3.1.3.16

isozyme PP2B is dependent on calmodulin

695126

-

3.1.3.16

no stimulation

134682

-

3.1.3.16

requirement, phosphatase 2B, i.e. calcineurin

134599, 134600, 134601

-

3.1.3.16

stimulation of phosphatase PfPP2B

134683

-

3.1.3.16

6 entries

3.1.4.17

-

703570, 711813, 692191

-

3.1.4.52

-

713097

-

4.1.1.15

-

716552, 713972

-

4.1.1.15

a unique feature of plant GAD is the presence of a calmodulin (CaM)-binding domain at its C-terminus. In plants, transient elevation of cytosolic Ca2+ in response to different types of stress is responsible for GAD activation via CaM

747173

-

4.1.1.15

Ca2+/calmodulin-dependent enzyme with calmodulin binding activity

3993

-

4.1.1.15

GAD can be regulated in vivo by Ca2+/calmodulin atpH 5.8. The addition of bovine calmodulin and Ca2+ to the reaction mix causes an activation of GAD activity of 32%

716650

-

4.1.1.15

plus Ca2+, at pH 5.8, activates

3985

-

4.1.1.15

stimulation be Ca2+ plus calmodulin, no stimulation by Ca2+ or calmodulin alone

3987

-

4.6.1.1

-

714051, 713708, 716279, 716341, 716253, 716006, 715586

-

4.6.1.1

activates adenylyl cyclases 1 and 8

709018

-

4.6.1.1

activation

34759, 34761, 34801, 34825, 34788, 34756, 34755, 34757, 34758, 34810, 34811, 34812, 34819

-

4.6.1.1

CyaA binds calmodulin that stimulates about 1000fold its enzymatic activity

709541

-

4.1.1.15

6 entries

4.6.1.1

4 entries

4.6.1.2

activation in presence of Ca2+

34828

-

Activator in Enzyme-catalyzed Reactions (161 results)

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Show Activating Compound (161 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.3

in the presence of above 0.1 mM Ca2+

246395

-

1.11.1.7

enhances ELP activity

699269

-

1.14.13.39

-

660022, 659646

-

1.14.13.39

activates O2 consumption of eNOS

687615

-

1.14.13.39

activates the neuronal NOS by binding and inhibiting the suppression through the C-terminal tail of the enzyme, overview

685120

-

1.14.13.39

Ca2+-calmodulin binds between the reductase and oxygenase domains to activate nitric-oxide synthesis. The enzyme adopts an ensemble of open and closed conformational states and that Ca2+-calmodulin binding induces a dramatic rearrangement of the reductase domain. Calmodulin-specific activation triggers release and rotation of the FMN subdomain to expose the flavin for electron transfer to the heme

745299

-

1.14.13.39

in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation. Binding of NADPH and calmodulin influence interdomain distance relationships as well as reaction chemistry. An important effect of calmodulin binding is to suppress adventitious electron transfer from nNOS to molecular oxygen and thereby preventing accumulation of reactive oxygen species

745293

-

1.14.13.39

required

658767, 658405

-

1.14.13.39

required for catalysis

687291

-

1.14.13.39

substrate 2,6-dichlorophenolindophenol, about 10fold increase in activity in presence of calmodulin

657741

-

1.14.13.39

8 entries

1.14.14.18

calcium-dependent binding to enzyme, 3fold increase in catalytic activity

659364

-

1.7.1.1

activates

392895

-

2.1.1.60

-

441318

-

2.4.1.121

stimulates

488523

-

2.7.1.11

binding of one calmodulin per monomer promotes the dimerization of the enzyme although maintaining its full catalytic activity, 30 nM calmodulin activates 6-phosphofructo-1-kinase in the presence of its inhibitors citrate and lactate

702446

-

2.7.1.11

clotrimazole-inhibited enzyme can be activated by calmodulin

671923

-

2.7.1.127

2-3fold activation of isozyme IP33K-A and 7-8fold of isozyme IP33K-B, in a Ca2+-dependent manner, the binding site contains amphiphilic alpha-helices with cluster of positively charged and hydrophobic amino acids

661446

-

2.7.1.127

i.e. CaM, regulatory function, in concert with Ca2+

662827

-

2.7.1.127

isozyme IP33K-A: 3-6fold activation in a Ca2+-dependent manner, the binding site contains amphiphilic alpha-helices with cluster of positively charged and hydrophobic amino acids, residues Ser156-Leu189 and Trp165 are required

661446

-

2.7.1.127

the enzyme is activated by Ca2+/calmodulin. The human isozyme IP3-3K A contains a CaM binding domain at residues 158-183, binding structure and identification all of the key residues involved in the interaction, overview

737647

-

2.7.1.127

the enzyme is activated by Ca2+/calmodulin. The isozyme contains a CaM binding domain

737402

-

2.7.1.127

the enzyme is highly activated by Ca2+/calmodulin, ten to twentyfold increase in activity in human platelets. The isozyme contains a CaM binding domain

737402

-

2.7.1.127

the enzyme is highly activated by Ca2+/calmodulin, two or threefold in rat brain. The isozyme contains a CaM binding domain

737402

-

2.7.1.127

the enzyme is highly activated by Ca2+/calmodulin. The isozyme contains a CaM binding domain

737402

-

2.7.1.127

up to 20fold activation in a Ca2+-dependent manner, the binding site contains amphiphilic alpha-helices with cluster of positively charged and hydrophobic amino acids

661446

-

2.7.1.11

2 entries

2.7.1.127

9 entries

2.7.1.138

binding site is located at residues 422-435, which form a amphipathic helical wheel, motif 1-8-14, calmodulin is involved in the Ca2+-dependent activation of ceramide kinase as a calcium-sensor

662431

-

2.7.1.21

stimulates the enzyme by 13.8%, might modify the activity, enzyme contains a calmodulin binding domain, Ca2+ is required for binding, compounds W7 and W13 prevent stimulation, overview

660905

-

2.7.1.23

-

660240

-

2.7.1.23

a 410000 Da Ca2+-calmodulin-independent isoform and a 63000 Da Ca2+-calmodulin-dependent isoform

641203

-

2.7.1.23

activates

682340

-

2.7.1.23

Ca2+-calmodulin-dependent enzyme. Half-saturating concentration of calmodulin is 19 ng

641200

-

2.7.1.23

Ca2+/calmodulin regulates NAD kinase activity. Ca2+/calmodulin has no detectable effect on recombinant human NAD kinase

691390

-

2.7.1.23

calmodulin-dependent enzyme is stimulated 3.5fold by addition of calmodulin in presence of Ca2+

641201

-

2.7.1.23

calmodulin-dependent isoform, full activation in presence of Ca2+

660240

-

2.7.1.23

CaM-2 isoform is a significantly more efficient activator of NAD kinase compared with the CaM-4 and CaM-6 isoforma

641190

-

2.7.1.23

five forms of NAD+ kinase: 1. a solvent Ca2+ sensitive form, 2. and 3. two Ca2+-calmodulin independent forms, one solvent and one membranal, 4. and 5. two Ca2+-calmodulin dependent forms, one solvent and one membranal. In dry seeds the membranal-Ca2+-calmodulin-dependent form represents 100% of the total pelletable activity

641197

-

2.7.1.23

in dry seeds the membranal-Ca2+-calmodulin-dependent form represents 30% of the total pelletable activity

641197

-

2.7.1.23

independent on calmodulin

641192

-

2.7.1.23

presence of bovine calmodulin, 100% activity, Nicotiana tabacum calmodulin 1, 207% activity, Nicotiana tabacum calmodulin 3, 235% activity, Nicotiana tabacum calmodulin 1, 9% activity

663065

-

2.7.1.23

the Ca2+-calmodulin-dependent NAD+ kinase isoforms, amongst which is the isoform bound to mitochondrial membranes play an important role at the end of sensu stricto germination and during the following growth of Avena sativa

641198

-

2.7.1.23

the enzyme can be activated by soybean CaM-1, but not by the divergent soybean CaM isoform CaM-4

641196

-

2.7.1.23

two peaks of calmodulin-dependent NAD+ kinase activity occur at times when the cells are not actively dividing: the first one, a few hours after medium inoculation and the second one, at the end of the exponential growth phase

641199

-

2.7.1.23

15 entries

2.7.1.91

Ca2+-dependent binding of recombinant wild-type and mutant enzymes

661750

-

2.7.10.1

ligand-binding induced dimerization enables transautophosphorylation of ErbB1 which results in enhanced intracellular Ca2+ concentration activating calmodulin which reverses autoinhibition by net charge changes in the juxtamembranes

662557

-

2.7.11.17

-

702957, 664750, 666139, 674557, 664472, 672850, 675034, 760732

-

2.7.11.17

absolutely dependent on

664928

-

2.7.11.17

activates

741420

-

2.7.11.17

CPK-1 contains a calmodulin-like regulatory apparatus, structural organization, overview

665533

-

2.7.11.17

dependent on

664278, 664865, 665662, 666130, 666454, 672940, 675065, 676174, 665701, 666119, 675969, 664935, 666401, 666707, 671227, 672941, 675526, 675548, 671266, 666324, 665648, 664641

-

2.7.11.17

dependent on, activates

666459, 666110

-

2.7.11.17

dependent on, activates at 3-1000 nM

665759

-

2.7.11.17

dependent on, activates the nonphosphorylated CaMKIV, residues F320, N321, D322, D323, N318, N324, N330, and N336 are involved in binding, the autoinhibitory domain harbors the binding site for Ca2+ and calmodulin

665624

-

2.7.11.17

dependent on, activating activity is abolished by calmodulin oxidation, phosphorylation of substrate by CaMKII and CaMKII autophosphorylation at Thr286, calmodulin binding to the enzyme inhibits autophosphorylation at Thr305/Thr306, which leads to enzyme inhibition, overview

671799

-

2.7.11.17

dependent on, Ca2+/calmodulin activate CaMKII prior to autophosphorylation which renders the enzyme independent of Ca2+/calmodulin

664537

-

2.7.11.17

dependent on, Ca2+/calmodulin-dependent, reversible enzyme clustering by self-association of the recombinant CaMKII, which might be hindered by autophosphorylation at Thr286, mechanism, overview

666132

-

2.7.11.17

dependent on, intracellular calcium receptor

664506

-

2.7.11.17

dependent on, the Ca2+/calmodulin-binding domain overlaps with the autoinhibition domain

665484

-

2.7.11.17

dependent on, transient, tightly regulated Ca2+/calmodulin-dependent activation requiring phosphorylation at Thr200 by CaMK kinase, the Ca2+/calmodulin binding-autoinhibitory domain is required for interaction with protein phosphatase PP2A, binding of Ca2+/CaM and PP2A is exclusive, overview

665541

-

2.7.11.17

determination of the calmodulin binding regulatory domain

663862

-

2.7.11.17

kinase activity is dependent on

666114

-

2.7.11.17

required

673266, 676849

-

2.7.11.17

the binding site comprises residues 913-932 with a basic amphiphilic alpha-helix structure, maximal binding at 105 nM, three different isoforms of calmodulin, CaM1, CaM3, and CaM13, differentially regulate CaMK1, overview, the unphosphorylated CaMK1 is dependent on Ca2+ and calmodulin, while the autophosphorylated enzyme is not

666623

-

2.7.11.17

the enzyme is activated by calcium-bound calmodulin

761298

-

2.7.11.17

the unphosphorylated CaMK1 is dependent on Ca2+ and calmodulin, while the autophosphorylated enzyme is not

666127

-

2.7.11.18

-

677138, 760963, 761774, 684356

-

2.7.11.18

a calmodulin-sensitive MLCK isozyme

674829

-

2.7.11.18

activates, dependent on

675623

-

2.7.11.18

dependent on

687732, 689353, 740026, 740060, 740266, 740823, 740289, 740887, 741247

-

2.7.11.18

dependent on, antagonizes the binding to actin

684910

-

2.7.11.18

dependent on, antagonizes the binding to actin, residues 26-41 of MLCK act as a CaM-binding region that regulates the binding of MLCK to actin, Ca/CaM is also binds at the Ala796-Ser815 sequence to regulate the kinase activity MLCK

684910

-

2.7.11.18

required

688628, 688705, 740727, 740131

-

2.7.11.18

the enzyme is dependent on Ca2+ and calmodulin

684333

-

2.7.11.19

-

762340, 762341

-

2.7.11.19

influences the conformational substates of the subunits, overview

677024

-

2.7.11.19

required

740074

-

2.7.11.20

-

664502, 760307, 760308, 760309, 760579, 760810, 761699, 760466, 762016

-

2.7.11.20

a central mediator of Ca2+-dependent signaling, the enzyme is dependent on calmodulin

739836

-

2.7.11.20

absolutely necessary for efficient enzyme activity

761472

-

2.7.11.20

Ca2+/calmodulin stimulates the autophosphorylation of elongation factor 2 kinase on Thr348 and Ser500 to regulate its activity and calcium dependence. At a calmodulin concentration of 0.002 mM, the enzyme exhibits significant activity

721662

-

2.7.11.20

calcium-calmodulin-dependent enzyme

684831

-

2.7.11.20

completely dependent on

665496

-

2.7.11.20

dependent on

666341, 665496, 740015

-

2.7.11.20

required

685402, 687926, 739828, 740281, 741080, 740752

-

2.7.11.20

required, enzyme eEF2K interacts with calmodulin (CaM) through a binding site which lies almost immediately N terminal to its catalytic domain. Comparison of human and murine CaM-binding sites, overview. Hydroxylation of Pro98 impairs binding of eEF2K to calmodulin and its activation by calmodulin

740996

-

2.7.11.20

strong activation, activation in response to exercise in skeletal muscle

666159

-

2.7.11.20

structural basis for the recognition of calmodulin by eukaryotic elongation factor 2 kinase, NMR spectrometric analysis, overview. The enzyme binds Ca2+-loaded CaM with high affinity largely through the CaM C lobe, but C-lobe-mediated interactions occur in a Ca2+-independent fashion. the lobe lacks bound calcium ions even under high calcium conditions. Conserved eEF-2K residue W85 anchors it to CaM by inserting into a deep hydrophobic cavity within the CaM C lobe. Mutation of residue W85 to S85 substantially weakens interactions between full-length eEF-2K and CaM in vitro and reduces eEF-2 phosphorylation in cells

741450

-

2.7.11.17

20 entries

2.7.11.18

8 entries

2.7.11.19

3 entries

2.7.11.20

11 entries

2.7.11.22

Ca2+/calmodulin induce the phosphorylation of p35 by Cdk5 after stimulation of the Ca2+-permeable cation channels NMDA receptor and kainate receptor, leading to cleavage of p35 to p25

666117

-

2.7.11.31

activation of AMPK is mediated by a CO2-triggered increase in intracellular Ca2+ concentration and Ca2+/calmodulin-dependent kinase kinase-beta, CaMKK-beta

693356

-

2.7.11.31

AMPK activation by phosphorylation through the Ca2+-calmodulin dependent protein kinase kinase, CaMKK

692170

-

2.7.11.31

2 entries

2.7.11.7

-

685402

-

2.7.2.3

a significant increase (1.8 times) in enzyme activity is observed in the co-presence of calmodulin (0.001 mM) and CaCl2 (0.01 mM). The enzyme activity remains unaltered in the presence of either calcium or calmodulin alone

760650

-

2.7.2.3

the enzyme is activated up to 85% in the presence of 0.001 mM calmodulin

760650

-

2.7.2.4

-

642331

-

2.7.2.4

isoenzyme II

642323

-

2.7.2.3

2 entries

2.7.2.4

2 entries

3.1.1.4

-

653509, 133876

-

3.1.3.16

-

657389, 657391, 656164

-

3.1.3.16

calcineurin is a Ca2+/calmodulin-activated Ser/Thr phosphatase

709957

-

3.1.3.16

calcineurin is a calcium- and calmodulin-dependent enzyme

751565

-

3.1.3.16

calcineurin is dependent on Ca2+/calmodulin

708027, 707924, 708789, 709112

-

3.1.3.16

dependent on

709923

-

3.1.3.16

5 entries

3.1.3.48

0.0025 to 0.005 mM, significant enhancement of activity

665245

-

3.1.4.16

stimulates activity towards 2',3'-cyclic nucleotides and 3',5'-cyclic nucleotides

135206

-

3.1.4.17

differential effect on isozymes, activation only in complex with Ca2+, overview

651468

-

3.1.4.17

isoform PDE1, stimulation of both hydrolysis of cAMP and cGMP

681548

-

3.1.4.17

2 entries

3.1.4.2

activation, source: bovine

95131

-

3.1.4.53

required, Km value 0.000057 mM

677917

-

3.4.22.54

calmodulin binds the calpain 3 non-catalytic domain C2L and promotes enzyme activation

732188

-

3.4.24.15

interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulation. Overexpression of calmodulin in HEK293 cells is sufficient to greatly increase the A23187-stimulated secretion of EP24.15, which can be inhibited by the calmodulin inhibitor calmidazolium

708478

-

3.5.4.6

Ca2+-calmodulin activates erythrocyte AMPD in conditions of disturbed calcium homeostasis during sickle cell disease

697025

-

3.6.1.42

5fold increase of activity at 0.001 mM

758117

-

3.9.1.3

115% activity at 5 mM Ca2+ plus 0.01 mM calmodulin

735627

-

4.1.1.15

24fold activation of wild-type in presence of both Ca2+ and calmodulin. For mutant lacking 19 amino acids at N-terminus, 12.9fold activation. Mutant lacking 9 amino acids at C-terminus, complete loss of activation

678410

-

4.1.1.15

42% activation, up to 200% activation in presence of both Ca2+ and calmodulin

665444

-

4.1.1.15

activates Gad1 in a unique way by relieving two C-terminal autoinhibition domains of adjacent active sites, forming a 393 kDa Gad-Ca2+/calmodulin complex with a 1:3 stoichiometry

705157

-

4.1.1.15

at a separate concentration of Ca2+ and calmodulin of 0.2 mM and 150 nM, the rice bran GAD is significantly enhanced 3fold. Addition of exogenous EGTA or TFP efficiently inhibited the stimulatory effect of Ca2+/CaM complex

705392

-

4.1.1.15

4 entries

4.4.1.5

7.9fold increase of activity in the presence of Ca2+ and Mg2+

650298

-

4.6.1.1

-

682285, 679129, 651177, 682024, 653453

-

4.6.1.1

a second isoform- and regulator-specific contact site in C2 is necessary to render enzyme activity susceptible to calmodulin modulation. In addition to the PFAHL-motif in C1b of ACII, calmodulin requires not only the Ca2+-independent AC28-region in C1b but also a Ca2+-dependent domain in C2a of ACI with the VLG-loop to stimulate this adenylyl cyclase isoform

678088

-

4.6.1.1

AC1 activity is regulated by both Ca2+/calmodulin and G proteins

693761

-

4.6.1.1

activates

693736

-

4.6.1.1

activates isozyme AC1

693760

-

4.6.1.1

activates isozyme AC8

693760

-

4.6.1.1

activates, the N-terminal portion of CaM binds to the beta-hairpin region in the CA domain of CyaA, interaction mode, structure analysis of the calmodulin-CyaA complex and interface, and mechanism of catalytic activation, detailed overview. The N-terminus of CaM is linked to the C-terminus of CaM by a flexible linker with a defined degree of freedom. The potency of CaM D50C mutant to activate CyaA is enhanced about 10fold, mutants T26C or T41C

693119

-

4.6.1.1

Ca2+ stimulates transmembrane isozyme AC8 via calmodulin

694269

-

4.6.1.1

Ca2+/calmodulin enhance cAMP production through AC9

682112

-

4.6.1.1

Ca2+/calmodulin-stimulated isozyme AC1

691175

-

4.6.1.1

Ca2+/calmodulin-stimulated isozyme AC8

691175

-

4.6.1.1

calmodulin activation of isoform Adcy1 can be regulated by selctive oxidation of the C-terminal Met residues in calmodulin, and by two N-terminal Met residues, M36 and M51. CaM with all Met residues oxidized is unable to activate the enzyme

747040

-

4.6.1.1

co-application of 200 nM Ca2+ and calmodulin enhances the rate of cAMP synthesis by a factor of about 2.5

729544

-

4.6.1.1

isozyme AC8 is a pure Ca2+/calmodulin sensor

693761

-

4.6.1.1

maximal activity at 0.001 mM

730048

-

4.6.1.1

no detectable stimulation of enzyme activity

666768

-

4.6.1.1

required for activity

690413

-

4.6.1.1

requirement for dual regulation of the AC by both Gs activation and Ca2+/calmodulin in a time-dependent manner

682285

-

4.6.1.1

stimulates AC1 and AC8 in a Ca2+-dependent manner

681976

-

4.6.1.1

stimulates AC8

682285

-

4.6.1.1

stimulates AC8 in a Ca2+-dependent manner

681976

-

4.6.1.1

stimulates AC8 which shows a dis-inhibitory activation mechanism, Ca2+ stimulates transmembrane isozymes AC1 and AC8 via calmodulin, and inhibits AC5 and AC6 directly

694269

-

4.6.1.1

stimulates the soluble isozyme

693876

-

4.6.1.1

strong activation

652269

-

5.6.1.2

10fold activation of 14S dynein, about 0.01 mM free Ca2+, half-maximal activation at about 0.0001 mM calmodulin

247035

-

5.6.1.2

from porcine brain, 3-to 8fold

247021

-

7.2.2.10

-

697858, 748570, 733404, 735233, 751094, 751523

-

7.2.2.10

0.001 mM calmodulin stimulates the activity of wild type enzyme by about 300%

720136

-

7.2.2.10

177% activity in the presence of 0.002 mg/ml calmodulin

750998

-

7.2.2.10

2fold increase of activity in the presence of 200 nM calmodulin

751525

-

7.2.2.10

activated by calmodulin

695858

-

7.2.2.10

activates

210489

-

7.2.2.10

activates, single-molecule characterization of the dynamics of calmodulin bound to oxidatively modified PMCA, overview

667623

-

7.2.2.10

auto-inhibited Ca2+-ATPase

720644

-

7.2.2.10

calmodulin depletion results in the transition of the Ca2+-pumping ATPase to a low Ca2+-affinity form

210482

-

7.2.2.10

calmodulin stimulates Ca2+ pumping in the plasma-membrane Ca2+-ATPase by binding to an autoinhibitory domain, which then dissociates from the catalytic domain of PMCA to allow full activation of the enzyme. Although the purified PMCA exhibits a significant basal Ca2+-dependent ATPase activity, the addition of calmodulin fluorescently labeled with tetramethylrhodamine (120 nM) at a saturating Ca2+ concentration (0.1 mM) results in significant activation of PMCA. The enzyme is fully activated at 0.025 mM calmodulin.

701104

-

7.2.2.10

enhances the Ca2+ transport

697160

-

7.2.2.10

no stimulation by bovine calmodulin

210497

-

7.2.2.10

Pmr1p is positively controlled by the calmodulin and calcineurin complex in the presence of an elevated Ca2+ level

697976

-

7.2.2.10

shifts the Ca2+-ATPase to the high-affinity form

210473

-

7.2.2.10

slight stimulation

210480

-

7.2.2.10

stimulates

210483

-

7.2.2.10

strongly activated by calmodulin

700250

-

7.2.2.10

the amino acid sequence of the calmodulin binding site is L1086RRGQILWFRGLNRIQTQIKVVKAFHSS1113, i.e. peptide 28, determination of essential residues for binding, overview, complex structure modelling, calmodulin binding mechanism, overview

667650

-

7.2.2.10

the fully auto-inhibited enzyme has a very low basal Ca2+-ATPase activity which is stimulated more than 5fold by calmodulin

719497

-

4.6.1.1

24 entries

5.6.1.2

2 entries

7.2.2.10

19 entries

Inhibitor in Enzyme-catalyzed Reactions (15 results)

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Show Inhibitors (15 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.26

UBE3B interacts with calmodulin via its N-terminal isoleucine-glutamine motif. Deletion of the motif (amino acids 29-58) results in loss of calmodulin binding and a significant increase in the in vitro ubiquitylation activity of UBE3B. Changes in calcium levels in vitro disrupt the calmodulin-UBE3B interaction

757186

-

2.3.2.B11

UBE3B interacts with calmodulin via its N-terminal isoleucine-glutamine motif. Deletion of the motif (amino acids 29-58) results in loss of calmodulin binding and a significant increase in the in vitro ubiquitylation activity of UBE3B. Changes in calcium levels in vitro disrupt the calmodulin-UBE3B interaction

757186

-

2.7.11.14

the high affinity calmodulin binding site is localized within a stretch of amino acid residues V150-K175 in the N-terminal regulatory region of rhodopsin kinase. The inhibitory effect of calmodulin and recoverin on rhodopsin kinase activity is synergetic

725081

-

2.7.11.14

very poor inhibitor

640728

-

2.7.11.15

-

672408

-

2.7.11.15

inhibits GRK2

661455

-

2.7.11.16

-

672408

-

2.7.11.16

inhibits GRK5

661455

-

2.7.11.16

inhibits the phosphorylation of rhodopsin by GRK5

685121

-

2.7.11.16

reaction of isoenzyme GRK4alpha with rhodopsin, IC50: 80 nM

491135

-

2.7.11.14

2 entries

2.7.11.15

2 entries

2.7.11.16

4 entries

2.7.11.19

inhibits cAMP-dependent protein kinase mediated activation of phosphorylase kinase, kinetics

492137

-

3.1.1.4

GVIA PLA2 is regulated by calmodulin which negatively regulates GVIA PLA2 through direct binding on the residues 694-705 of GVIA-1 PLA2

691654

-

3.1.3.43

-

94882

-

3.6.5.2

binding of calmodulin to GST-immobilized Kir/Gem peptide inhibits GTP binding

644129

-

5.6.1.3

activated calmodulin inhibits KCBP interaction with microtubules thereby abolishing its motor- and microtubules-dependent ATPase activity

656103

-

Metals and Ions (2 results)

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Show Metals Ions (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.16

activates the enzyme with substratees phospho-L-serine and phospho-L-threonine, but not with phospho-L-tyrosine

665243

-

7.2.2.10

PMCA is dependent on Ca2+-calmodulin

698973

-

Enzyme Kinetic Parameters

K_M Value (9 results)

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Show KM Value (9 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.13.39

0.000004

-

-

440214

1.8.4.11

0.197

-

myristoylated enzyme, in 20 mM Tris-HCl, pH 7.5, 1 mM CaCl2, at 37°C

725066

2.1.1.60

0.00001

-

-

441314

2.3.2.B11

0.0009

-

calmodulin from paramecium tetraurelia

648934

2.3.2.B11

0.0013

-

calmodulin from Xenopus laevis

648934

2.3.2.B11

0.0049

-

calmodulin from bovine testis

648934

2.3.2.B11

0.0081

-

pH 8.0, 37°C

648928

2.7.11.18

0.000002

-

30°C, pH 6.8

640623

2.7.11.18

0.000002

-

30°C, pH 7.5

640628

2.3.2.B11

4 entries

2.7.11.18

2 entries

IC₅₀ Value (1 result)

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Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

2.7.11.16

0.00008

-

reaction of isoenzyme GRK4alpha with rhodopsin, IC50: 80 nM

491135

References & Links

Literature References (494)

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Show Reference (494 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

3985

-

Purification and characterization of glutamate decarboxylase from cowpea

1997

Johnson, B.S.; Singh, N.K.; Cherry, J.H.; Locy, R.D.

Phytochemistry

46

39-44

3987

9701597

Characterization of two glutamate decarboxylase cDNA clones from Arabidopsis

1998

Turano, F.J.; Fang, T.K.

Plant Physiol.

117

1411-1421

3993

9638642

Cloning and characterization of a tobacco cDNA encoding calcium/calmodulin-dependent glutamate decarboxylase

1998

Yun, S.J.; Oh, S.H.

Mol. Cells

8

125-129

34755

2901413

Bordetella pertussis adenylate cyclase. Identification of multiple forms of the enzyme by antibodies

1988

Rogel, A.; Farfel, Z.; Goldschmidt, S.; Shiloach, J.; Hanski, E.

J. Biol. Chem.

263

13310-13316

34756

3128270

Adenylate cyclase activity in a higher plant, alfalfa (Medicago sativa)

1988

Carricarte, V.C.; Bianchini, G.M.; Muschietti, J.P.; Tellez-Inon, M.T.; Perticari, A.; Torres, N.; Flawia, M.M.

Biochem. J.

249

807-811

34757

2877986

Bordetella pertussis adenylate cyclase. Purification, characterization, and radioimmunoassay

1986

Ladant, D.; Brezin, C.; Alonso, J.M.; Crenon, I.; Guiso, N.

J. Biol. Chem.

261

16264-16269

34758

2870055

Secreted adenylate cyclase of Bordetella pertussis: calmodulin requirements and partial purification of two forms

1986

Kessin, R.H.; Franke, J.

J. Bacteriol.

166

290-296

34759

2867778

Purification and characterization of a calmodulin-sensitive adenylate cyclase from Bordetella pertussis

1985

Shattuck, R.L.; Oldenburg, D.J.; Storm, D.R.

Biochemistry

24

6356-6362

34761

4041438

Purification of the calmodulin-sensitive adenylate cyclase from bovine cerebral cortex

1985

Yeager, R.E.; Heideman, W.; Rosenberg, G.B.; Storm, D.R.

Biochemistry

24

3776-3783

34788

2034122

Purification of adenylyl cyclase from heart and brain

1991

Pfeuffer, E.; Mollner, S.; Pfeuffer, T.

Methods Enzymol.

195

83-91

34801

2022671

Expression and characterization of calmodulin-activated (type I) adenylylcyclase

1991

Tang, W.J.; Krupinski, J.; Gilman, A.G.

J. Biol. Chem.

266

8595-8603

34810

2882409

Mechanisms of bacterial pathogenicity that involve production of calmodulin-sensitive adenylate cyclases

1987

Masure, H.R.; Shattuck, R.L.; Storm, D.R.

Microbiol. Rev.

51

60-65

34811

2896201

The interaction of Ca2+ with the calmodulin-sensitive adenylate cyclase from Bordetella pertussis

1988

Masure, H.R.; Oldenburg, D.J.; Donovan, M.G.; Shattuck, R.L.; Storm, D.R.

J. Biol. Chem.

263

6933-6940

34812

6253992

Calmodulin activates prokaryotic adenylate cyclase

1980

Wolff, J.; Cook, G.H.; Goldhammer, A.R.; Berkkowitz, S.A.

Proc. Natl. Acad. Sci. USA

77

3841-3844

34819

2897067

The calmodulin-sensitive adenylate cyclase of Bordetella pertussis: cloning and expression in Escherichia coli

1988

Glaser, P.; Landant, D.; Sezer, O.; Pichot, F.; Ullmann, A.; Danchin, A.

Mol. Microbiol.

2

19-30

34825

2034121

Purification and characterization of calmodulin-sensitive adenylyl cyclase from bovine brain

1991

Wang, P.; Storm, D.R.

Methods Enzymol.

195

65-82

34828

2880561

Properties of digitonin-solubilized calmodulin-dependent guanylate cyclase from the plasma membranes of Tetrahymena pyriformis NT-1 cells

1987

Nagao,S.; Nozawa, Y.

Arch. Biochem. Biophys.

252

179-187

94882

16665242

Some properties of pea mitochondrial phospho-pyruvate dehydrogenase-phosphatase

1987

Miernyk, J.A.; Randall, D.D.

Plant Physiol.

83

311-315

95131

7862100

Ca2+ dependent activation of rat uterine glycerylphosphorylcholine diesterase: Presence of a positive modulator protein in uterine secretion

1994

Mitra, Y.; Chowdhury, M.

Mol. Cell. Biochem.

139

101-108

133876

8940072

Expression, purification and kinetic characterization of a recombinant 80-kDa intracellular calcium-independent phospholipase A2

1996

Wolf, M.J.; Gross, R.W.

J. Biol. Chem.

271

30879-30885

134595

-

Phosphoprotein phosphatases

1986

Ballou, L.M.; Fischer, E.H.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed.)

17

311-361

134598

-

Control of calcineurin protein phosphatase activity

1985

Klee, C.B.; Krinks, M.H.; Manalan, A.S.; Draetta, G.F.; Newton, D.L.

Adv. Protein Phosphatases

1

135-146

134599

-

Substrate specificity and metal activation of calcineurin

1985

Pallen, C.J.; Sharma, R.K.; Matsui, H.M.; Wang, J.H.

Adv. Protein Phosphatases

1

147-162

134600

-

Substrate specificity of calmodulin-dependent protein phosphatases

1985

Blumenthal, D.K.; Chan, C.P.; Takio, K.; Gallis, B.; Hansen, R.S.; Krebs, E.G.

Adv. Protein Phosphatases

1

163-174

134601

-

Regulation of calmodulin-dependent phosphoprotein phosphatase (calcineurin) by synergistic action of Ca(II), calmodulin, and Mg(II) or transition metal ions

1985

Simonelli, P.F.; Li, H.G.

Adv. Protein Phosphatases

1

175-190

134632

3035332

Calmodulin-dependent protein phosphatase: isolation of subunits and reconstitution to holoenzyme

1987

Merat, D.L.; Cheung, W.Y.

Methods Enzymol.

139

79-87

134682

10513400

Purification and characterization of a protein phosphatase from winged bean

1999

Ganguly, S.; Singh, M.

Phytochemistry

52

239-246

134683

10340482

Characterization of protein Ser/Thr phosphatases of the malaria parasite, Plasmodium falciparum: inhibition of the parasitic calcineurin by cyclophilin-cyclosporin complex

1999

Dobson, S.; May, T.; Berriman, M.; Del Vecchio, C.; Fairlamb, A.H.; Chakrabarti, D.; Barik, S.

Mol. Biochem. Parasitol.

99

167-181

135206

-

Cyclic nucleotide phosphodiesterase from Lemna paucicostata: effect of calmodulin and theophylline

1994

Gangwani, L.; Khurana, J.P.; Maheshwari, S.C.

Phytochemistry

35

857-861

210473

6218823

The Ca2+-pumping ATPase of plasma membranes. Purification, reconstitution and properties

1982

Carafoli, E.; Zurini, M.

Biochim. Biophys. Acta

683

279-301

210480

2971350

Characteristics of the Ca2+ pump and Ca2+-ATPase in the plasma membrane of rat myometrium

1988

Enyedi, A.; Minami, J.; Caride, A.J.; Penniston, J.T.

Biochem. J.

252

215-220

210482

6451626

The Ca2+-pumping ATPase of heart sarcolemma. Characterization, calmodulin dependence, and partial purification

1981

Caroni P.; Carafoli, E.

J. Biol. Chem.

256

3263-3270

210483

-

Calmodulin stimulated calcium pump ATPase: inhibition by zinc and vanadate

1980

Vicenzi, F.F.; Ashleman, B.T.

Calcium-binding Proteins, Structure and Function (Siegel, F. L. , Carafoli, E. , Kretsinger, R. H. , MacLennan, D. H. , Wasserman, R. H. , eds. )

-

173-179

210489

1310307

The Ca2+ pump of the plasma membrane

1992

Carafoli, E.

J. Biol. Chem.

267

2115-2118

210497

2147112

Characterization of a putative Ca2+-transporting Ca2+-ATPase in the pellicles of Paramecium tetraurelia

1990

Wright, M.V.; van Houten, J.L.

Biochim. Biophys. Acta

1029

241-251

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