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Ligand MgATP2-

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.6.3

6-hydroxymethyl-7,8-dihydropterin + MgATP2- = 6-hydroxymethyl-7,8-dihydropterin diphosphate + MgAMP

672082

-

2.7.7.3

phosphopantetheine + Mg-ATP = dephospho-CoA + diphosphate

674344

-

2.7.7.3

phosphopantetheine + MgATP2- + 4 H+ = dephospho-CoA + diphosphate + Mg2+

674344

-

2.7.7.3

2 entries

4.6.1.1

MgATP2- = ?

34805, 34791

-

Substrate in Enzyme-catalyzed Reactions (21 results)

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Show Substrate (21 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.12.7

luciferin + MgATP2- = AMP + diphosphate

484831, 484853, 484860, 657942, 658103

-

2.7.1.105

MgATP2- + beta-D-fructose 6-phosphate = ?

94936, 660957, 661754, 672208, 640281, 640282, 640286, 640320, 640300, 692346

-

2.7.1.25

MgATP2- + adenosine 5'-phosphosulfate = MgADP- + 3'-phosphoadenosine 5'-phosphosulfate

701464

-

2.7.1.25

MgATP2- + adenylyl sulfate = MgADP- + 3'-phosphoadenylyl sulfate

674838, 675437

-

2.7.1.25

2 entries

2.7.4.22

MgATP2- + UMP = MgADP- + UDP

698858

-

2.7.4.8

GMP + MgATP2- = MgADP- + GDP

642701, 642702, 642694

-

2.7.6.1

Mg-ATP2- + D-ribose 5-phosphate = Mg-AMP2- + 5-phospho-alpha-D-ribose 1-diphosphate

723524

-

2.7.6.3

6-hydroxymethyl-7,8-dihydropterin + MgATP2- = 6-hydroxymethyl-7,8-dihydropterin diphosphate + MgAMP

672082

-

2.7.7.3

phosphopantetheine + Mg-ATP = dephospho-CoA + diphosphate

674344

-

2.7.7.3

phosphopantetheine + MgATP2- + 4 H+ = dephospho-CoA + diphosphate + Mg2+

674344

-

2.7.7.4

MgATP2- + adenylyl sulfate = MgADP- + 3-phosphoadenylyl sulfate

675422

-

2.7.7.4

MgATP2- + sulfate = magnesium diphosphate + adenylyl sulfate

675422

-

2.7.7.4

MgATP2- + sulfate = Mg-diphosphate + adenylyl sulfate

701923

-

2.7.7.3

2 entries

2.7.7.4

3 entries

3.5.2.9

MgATP2- + H2O = ?

209371, 209382, 209383, 209387, 209379, 209373

-

4.6.1.1

MgATP2- = ?

34808, 34778, 34765, 34805, 34791

-

6.2.1.12

4-coumarate + MgATP2- + tetrapolyphosphate = adenosine 5'-pentaphosphate + ?

653536

-

6.2.1.12

4-coumarate + MgATP2- + tripolyphosphate = adenosine 5'-tetraphosphate + ?

653536

-

6.2.1.12

MgATP2- = diadenosine 5',5'',P1,P4-tetraphosphate + ?

653536

-

6.2.1.12

3 entries

6.3.1.8

gamma-L-Glu-L-Cys-Gly + spermidine + MgATP2- = N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + MgADP- + phosphate

965, 649733, 650561

-

6.3.5.2

XMP + Mg-ATP2- = adenyl-XMP + diphosphate + Mg2+

1384, 705173

-

7.4.2.8

MgATP + H2O = MgADP + phosphate

669106

-

Enzyme Cofactor/Cosubstrate (9 results)

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Show Cofactor (9 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.18.6.1

required

714796

-

2.7.1.21

-

661195

-

2.7.11.1

preferred substrate

694132

-

2.7.3.2

-

661095

-

3.1.1.13

-

133832

-

3.1.1.13

activation only for neutral CEase

133849

-

3.1.1.13

increasing activity with addition of cAMP-dependend protein kinase

133829, 133851, 133849

-

3.1.1.13

3 entries

6.3.3.2

enzyme is inhibited by salt, therefore MgATP2- is used as cofactor instead of MgCl2 and NaATP-

652260

-

7.3.2.7

neccasary for the pump function

654492

-

Activator in Enzyme-catalyzed Reactions (14 results)

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Show Activating Compound (14 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.205

a positive effector for the cooperative class I IMPDH IMPDHnm

741229

-

1.1.1.205

allosteric regulation of Pseudomonas aeruginosa IMPDH by MgATP2-. The the ATP-binding sites are located within the two CBS motifs. The compound acts as a positive effector increasing the catalytic activity of the wild-type enzyme, and also of the D199N variant, influencing both the maximal rate and the affinity for IMP, and showing a cooperativity effect for IMP, that is lost in mutant D199N

739794

-

1.1.1.205

has a positive effector of IMPDHpa acting on the maximal rate and on the affinity for IMP. The positive effector binds onto the two CBS modules, with consequences on the global shape

741229

-

1.1.1.205

MgATP2- has a drastic impact on the kinetic properties of class I IMPDHs. It increases the thermostability of the enzyme, is a positive effector for the cooperative class I IMPDH IMPDHpp

741229

-

1.1.1.205

MgATP2- has no effect on the catalytic activity of class II IMPDHsa, but has a role in the modulation of the quaternary structure of class II IMPDHs

741229

-

1.1.1.205

5 entries

1.21.1.2

conversation of 2,4-dichlorobenzoyl-CoA in cytosolic fraction

288484

-

2.7.1.11

the apparent Km for MgATP2- is 0.022 mM

722736

-

2.7.1.90

activation, about 15% as efficient as AMP

642075

-

3.1.3.46

-

94929

-

3.2.1.28

C-trehalase can be activated by MgATP2- in presence of cAMP

136150

-

3.2.2.24

-

731792

-

3.2.2.4

-

171815, 171818, 171819, 171823, 171827, 171829, 171838, 171820, 171821, 171822, 171824, 171826, 171830, 171833, 171834, 171835, 171836, 171837, 171839, 171841, 171843, 171844, 171845, 171847, 171849

-

3.2.2.4

mutant AMP nucleosidase

171828

-

3.2.2.4

2 entries

7.1.2.1

activation of H+-ATPase occurs by the addition of 5 mM Mg-ATP

720724

-

Inhibitor in Enzyme-catalyzed Reactions (48 results)

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Show Inhibitors (48 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.34

-

286568

-

1.1.1.34

4 mM

286568

-

1.1.1.34

2 entries

1.13.12.7

-

484853

-

1.2.1.104

-

348980

-

1.2.1.104

5 mM, 93% inhibition due to phosphorylation

348954

-

1.2.1.104

5 mM, about 70% inhibition after 3 h

348986

-

1.2.1.104

3 entries

1.2.4.1

due to phosphorylation of the enzyme by pyruvate dehydrogenase kinase

348935

-

2.3.1.105

extreme inhibition in all microsomal fractions

486104

-

2.3.1.26

-

486689, 486694

-

2.3.1.26

inhibition of activity

486689

-

2.3.1.26

2 entries

2.3.1.67

32% and 54% inhibition at 0.125 and 1 mM respectively in neuronal nuclear fraction

487393

-

2.4.1.1

reversible by AMP

488244

-

2.4.2.37

-

731792

-

2.4.2.37

in the presence of Mg-ADP

489803

-

2.7.1.105

inhibited by, structure determination reveals substrate inhibition due to sequential binding of two MgATP molecules per subunit, the first at the usual site occupied by the nucleotide in homologous enzymes and the second at the allosteric site, making a number of direct and Mg-mediated interactions with the first, two configurations observed for the second MgATP, one of which involves interactions with Tyr-23 from the adjacent subunit in the dimer and the other making an unusual non-Watson-Crick base pairing with the adenine in the substrate ATP

693665

-

2.7.1.105

allosteric inhibition

692346

-

2.7.1.105

allosteric inhibition, important regulation of in vivo carbohydrate metabolism under gluconeogenic conditions

661754

-

2.7.1.105

E190Q mutant presents alterations in the inhibition by MgATP2- and phosphate

672208

-

2.7.1.11

-

640462, 640476, 640484

-

2.7.1.11

cytosolic isozyme

640427

-

2.7.1.11

inhibition occurs at high concentrations of MgATP2-

722736

-

2.4.2.37

2 entries

2.7.1.105

4 entries

2.7.1.11

3 entries

2.7.1.20

above 1 mM

641080

-

2.7.1.4

-

641497

-

2.7.1.4

inhibition at pH 6.6

641479

-

2.7.1.4

linear-uncompetitive with respect to fructose

641482

-

2.7.1.40

-

641576, 641603, 641614

-

2.7.1.40

activators restore activity

641566

-

2.7.1.40

allosteric inhibitor; fructose 1,6-diphosphate restores

641565

-

2.7.1.40

feed-back inhibition; fructose 1,6-diphosphate restores

641546

-

2.7.1.40

potent inhibitor

675943

-

2.7.1.4

3 entries

2.7.1.40

5 entries

2.7.1.56

-

686728

-

2.7.1.82

substrate inhibition

642041

-

2.7.11.4

-

640575

-

2.7.3.3

enzyme form AK2 is strongly inhibited at high concentrations

642457

-

2.7.4.14

competitive with UMP

645148

-

2.7.4.8

-

642701, 642702

-

2.7.7.4

-

643258, 643280

-

2.7.7.4

competitive with respect to adenosine 5'-phosphosulfate

643267

-

2.7.7.4

competitive with respect to adenosine 5'-phosphosulfate; mixed-type with respect to diphosphate

643268

-

2.7.7.4

3 entries

2.7.7.46

metal chelates being the true substrates, free nucleotides being inhibitors

645286

-

3.1.1.3

-

80849

-

3.1.3.11

-

170770

-

3.1.3.53

inhibits SMMP activity towards P-myosin, disassembles P-myosin mostly into a folded conformation

646352

-

4.1.1.94

inhibits the enzyme slightly

717859

-

6.3.2.2

although the enzyme preparation shows a strict requirement for MgATP2- for gamma-glutamylcysteine synthesis, preincubation of the homogenate under phosphorylating conditions with MgATP2- also causes a maximal inhibition of 89%

672367

-

6.3.2.2

although the enzyme preparation shows a strict requirement for MgATP2- for gamma-glutamylcysteine synthesis, preincubation of the homogenates under phosphorylating conditions with MgATP2- also causes a maximal inhibition of 94%, 77%, 85%, 87%, 83% and 95% in cerebellum, hippocampus, brainstem, striatum, cortex and heart

672367

-

6.3.2.2

2 entries

6.3.5.5

product inhibition

1728

-

6.4.1.1

substrate inhibition

692637

-

Metals and Ions (8 results)

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Show Metals Ions (8 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.205

a positive effector for the cooperative class I IMPDH IMPDHnm

741229

-

1.1.1.205

allosteric regulation of Pseudomonas aeruginosa IMPDH by MgATP2-

739794

-

1.1.1.205

has a positive effector of IMPDHpa acting on the maximal rate and on the affinity for IMP. The positive effector binds onto the two CBS modules, with consequences on the global shape

741229

-

1.1.1.205

MgATP2- has a drastic impact on the kinetic properties of class I IMPDHs. It increases the thermostability of the enzyme, is a positive effector for the cooperative class I IMPDH IMPDHpp

741229

-

1.1.1.205

MgATP2- has no effect on the catalytic activity of class II IMPDHsa, but has a role in the modulation of the quaternary structure of class II IMPDHs

741229

-

1.1.1.205

5 entries

2.2.1.6

activates

671854

-

6.3.4.21

-

637750

-

6.3.4.21

maximal activation at equimolar levels of Mg2+ and ATP, presumably enzyme structure stabilizing

637749

-

6.3.4.21

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (20 results)

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Show Turnover Number (20 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.13.12.7

0.000000157

-

mutant enzyme K443A/K529A

658103

1.13.12.7

0.0000629

-

mutant enzyme K443A

658103

1.13.12.7

0.00025

-

mutant enzyme K529A

658103

1.13.12.7

0.02

-

mutant enzyme G446I

658103

1.13.12.7

0.0875

-

mutant enzyme Q448A

658103

1.13.12.7

0.167

-

wild-type enzyme

658103

1.13.12.7

0.24

-

mutant enzyme K445Q

658103

2.7.1.105

0.14

-

mutant enzyme E190Q, 1 mM Mg2+

672208

2.7.1.105

1.43

-

mutant enzyme E190Q, 30 mM Mg2+

672208

2.7.1.105

13

-

recombinant mutant C295F

661754

2.7.1.105

39

-

recombinant mutant C295A

661754

2.7.1.105

53

-

wild-type enzyme, 1 mM Mg2+

672208

2.7.1.105

53

-

wild-type enzyme, 30 mM Mg2+

672208

2.7.1.105

70

-

recombinant mutants C238A and C238F

661754

2.7.1.105

90

-

recombinant wild-type enzyme

661754

2.7.1.105

9240

-

native enzyme

660957

2.7.1.105

9320

-

C238-pyrene maleimide modified enzyme

660957

2.7.6.1

34.6

-

in the presence of 5 mM Mg2+, in 50 mM potassium phosphate pH 8.0, at 37°C

723524

2.7.6.1

35.5

-

in the absence of free Mg2+ or Mn2+, in 50 mM potassium phosphate pH 8.0, at 37°C

723524

2.7.6.1

44.3

-

in the presence of 5 mM Mn2+, in 50 mM potassium phosphate pH 8.0, at 37°C

723524

1.13.12.7

7 entries

2.7.1.105

10 entries

2.7.6.1

3 entries

K_M Value (111 results)

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Show KM Value (111 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.12.7

0.025

-

-

484853

1.13.12.7

0.029

-

mutant enzyme G246A

657942

1.13.12.7

0.0486

-

mutant enzyme K443A

658103

1.13.12.7

0.069

-

mutant enzyme K445Q

658103

1.13.12.7

0.073

-

mutant enzyme G446I

658103

1.13.12.7

0.08

-

mutant enzyme F247Y

657942

1.13.12.7

0.107

-

mutant enzyme G316A

657942

1.13.12.7

0.133

-

mutant enzyme F250S

657942

1.13.12.7

0.16

-

-

484860

1.13.12.7

0.16

-

wild-type enzyme

657942, 658103

1.13.12.7

0.166

-

mutant enzyme F250G

657942

1.13.12.7

0.2

-

mutant enzyme G341A

657942

1.13.12.7

0.226

-

mutant enzyme F247L

657942

1.13.12.7

0.24

-

mutant enzyme H245A

657942

1.13.12.7

0.285

-

mutant enzyme I351A

657942

1.13.12.7

0.341

-

mutant enzyme Q448A

658103

1.13.12.7

0.344

-

mutant enzyme S347A

657942

1.13.12.7

0.56

-

mutant enzyme K443A/K529A

658103

1.13.12.7

0.857

-

mutant enzyme T343A

657942

1.13.12.7

1.038

-

mutant enzyme A348V

657942

1.13.12.7

1.2

-

mutant enzyme G315A

657942

1.13.12.7

1.2

-

mutant enzyme K529A

657942, 658103

1.13.12.7

1.2

-

mutant enzyme L342A

657942

1.13.12.7

2

-

mutant enzyme T251A

657942

1.13.12.7

3.5

-

mutant enzyme F247A

657942

1.13.12.7

6.2

-

mutant enzyme R218A

657942

1.13.12.7

26 entries

2.5.1.6

0.3

-

ATP in form of MgATP2-

639040

2.7.1.105

0.0072

-

pH 7.1, 30°C, phosphorylated enzyme

94936

2.7.1.105

0.0095

0.012

pH 7.1, 30°C, native pigeon enzyme

94936

2.7.1.105

0.0095

0.012

pH 7.5, 30°C

640300

2.7.1.105

0.01

-

C-terminal deletion mutant L307, 1 mM co-substrate

692346

2.7.1.105

0.0107

-

recombinant mutant C295F

661754

2.7.1.105

0.0137

-

Y306A, C-terminal point mutant, 1 mM co-substrate

692346

2.7.1.105

0.015

-

wild-type, 1 mM co-substrate

692346

2.7.1.105

0.017

-

recombinant wild-type enzyme and mutant C238A

661754

2.7.1.105

0.02

-

wild-type enzyme, 1 mM Mg2+

672208

2.7.1.105

0.021

-

recombinant mutant C238F

661754

2.7.1.105

0.022

-

wild-type enzyme, 30 mM Mg2+

672208

2.7.1.105

0.042

-

native enzyme

660957

2.7.1.105

0.044

-

C238-pyrene maleimide modified enzyme

660957

2.7.1.105

0.061

-

recombinant mutant C295A

661754

2.7.1.105

0.149

-

mutant enzyme E190Q, 1 mM Mg2+

672208

2.7.1.105

0.29

-

pH 7.1, 30°C, native chicken enzyme

94936

2.7.1.105

0.32

-

mutant enzyme E190Q, 30 mM Mg2+

672208

2.7.1.105

0.5

-

-

640281

2.7.1.105

0.5

-

pH 7.5, 30°C

640282, 640286, 640320

2.7.1.105

0.8

-

C-terminal deletion mutant A305, 1 mM co-substrate

692346

2.7.1.105

0.88

-

C-terminal deletion mutant Y306, 1 mM co-substrate

692346

2.7.1.105

0.954

-

L307A, C-terminal point mutant, 1 mM co-substrate

692346

2.7.1.105

2

-

C-terminal deletion mutant D299, 1 mM co-substrate

692346

2.7.1.105

23 entries

2.7.1.20

0.014

-

pH 7.2, 37ºC

641092

2.7.11.19

0.017

0.027

autophosphorylation

492101

2.7.11.19

0.07

-

activated rabbit skeletal muscle enzyme, pH 8.2

492105

2.7.11.19

0.07

-

ATP (+ melittin)

492147

2.7.11.19

0.08

-

activated rabbit skeletal muscle enzyme, pH 6

492105

2.7.11.19

0.08

-

ATP (+ tetrapeptide)

492147

2.7.11.19

0.08

-

pH 8.2, gamma subunit or holoenzyme

492135

2.7.11.19

0.08

-

phosphorylase b, activated enzyme

492113

2.7.11.19

0.098

-

pH 8.2, gamma subunit or holoenzyme

492135

2.7.11.19

0.1

-

dogfish phosphorylase b, pH 8.2, dogfish enzyme

492109

2.7.11.19

0.1

-

nonactivated rabbit skeletal muscle enzyme, pH 6

492105

2.7.4.22

0.19

-

D159N mutant protein, 0.3 mM UMP

698858

2.7.4.22

0.2

-

D159N mutant protein, 1 mM UMP, 0.5 mM GTP

698858

2.7.4.22

0.21

-

D159N mutant protein, 0.3 mM UMP

698858

2.7.4.22

0.21

-

N140A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP

698858

2.7.4.22

0.23

-

N140A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP

698858

2.7.4.22

0.24

-

D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP

698858

2.7.4.22

0.25

-

N140A/D159N mutant protein, 0.3 mM UMP

698858

2.7.4.22

0.26

-

D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP

698858

2.7.4.22

0.27

-

D93A/D159N mutant protein, 0.3 mM UMP

698858

2.7.4.22

0.27

-

D93A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP

698858

2.7.4.22

0.36

-

D93A/D159N mutant protein, 0.3 mM UMP

698858

2.7.4.22

0.4

-

N72A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP

698858

2.7.4.22

0.41

-

D93A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP

698858

2.7.4.22

0.53

-

N140A/D159N mutant protein, 0.3 mM UMP, 0.5 mM UTP

698858

2.7.4.22

0.59

-

D93A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP

698858

2.7.4.22

0.59

-

N72A/D159N mutant protein, 0.3 mM UMP

698858

2.7.4.22

0.59

-

N72A/D93A/D159N mutant protein, 0.3 mM UMP

698858

2.7.4.22

0.64

-

D93A/D159N mutant protein, 0.3 mM UMP, 0.5 mM UTP

698858

2.7.4.22

0.66

-

N72A/D93A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP

698858

2.7.4.22

0.77

-

D159N mutant protein, 0.3 mM UMP, 0.5 mM UTP

698858

2.7.4.8

0.2

-

pH 7.5, 25ºC

642701

2.7.4.8

0.2

-

pH 7.7, 25ºC

642702

2.7.4.8

0.23

-

pH 7.5, 25ºC, S80A mutant

642701

2.7.4.8

0.42

-

-

642694

2.7.4.8

0.45

-

pH 7.7, 25ºC, Y78F mutant

642702

2.7.11.19

10 entries

2.7.4.22

20 entries

2.7.4.8

5 entries

2.7.7.3

0.22

-

forward reaction

674344

2.7.7.4

0.23

-

pH 8.0, 30°C, reaction with MoO42-

643286

2.7.7.4

0.78

-

adenylyl sulfate synthesis

701923

2.7.7.4

1.1

-

pH 8.0, 30°C, reaction with SO42-

643286

3.5.2.9

0.1

-

-

209387

3.5.2.9

0.15

-

-

209371, 209373

3.5.2.9

0.1727

-

-

209382

3.5.2.9

4.2

-

-

209379

2.7.7.4

3 entries

3.5.2.9

4 entries

3.6.1.15

0.0185

-

concentration of MgATP2- higher than 0.006 mM

209874

3.6.1.45

0.25

-

-

289180

3.6.4.6

0.62

-

-

210584

4.6.1.1

0.009

-

in presence of almathicin

34808

4.6.1.1

0.019

-

in absence of amathicin

34808

4.6.1.1

0.13

-

-

34778

4.6.1.1

2.2

-

-

34765

4.6.1.1

4 entries

5.6.1.6

0.15

-

pH 7.5, 37°C

654722

6.2.1.14

0.17

-

-

631

6.2.1.2

0.97

-

-

669

6.3.1.9

0.063

-

pH 7.7, 25°C, recombinant trypanothione synthase

662802

6.3.1.9

0.222

-

pH 7.2, 25°C, recombinant trypanothione synthase

662446

6.3.1.9

0.4

-

-

971

6.3.1.9

3 entries

6.3.2.17

0.018

-

ATP

1075

6.3.2.6

0.04

-

-

1268

6.3.5.2

0.11

-

-

1384

7.4.2.8

0.22

-

pH 7.5, 37°C, ATPase activity of N-terminal cytoplasmic domain

669106

K_i Value (22 results)

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Show KI Value (22 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.12.7

1

-

-

484853

2.7.1.4

0.16

-

pH 8, 30°C

641482

2.7.1.4

0.2

-

-

641497

2.7.1.40

1.77

-

37°C, pH 7.0

641614

2.7.1.40

3.9

-

cosubstrate MgADP-, pH 6.9, 25°C

641603

2.7.1.40

4

-

cosubstrate MgADP-, pH 7.5, 25°C

641603

2.7.1.40

9.6

-

cosubstrate phosphoenolpyruvate, pH 6.9, 25°C

641603

2.7.1.40

10

-

cosubstrate phosphoenolpyruvate, pH 7.5, 25°C

641603

2.7.4.8

0.08

-

pH 7.5, 25ºC

642701

2.7.4.8

0.08

-

pH 7.7, 25ºC

642702

2.7.4.8

0.16

-

pH 7.7, 25ºC, Y78F mutant

642702

2.7.7.4

0.33

-

pH 8.0, 30°C

643268

2.7.7.4

0.385

-

pH 8.0, 30°C, reaction with SeO42- or CrO42-

643268

2.7.7.4

0.41

-

pH 8.0, 30°C, reaction with SO42-

643268

2.7.7.4

0.417

-

pH 8.0, 30°C, reaction with MoO42-

643268

2.7.7.4

0.5

-

pH 8.0, 30°C

643258

2.7.7.4

0.606

-

pH 8.0, 30°C, reaction with WO42-

643268

2.7.7.4

0.71

-

pH 8.0, 30°C

643267

2.7.7.4

0.75

1.3

pH 8.0, 30°C

643280

2.7.1.4

2 entries

2.7.1.40

5 entries

2.7.4.8

3 entries

2.7.7.4

8 entries

2.7.7.46

0.864

-

pH 9.0, 25°C

645286

6.4.1.1

0.4

-

pH 7.8, 30°C, in absence of acetyl-CoA

692637

6.4.1.1

0.5

-

pH 7.8, 30°C, in presence of acetyl-CoA

692637

6.4.1.1

2 entries

References & Links

Literature References (157)

top print hide

Show Reference (157 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

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Biochemistry

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Mol. Cell. Biol.

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Characterization of mono-, di- and triacylglycerol lipase activities in the isolated rat heart

1986

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Biochim. Biophys. Acta

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1987

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Eur. J. Biochem.

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Biochim. Biophys. Acta

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1983

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133851

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1983

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Hexosediphosphatase from spinach chloroplasts. Purification, crystallization and some properties

1974

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Crystallographic quaternary structural analysis of AMP nucleosidases from Escherichia coli and Azotobacter vinelandii

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Crystallization and preliminary X-ray study of AMP nucleosidase

1986

Giranda, V.L.; Berman, H.M.; Schramm, V.L.

J. Biol. Chem.

261

15307-15309

171819

3552037

Catalytic and allosteric mechanism of AMP nucleosidase from primary, beta-secondary, and multiple heavy atom kinetic isotope effects

1987

Parkin, D.W.; Schramm, V.L.

Biochemistry

26

913-920

171820

3552038

Transition state structures for N-glycoside hydrolysis of AMP by acid and by AMP nucleosidase in the presence and absence of allosteric activator

1987

Mentch, F.; Parkin, D.W.; Schramm, V.L.

Biochemistry

26

921-930

171821

3741845

AMP nucleosidase: Kinetic mechanism and thermodynamics

1986

DeWolf, W.E.; Emig, F.A.; Schramm, V.L.

Biochemistry

25

4132-4140

171822

3485632

Mechanism and activation for allosteric adenosine 5¦-monophosphate nucleosidase

1986

Skoog, M.T.

J. Biol. Chem.

261

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171823

6378909

Effects of allosteric activation on the primary and secondary kinetic isotope effects for three AMP nucleosidases

1984

Parkin, D.W.; Schramm, V.L.

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171824

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Effect of growth rate and nutrient limitation on the adenine nucleotide content, energy charge and enzymes of adenylate metabolism in Azotobacter beijerinckii

1981

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Transition-state analysis of a Vmax mutant of AMP nucleosidase by the application of heavy-atom kinetic isotope effects

1991

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Biochemistry

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171827

2690948

Structure and regulation of the AMP nucleosidase gene (amn) from Escherichia coli

1989

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Biochemistry

28

8726-8733

171828

6796578

A mutant AMP nucleosidase. Purification, properties and in vivo turnover of the protein

1981

Leung, H.B.; Schramm, V.L.

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256

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171829

7000783

Adenylate degradation in Escherichia coli. The role of Amp nucleosidase and properties of the purified enzyme

1980

Leung, H.B.; Schramm, V.L.

J. Biol. Chem.

255

10867-10874

171830

6251048

Evidence for substantial separation of the catalytic and allosteric sites of AMP nucleosidase

1980

De Wolf Jr., W.E.; Markham, G.D.; Schramm, V.L.

J. Biol. Chem.

255

8210-8215

171833

486499

Effects of monovalent cations on AMP nucleosidase from Azotobacter vinelandii

1979

Yoshino, M.; Murakami, K.; Tsushima, K.

Biochim. Biophys. Acta

570

118-123

171834

-

Polyamines as activators of AMP nucleosidase from Azotobacter vinelandii

1979

Yoshino, M.; Murakami, K.; Tsushima, K.

Experientia

35

587-579

171835

5118623

Stabilization of allosteric adenosine monophosphate nucleosidase by inorganic salts, substrate, and essential activator

1971

Schramm, V.L.; Hochstein, L.I.

Biochemistry

10

3411-3417

171836

40976

The catalytic site of AMP nucleosidase

1979

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254

10868-10875

171837

221493

Synthesis of a new 8-spin-labeled analog of adenosine 5¦-phosphate and its interaction with AMP nucleosidase

1979

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254

6215-6217

171838

357895

Adenosine monophosphate nucleosidase from Azotobacter vinelandii and Escherichia coli

1978

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The enzymatic cleavage of adenylic acid to adenine and ribose 5-phosphate

1957

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171841

4248622

AMP nucleosidase from Azotobacter vinelandii

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171843

632260

Kinetics of adenosine monophosphate nucleosidase inactivation by phosphate and protection by substrate and allosteric activator

1978

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171844

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Comparison of initial velocity and binding data for allosteric adenosine monophosphate nucleosidase

1976

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251

3417-3424

171845

4361821

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Purification, crystallization, and subunit structure of allosteric adenosine 5¦-monophosphate nucleosidase

1972

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Biochemistry

11

2777-2783

171849

8043576

Electrostatic potential surface analysis of the transition state for AMP nucleosidase and for formycin 5'-phosphate, a transition state inhibitor

1994

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Biochemistry

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8890-8896

209371

3911007

5-Oxo-L-prolinase from Pseudomonas putida

1985

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209373

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1984

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16660609

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1978

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1181279

5-Oxoprolinase from rat kidney, I assay, purification, and determination of kinetic parameters

1975

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1971

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Proc. Natl. Acad. Sci. USA

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209874

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Interaction of calcium and magnesium in activating and inhibiting the nucleoside triphosphatase of sarcoplasmic reticulum vesicles

1975

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Biochim. Biophys. Acta

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210584

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286568

-

Hydroxymethylglutaryl CoA reductase (NADPH) in the latex of Hevea brasiliensis

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Phytochemistry

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288484

8626335

NADPH-dependent reductive ortho dehalogenation of 2,4-dichlorobenzoic acid in Corynebacterium sepedonicum KZ-4 and Coryneform Bacterium strain NBT-1 via 2,4-dichlorobenzoyl coenzym A

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348935

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348980

4317491

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484831

775940

Firefly luciferase

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MgATP inhibits the synthesis of 1-alkyl-2-acetyl-sn-glycero-3-phosphate by microsomal acetyltransferase of immature rabbit cerebral cortex

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486689

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1983

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Phosphorylase kinase

1986

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492105

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1979

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Phosphorylase kinase from dogfish skeletal muscle. Purification and properties

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1982

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Nicotinate phosphoribosyltransferase of yeast. Purification and properties

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Partial purification and characterization of methionine adenosyltransferase from pea seedlings

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Phosphofructokinase 2: the enzyme that forms fructose 2,6-bisphosphate from fructose 6-phosphate and ATP

1981

Van Schaftingen, E.; Hers, H.G.

Biochem. Biophys. Res. Commun.

101

1078-1084

640282

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1981

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