Ligand ATPgammaS

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Basic Ligand Information

Molecular Structure
Picture of ATPgammaS (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C10H16N5O12P3S
ATPgammaS
NLTUCYMLOPLUHL-KQYNXXCUSA-N
Synonyms:
adenosine-5'-O-(3-thiotriphosphate), adenosine-5'-[gamma-thio]triphosphate, adenosine 5'-(3-thio)triphosphate, adenosine 5'-(3-thiotriphosphate), adenosine 5'-(gamma-thio)triphosphate, adenosine 5'-O-(3-thio)triphosphate, adenosine 5'-O-(3-thio-triphosphate), adenosine 5'-O-(3-thiotriphosphate), adenosine 5'-O-(3thiotriphosphate), adenosine 5'-[gamma-thio]-triphosphate, adenosine 5' [gamma-thio] triphosphate, adenosine 5-(gamma-thio)triphosphate, AMP-PP(S), ATP(gamma)S, ATP-gamma-S, ATP-gammaS, ATP[gammaS], gamma-S-ATP, gamma-Thio-ATP, [gamma-S]ATP

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATPgammaS + myelin basic protein = ADP + thiophosphorylated myelin basic protein
show the reaction diagram

Substrate in Enzyme-catalyzed Reactions (22 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
coelenterazine disulfate + O2 + ATP-gamma-S = ? + CO2 + hv
show the reaction diagram
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + gamma-S-ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + thiophosphate + R-S-S-R
show the reaction diagram
-
gamma-thio-ATP + fructose 6-phosphate = ADP + fructose 1-thio-phosphate-6-phosphate
show the reaction diagram
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adenosine 5'-O-(3-thiotriphosphate) + adenosine 5-phosphosulfate = ADP + 3'-thiophosphoadenosine 5'-phosphosulfate
show the reaction diagram
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adenosine-5'-O-(3-thiotriphosphate) + riboflavin = ?
show the reaction diagram
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adenosine 5'-O-(3-thio-triphosphate) + mevalonate = adenosine 5'-O-(3-thio-diphosphate) + 5-phosphomevalonate
show the reaction diagram
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ATPgammaS + rhodopsin = ?
show the reaction diagram
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ATPgammaS + myelin basic protein = ADP + thiophosphorylated myelin basic protein
show the reaction diagram
adenosine 5'-(3-thio)triphosphate + AMP = adenosine 5'-diphosphate + adenosine 5'-(3-thio)diphosphate
show the reaction diagram
-
gamma-S-ATP + GDP = ADP + gamma-S-GTP
show the reaction diagram
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adenosine 5'-O-(3-thiotriphosphate) + H2O = AMP + ?
show the reaction diagram
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Adenosine 5'-O-(3-thio)triphosphate + L-leucine + tRNALeu = adenosine 5'-monophosphate + thiodiphosphate + L-leucyl-tRNALeu
show the reaction diagram
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ATPgammaS + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine = ADP + ? + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
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ATPgammaS + 5-formyltetrahydrofolate = ADPgammaS + phosphate + 5,10-methylenetetrahydrofolate
show the reaction diagram
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ATPgammaS + XMP + Gln = ?
show the reaction diagram
-
ATP-gammaS + Glu-tRNAGln + L-glutamine = ? + phosphate + Gln-tRNAGln + L-glutamate
show the reaction diagram
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adenosine 5'-[gamma-thio]-triphosphate + (deoxyribonucleotide)n + (deoxyribonucleotide)m = ?
show the reaction diagram
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ATPgammaS + ATP = P1,P4-bis(5'-adenosyl) tetraphosphate + thiodiphosphate
show the reaction diagram
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ATPgammaS + RNA 3'-terminal-phosphate = AMP + thiodiphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
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ATPgammaS + H2O + H+/in = ADP + thiophosphate + H+/out
show the reaction diagram
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Enzyme Cofactor/Cosubstrate (7 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
dissociation constants as ATP in binding to PDK3
-
i.e. ATP-gamma-thiophosphate
-
wild-type enzyme and mutants, dependent on protein substrate, low activity
-
HslVU degrades insulin B-chain more rapidly in the presence of ATPgammaS than with ATP
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Activator in Enzyme-catalyzed Reactions (17 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
80% of the activation with ATP
-
in 1:1 mixture with ATP, greatly stimulates protein remodeling
-
nonhydrolyzable ATP analogue sustains production of positive supercoils, but to a lesser extent, suggesting that ATP hydrolysis is necessary for efficient activity
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Inhibitor in Enzyme-catalyzed Reactions (45 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
36% inhibition
-
competitive inhibition, Ki: 33 mM
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inhibits 26S proteasome ATPase activity over the same concentration range in which it stimulates peptidase activity
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complete inhibition of ATPase activity
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IC50: 0.19 mM
-
inhibits ATPase activity but not the Na+ binding capacity of the enzyme
-
existence of two binding sites for ATPS with remarkably different binding affinities. One site binds ATPgammaS with Kd of 6 microM and the second binds ATPgammaS with Kd of 0.74 mM
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3D Structure of Enzyme-Ligand-Complex (PDB) (1976 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (3 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
0.016
-
wild-type, pH 7.0, 30°C
0.09
-
pH 8.0
0.00283
-
pH-independent, 30°C

KM Value (11 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.13
-
pH 7.0, 30°C
0.06
-
pH 8.0
0.025
-
-
0.027
-
pH 7.5, 30°C
0.055
-
-
0.172
-
-
0.00021
-
-

Ki Value (5 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.18
-
pH 7.4, 30°C
0.0571
-
30°C, Src
0.24
-
pH 7.0
0.11
-
pH 6.8, temperature not specified in the publication
0.36
-
pH 7.5, 37°C

IC50 Value (2 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.027
-
inhibition of degradation of [PO]-d[TCCTCTTTTTTT]
0.19
-
IC50: 0.19 mM

References & Links

Links to other databases for ATPgammaS

ChEBI
PubChem
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PubChem