Ligand apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Basic Ligand Information
Molecular Structure

C16H29N3O3R2S2
apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
Roles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)
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ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrate in Enzyme-catalyzed Reactions (5 results)
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ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
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CTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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GTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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ITP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Enzyme Kinetic Parameters
References & Links
Literature References (3)
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Purification and properties of bovine and human holocarboxylase synthetase
1997
Suzuki, Y.; Narisawa, K.
Methods Enzymol.
279
386-393
Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity
2011
Bao, B.; Wijeratne, S.S.; Rodriguez-Melendez, R.; Zempleni, J.
Biochem. Biophys. Res. Commun.
412
115-120
Holocarboxylase synthetase interacts physically with euchromatic histone-lysine N-methyltransferase, linking histone biotinylation with methylation events
2013
Li, Y.; Hassan, Y.I.; Moriyama, H.; Zempleni, J.
J. Nutr. Biochem.
24
1446-1452
Links to other databases for apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]