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Ligand apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.3.4.10

ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]

726859, 728180

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Substrate in Enzyme-catalyzed Reactions (5 results)

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Show Substrate (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.3.4.10

ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]

1390

-

6.3.4.10

ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]

726859, 728180

-

6.3.4.10

CTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]

1390

-

6.3.4.10

GTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]

1390

-

6.3.4.10

ITP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]

1390

-

6.3.4.10

5 entries

Enzyme Kinetic Parameters

References & Links

Literature References (3)

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Show Reference (3 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1390

9211291

Purification and properties of bovine and human holocarboxylase synthetase

1997

Suzuki, Y.; Narisawa, K.

Methods Enzymol.

279

386-393

726859

21802411

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

728180

23337344

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)]

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Show Links (1 entry)

ChEBI

PubChem

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