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Literature summary extracted from

  • Li, Y.; Hassan, Y.I.; Moriyama, H.; Zempleni, J.
    Holocarboxylase synthetase interacts physically with euchromatic histone-lysine N-methyltransferase, linking histone biotinylation with methylation events (2013), J. Nutr. Biochem., 24, 1446-1452.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.4.10 ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] Homo sapiens
-
AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.10 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.10 ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Homo sapiens AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?

Synonyms

EC Number Synonyms Comment Organism
6.3.4.10 HCS
-
Homo sapiens
6.3.4.10 Holocarboxylase synthetase
-
Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.4.10 ATP
-
Homo sapiens

General Information

EC Number General Information Comment Organism
6.3.4.10 metabolism holocarboxylase synthetase catalyzes the binding of the vitamin biotin to histones H3 and H4, thereby creating rare histone biotinylation marks in the epigenome. The enzyme interacts physically with euchromatic histone-lysine N-methyltransferase Homo sapiens