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Literature summary for 6.3.4.10 extracted from

  • Hassan, Y.I.; Moriyama, H.; Olsen, L.J.; Bi, X.; Zempleni, J.
    N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition (2009), Mol. Genet. Metab., 96, 183-188.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.4.10

Cloned(Commentary)

Cloned (Comment) Organism
expression of p67 and truncated HCS in Saccharomyces cerevisiae for interaction analysis in the two-hybrid system, overview. Usage of derivatives of Saccharomyces cerevisiae wild-type strain W303 Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + biotin + apo-[propionyl-CoA carboxylase] Homo sapiens
-
 AMP + diphosphate + propionyl-CoA carboxylase
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + apo-[propionyl-CoA carboxylase]
-
 Homo sapiens AMP + diphosphate + propionyl-CoA carboxylase
-
 ?
ATP + biotin + apo-[propionyl-CoA carboxylase] substrate is p67, the carboxyl-terminal fragment of the propionyl-CoA-carboxylase alpha subunit, the substrate is biotinylated at Lys67. Determination of amino acid of HCS involved in the interaction, docking of p67 near Arg508 and Ser515 within the central domain of HCS, overview Homo sapiens AMP + diphosphate + propionyl-CoA carboxylase
-
 ?

Subunits

Subunits Comment Organism
More modeling of the 3D structure of human HCS, HCS comprises four putative domains, i.e. the N-terminus, the biotin transfer/ATP-binding domain, a putative linker domain, and the C-terminus. Both N- and C-termini are essential for biotinylation of carboxylases by HCS Homo sapiens

Synonyms

Synonyms Comment Organism
HCS
-
 Homo sapiens
Holocarboxylase synthetase
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function HCS catalyzes the binding of the vitamin biotin to carboxylases and histones Homo sapiens