Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Lee, C.K.; Cheong, C.; Jeon, Y.H.
    The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein (2010), FEBS Lett., 584, 675-680.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.10 Mg2+
-
 Homo sapiens
6.3.4.15 Mg2+
-
 Homo sapiens

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 carboxylase] Homo sapiens
-
 AMP + diphosphate + propionyl CoA carboxylase
-
 ?
6.3.4.15 ATP + biotin + apocarboxylase Homo sapiens
-
 AMP + diphosphate + holocarboxylase
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.10 Homo sapiens
-
-
-
6.3.4.15 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 carboxylase]
-
 Homo sapiens AMP + diphosphate + propionyl CoA carboxylase
-
 ?
6.3.4.10 additional information the N-terminal domain of hHCS recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain Homo sapiens ?
-
 ?
6.3.4.15 ATP + biotin + apo-[acetyl-CoA carboxylase 2] i.e. ACC2, substrate is the recombinantly expressed His-tagged biotinoyl domain, ACC75, of ACC2. The apo-biotinoyl domain is biotinylated at Lys929 to form the holoprotein Homo sapiens AMP + diphosphate + acetyl-CoA carboxylase 2
-
 ?
6.3.4.15 ATP + biotin + apocarboxylase
-
 Homo sapiens AMP + diphosphate + holocarboxylase
-
 ?
6.3.4.15 additional information the N-terminal domain of hHCS recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.4.10 More the N-terminal domain has a crucial effect on the enzymatic activity. The domain interacts not only with biotin acceptor protein, but also with the catalytic domain of hHCS. It recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain. Human HCS shows a high degree of sequence homology in the catalytic domain with bacterial biotin ligases such as Escherichia coli BirA, but differs in the length and sequence of the N-terminus Homo sapiens
6.3.4.15 More the N-terminal domain has a crucial effect on the enzymatic activity. The domain interacts not only with biotin acceptor protein, but also with the catalytic domain of hHCS. It recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain. Human HCS shows a high degree of sequence homology in the catalytic domain with bacterial biotin ligases such as Escherichia coli BirA, but differs in the length and sequence of the N-terminus Homo sapiens

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.4.10 30
-
 assay at Homo sapiens
6.3.4.15 30
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.4.10 8
-
 assay at Homo sapiens
6.3.4.15 8
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.4.10 ATP
-
 Homo sapiens
6.3.4.15 ATP
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
6.3.4.10 malfunction deficiency in human HCS results in decreased activity of the acyl-CoA carboxylase and affects various metabolic processes Homo sapiens
6.3.4.15 malfunction deficiency in human HCS results in decreased activity of the acyl-CoA carboxylase and affects various metabolic processes Homo sapiens