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Literature summary for 6.3.4.10 extracted from

  • Hassan, Y.I.; Moriyama, H.; Zempleni, J.
    The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation (2010), Arch. Biochem. Biophys., 495, 35-41.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens holocarboxylase synthetase, HCS, catalyzes the binding of biotin to lysines in carboxylases and histones in two steps. First, HCS catalyzes the synthesis of biotinyl-5'-AMP, and second, the biotinyl moiety is ligated to lysine residues, binding structure, modelling, overview ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + protein Syn67 mutated Syn67, both N- and C-termini of HCS interact with Syn67, a polypeptide with a basic patch of lysines and arginines, and the Syn67 docking site is located near the active pocket of HCS. The target lysine in Syn67 is biotinylated by HCS only after arginine-to-glycine substitutions in Syn67 produce a histone-like peptide, binding structure, modelling, overview Homo sapiens AMP + diphosphate + protein Syn67-biotin
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additional information holocarboxylase synthetase, HCS, catalyzes the binding of biotin to lysines in carboxylases and histones in two steps. First, HCS catalyzes the synthesis of biotinyl-5'-AMP, and second, the biotinyl moiety is ligated to lysine residues, binding structure, modelling, overview Homo sapiens ?
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?

Synonyms

Synonyms Comment Organism
HCS
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Homo sapiens
Holocarboxylase synthetase
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Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
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Homo sapiens