6.3.4.10: biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase
This is an abbreviated version!
For detailed information about biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase, go to the full flat file.
Word Map on EC 6.3.4.10
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6.3.4.10
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biotinylation
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carboxylases
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biotin-dependent
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histone
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biotinidase
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acidosis
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biotin-responsive
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multivitamin
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aciduria
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biotinyl-5\'-amp
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biotin-deficient
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apocarboxylases
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methylcitrate
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3-hydroxyisovaleric
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hyperammonemia
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tokodaii
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3-methylcrotonyl-coa
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biotin-binding
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diagnostics
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medicine
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analysis
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synthesis
- 6.3.4.10
-
biotinylation
- carboxylases
-
biotin-dependent
- histone
- biotinidase
- acidosis
-
biotin-responsive
-
multivitamin
- aciduria
-
biotinyl-5\'-amp
-
biotin-deficient
- apocarboxylases
-
methylcitrate
-
3-hydroxyisovaleric
-
hyperammonemia
- tokodaii
- 3-methylcrotonyl-coa
-
biotin-binding
- diagnostics
- medicine
- analysis
- synthesis
Reaction
Synonyms
biotin protein ligase, Biotin-propionyl coenzyme A carboxylase synthetase, Biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] synthetase, BPL, HCS, HLCS, Holocarboxylase synthetase, Propionyl coenzyme A holocarboxylase synthetase, Synthetase, biotin-propionyl coenzyme A carboxylase
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Subunits
Subunits on EC 6.3.4.10 - biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase
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monomer
additional information
monomer
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1 * 81000, the two isozymes are monomers both in their apoforms and when bound to the enzymatic intermediate biotinyl 5'-AMP, equilibrium sedimentation centrifugation
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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
additional information
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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