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
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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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General Information
General Information on EC 6.3.4.10 - biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase
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malfunction
metabolism
physiological function
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biotin deficiency, e.g. occuring in patients with BTD deficiency, in severely malnourished children in developing countries, and in individuals consuming large amounts of raw egg white which contains the protein avidin, has adverse effects on cellular and humoral immune functions, and it can lead to candida dermatitis and presented with absent delayed-hypersensitivity skin-tests responses, IgA deficiency, and subnormal percentages of T-lymphocytes in peripheral blood, overview
malfunction
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defective activity of holocarboxylase synthetase in the biotin cycle causes multiple carboxylase deficiency, MCD, an autosomal recessive metabolic disorder usually in the neonatal or early-onset form
malfunction
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deficiency in human HCS results in decreased activity of the acyl-CoA carboxylase and affects various metabolic processes
malfunction
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holocarboxylase synthetase deficiency causes multiple carboxylase deficiency, phenotypes, overview
malfunction
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holocarboxylase synthetase, HCS, deficiency is an inborn error of biotin metabolism, leading to a multiple carboxylases deficiency. A Japanese male neonate with HCS deficiency received maternal administration of biotin from 33 weeks gestation, acylcarnitine profiles compared to control, phenotype, overview
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holocarboxylase synthetase governs the cellular fate of the essential micronutrient biotin, i.e. vitamin H or B7
metabolism
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the enzyme is part of the biotin metabolism in which it catalyses the attachment of biotin to apoenzyme carboxylases
metabolism
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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
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biotinylation of lysine residues in histones by holocarboxylase synthetase is an epigenetic diet-dependent mechanism to regulate chromatin structure and gene expression
physiological function
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HCS catalyzes the binding of the vitamin biotin to carboxylases and histones
physiological function
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HCS catalyzes transfer of biotin to biotin-dependent carboxylases, and the enzyme is therefore of fundamental importance for many physiological processes, including fatty acid synthesis, gluconeogenesis, and amino acid catabolism. In addition, the enzyme functions in regulating transcription initiation at several genes that code for proteins involved in biotin metabolism
physiological function
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HCS is responsible for attaching biotin onto the biotin-dependent enzymes that reside in the cytoplasm and mitochondria
physiological function
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HCS co-localizes with histone H3 in human cells with physical interactions between HCS and H3. The N-terminal and C-terminal domains in HCS participate in H3 binding
physiological function
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HCS migrates to the nucleus at the gastrulation stage. In polytene chromosomes, it is associated to heterochromatin bands where it co-localizes with histone 3 trimethylated at lysine 9 but not with the euchromatin mark histone 3 acetylated at lysine 9. HCS associates with the hsp70 promoter. On heat-shock activation of the hsp70 promoter, HCS is displaced and the promoter region becomes enriched with the TFIIH subunits XPD and XPB and elongating RNA pol I
physiological function
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identification of HCS docking sites in chromatin. 4 out of 15 docking sites overlap between MCF-7 and MCF-10A cells, i.e. inositol polyphosphate-5-phosphatase A, corticotropin hormone precursor, ribosome biogenesis regulatory protein, and leptin precursor
physiological function
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enzyme-dependent biotinylation of heat shock protein 72 increases expression of the chemokine regulated on activation normal T-expressed and presumably secreted by HEK-293 cells