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ATP + biotin + apo-beta-methylcrotonyl-CoA carboxylase
AMP + diphosphate + holo-beta-methylcrotonyl-CoA carboxylase
-
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
ATP + biotin + apo-[propionyl CoA carboxylase]
AMP + diphosphate + propionyl CoA carboxylase
-
-
-
-
?
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apoacetyl-CoA carboxylase
AMP + diphosphate + holoacetyl-CoA carboxylase
-
biotinylation of cytosolic ACC
-
-
?
ATP + biotin + apocarboxyl carrier protein
AMP + diphosphate + holocarboxyl carrier protein
-
HCS catalyzes the incorporation of biotin into carboxylases, recombinant apo-CCP from Escherichia coli
-
-
?
ATP + biotin + apocarboxylase
AMP + diphosphate + holocarboxylase
-
-
-
-
?
ATP + biotin + apopropionyl-CoA carboxylase
AMP + diphosphate + holopropionyl-CoA carboxylase
-
biotinylation of mitochondrial PCC
-
-
?
ATP + biotin + apopyruvate carboxylase
AMP + diphosphate + holopyruvate carboxylase
-
-
-
-
?
ATP + biotin + BCCP87
AMP + diphosphate + biotin-BCCP87
-
substrate is the biotinoyl domain, BCCP87, of Escherichia coli biotin carboxyl carrier protein, BCCP, binding pattern, overview
-
-
?
ATP + biotin + histone H2A
AMP + diphosphate + biotin-histone H2A
-
pattern of biotin attachment and comparison to nonenzymatic biotinylation of histone H2A, none of the lysine sites within histone H2A resembles the biotin attachment consensus sequence seen in carboxylases, mechanism, overview. H2A is a poor substrate for biotin attachment compared to the apocarboxylase biotin-attachment domain
-
-
?
ATP + biotin + histone H3.2
AMP + diphosphate + biotin-histone H3.2
-
-
biotinylation of residues K9 and K18 in histone H3
-
?
ATP + biotin + histone H3.2 N-terminal amino acids 1-25
AMP + diphosphate + biotin-histone H3.2 N-terminal amino acids 1-25
-
-
biotinylation of residues K9 and K18
-
?
ATP + biotin + histone H4
AMP + diphosphate + biotin-histone H4
-
biotinylation at Lys12 especially in telomeric repeats, overview
-
-
?
ATP + biotin + p67
AMP + diphosphate + biotinyl-p67
-
comprises the 67 C-terminal amino acids in human propionyl-CoA carboxylase, including the biotin-binding site lysine-669
-
-
?
ATP + biotin + protein Syn67
AMP + diphosphate + protein Syn67-biotin
-
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
-
-
?
biotinyl-5'-AMP + apocarboxylase
AMP + holocarboxylase
-
-
-
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
CTP can totally replace ATP
-
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
GTP is approximately half as active as ATP
-
-
?
ITP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
ITP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
ITP is approximately half as active as ATP
-
-
?
UTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
UMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
additional information
?
-
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
-
plays an essential role in biotin utilization
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
-
its deficiency causes biotin-responsive multiple carboxylase deficiency in humans
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
-
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
biotinylates apopropionyl-CoA carboxylase from patients with holocarboxylase synthetase deficiency
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
biotinyl-AMP is an intermediate
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
the alpha-subunit of propionyl-CoA carboxylase and its mature counterpart are competent for biotinylation
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
-
-
-
-
?
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
-
substrate is p67, the carboxyl-terminal fragment of the propionyl-CoA-carboxylase alpha subunit, the substrate is biotinylated at Lys67
-
-
?
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + 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
-
-
?
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
HCS catalyzes the incorporation of biotin into carboxylases, holo-PCC is formed from the apo-PCC from biotin-deficient rat liver or human lymphoblast in the presence of d-biotin and ATP, much higher activity with apo-PCC from rat livers than from human lymphoblasts
-
-
?
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
HCS catalyzes the incorporation of biotin into carboxylases, holo-PCC is formed from the apo-PCC
-
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
as active as ATP
-
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
117% of the activity relative to ATP
-
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
28% of the activity relative to ATP
-
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
19% of the activity relative to ATP
-
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
50% of the activity relative to ATP
-
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
46% of the activity relative to ATP
-
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
11% of the activity relative to ATP
-
-
?
ITP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
50% of the activity relative to ATP
-
-
?
ITP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
47% of the activity relative to ATP
-
-
?
ITP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
UTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
UMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
95% of the activity relative to ATP
-
-
?
UTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
UMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
24% of the activity relative to ATP
-
-
?
additional information
?
-
-
HCS catalyzes the ATP-dependent biotinylation of the four biotin-dependent carboxylases found in humans
-
-
?
additional information
?
-
-
although mammals have multiple biotin-dependent enzymes there is only a single gene encoding holocarboxylase synthetase, HCS, responsible for all cellular biotinylation. The enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
-
holocarboxylase synthetase catalyzes the attachment of biotin to the epsilon-amino group of a specific lysine residue in apocarboxylases, biotinylation of biotin-dependent carboxylases requires ATP and proceeds in the following two steps
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
-
the 4'-hydroxyazobenzene-2-carboxylic acid dye assay can be used to quantify biotin
-
-
?
additional information
?
-
-
the N-terminal domain of hHCS recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain
-
-
?
additional information
?
-
-
the enzyme is critical to utilization of exogenous or dietary biotin and responds to biotin deprivation by reduction in the steady state level of their mRNAs. The free biotin is directed to brain because the reduction in holocarboxylase synthetase, sodium-dependent multivitamin-transporter and carboxylase mRNAs in liver reduces their capacity to utilize biotin while leaving free biotin in circulation
-
-
?
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malfunction
-
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
-
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
-
deficiency in human HCS results in decreased activity of the acyl-CoA carboxylase and affects various metabolic processes
malfunction
-
holocarboxylase synthetase deficiency causes multiple carboxylase deficiency, phenotypes, overview
malfunction
-
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
metabolism
-
holocarboxylase synthetase governs the cellular fate of the essential micronutrient biotin, i.e. vitamin H or B7
metabolism
-
the enzyme is involved in the biotin metabolism, detailed overview
metabolism
-
the enzyme is part of the biotin metabolism in which it catalyses the attachment of biotin to apoenzyme carboxylases
metabolism
-
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
physiological function
-
biotinylation of lysine residues in histones by holocarboxylase synthetase is an epigenetic diet-dependent mechanism to regulate chromatin structure and gene expression
physiological function
-
HCS catalyzes the binding of the vitamin biotin to carboxylases and histones
physiological function
-
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
-
HCS is responsible for attaching biotin onto the biotin-dependent enzymes that reside in the cytoplasm and mitochondria
physiological function
-
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
-
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
-
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
-
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
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Murthy, P.N.A.; Mistry, S.P.
In vitro synthesis of propionyl-CoA holocarboxylase by a partially purified mitochondrial preparation from biotin-deficient chicken liver
Can. J. Biochem.
52
800-803
1974
Gallus gallus
brenda
Suzuki, Y.; Narisawa, K.
Purification and properties of bovine and human holocarboxylase synthetase
Methods Enzymol.
279
386-393
1997
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
brenda
Taroni, F.; Rosenberg, L.E.
The precursor of the biotin-binding subunit of mammalian propionyl-CoA carboxylase can be translocated into mitochondria as apo- or holoprotein
J. Biol. Chem.
266
13267-13271
1991
Rattus norvegicus
brenda
Dupuis, L.; Leon-del Rio, A.; Leclerc, D.; Campeau, E.; Sweetman, L.; Saudubray, J.M.; Herman, G.; Gibson, K.M.; Gravel, R.A.
Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency
Hum. Mol. Genet.
5
1011-1016
1996
Homo sapiens
brenda
Suzuki, Y.; Aoki, Y.; Ichida, Y.; Chiba, A.; Iwamatsu, T.; Kishini, T.; Matsubara, Y.; Narisawa, K.
Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA
Nature Genet.
8
122-128
1994
eukaryota, Homo sapiens
brenda
Siegel, L.; Foote, J.L.; Coon, M.J.
The enzymatic synthesis of propionyl coenzyme A holocarboxylase from d-biotinyl 5'-adenylate and the apocarboxylase
J. Biol. Chem.
240
1025-1031
1965
Oryctolagus cuniculus, Rattus norvegicus
brenda
Chiba, Y.; Suzuki, Y.; Aoki, Y.; Ishida, Y.; Narisawa, K.
Purification and properties of bovine liver holocarboxylase synthetase
Arch. Biochem. Biophys.
313
8-14
1994
Bos taurus
brenda
Tissot, G.; Douce, R.; Alban, C.
Evidence for multiple forms of biotin holocarboxylase synthetase in pea (Pisum sativum) and in Arabidopsis thaliana: subcellular fractionation studies and isolation of cDNA clone
Biochem. J.
323
179-188
1997
Arabidopsis thaliana, Pisum sativum
brenda
Cronan, J.E.; Wallace, J.C.
The gene encoding the biotin-apoprotein ligase of Saccharomyces cerevisiae
FEMS Microbiol. Lett.
130
221-230
1995
Saccharomyces cerevisiae
brenda
Pacheco-Alvarez, D.; Solorzano-Vargas, R.S.; Gravel, R.A.; Cervantes-Roldan, R.; Velazquez, A.; Leon-Del-Rio, A.
Paradoxical regulation of biotin utilization in brain and liver and implications for inherited multiple carboxylase deficiency
J. Biol. Chem.
279
52312-52318
2004
Rattus norvegicus
brenda
Hassan, Y.I.; Moriyama, H.; Zempleni, J.
The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation
Arch. Biochem. Biophys.
495
35-41
2010
Homo sapiens
brenda
Bailey, L.M.; Wallace, J.C.; Polyak, S.W.
Holocarboxylase synthetase: correlation of protein localisation with biological function
Arch. Biochem. Biophys.
496
45-52
2010
Homo sapiens
brenda
Zempleni, J.; Wijeratne, S.S.; Hassan, Y.I.
Biotin
Biofactors
35
36-46
2009
Homo sapiens
brenda
Yokoi, K.; Ito, T.; Maeda, Y.; Nakajima, Y.; Kurono, Y.; Sugiyama, N.; Togari, H.
A case of holocarboxylase synthetase deficiency with insufficient response to prenatal biotin therapy
Brain Dev.
31
775-778
2009
Homo sapiens
brenda
Tammachote, R.; Janklat, S.; Tongkobpetch, S.; Suphapeetiporn, K.; Shotelersuk, V.
Holocarboxylase synthetase deficiency: novel clinical and molecular findings
Clin. Genet.
78
88-93
2009
Homo sapiens
brenda
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
FEBS Lett.
584
675-680
2010
Homo sapiens
brenda
Ingaramo, M.; Beckett, D.
Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition
J. Biol. Chem.
284
30862-30870
2009
Homo sapiens
brenda
Nyhan, W.L.; Willis, M.; Barshop, B.A.; Gangoiti, J.
Positive newborn screen in the biochemically normal infant of a mother with treated holocarboxylase synthetase deficiency
J. Inherit. Metab. Dis.
32
S79-82
2009
Homo sapiens
brenda
Wijeratne, S.S.; Camporeale, G.; Zempleni, J.
K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
J. Nutr. Biochem.
21
310-316
2010
Homo sapiens
brenda
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
Mol. Genet. Metab.
96
183-188
2009
Homo sapiens
brenda
Healy, S.; Heightman, T.D.; Hohmann, L.; Schriemer, D.; Gravel, R.A.
Nonenzymatic biotinylation of histone H2A
Protein Sci.
18
314-328
2009
Homo sapiens
brenda
Singh, D.; Pannier, A.; Zempleni, J.
Identification of holocarboxylase synthetase chromatin binding sites in human mammary cell lines using the DNA adenine methyltransferase identification technology
Anal. Biochem.
413
55-59
2011
Homo sapiens
brenda
Rios-Avila, L.; Prince, S.; Wijeratne, S.; Zempleni, J.
A 96-well plate assay for high-throughput analysis of holocarboxylase synthetase activity
Clin. Chim. Acta
412
735-739
2011
Homo sapiens
brenda
Bao, B.; Pestinger, V.; Hassan, Y.; Borgstahl, G.; Kolar, C.; Zempleni, J.
Holocarboxylase synthetase is a chromatin protein and interacts directly with histone H3 to mediate biotinylation of K9 and K18
J. Nutr. Biochem.
22
470-475
2011
Homo sapiens
brenda
Bao, B.; Rodriguez-Melendez, R.; Wijeratne, S.; Zempleni, J.
Biotin regulates the expression of holocarboxylase synthetase in the miR-539 pathway in HEK-293 cells
J. Nutr.
140
1546-1551
2010
Homo sapiens
brenda
Reyes-Carmona, S.; Valadez-Graham, V.; Aguilar-Fuentes, J.; Zurita, M.; Leon-Del-Rio, A.
Trafficking and chromatin dynamics of holocarboxylase synthetase during development of Drosophila melanogaster
Mol. Genet. Metab.
103
240-248
2011
Drosophila melanogaster
brenda
Xue, J.; Zhou, J.; Zempleni, J.
Holocarboxylase synthetase catalyzes biotinylation of heat shock protein 72, thereby inducing RANTES expression in HEK-293 cells
Am. J. Physiol. Cell Physiol.
305
C1240-C1245
2013
Homo sapiens
brenda
Bao, B.; Wijeratne, S.S.; Rodriguez-Melendez, R.; Zempleni, J.
Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity
Biochem. Biophys. Res. Commun.
412
115-120
2011
Homo sapiens
brenda
Li, Y.; Hassan, Y.I.; Moriyama, H.; Zempleni, J.
Holocarboxylase synthetase interacts physically with euchromatic histone-lysine N-methyltransferase, linking histone biotinylation with methylation events
J. Nutr. Biochem.
24
1446-1452
2013
Homo sapiens
brenda
Miyao, H.; Ikeda, Y.; Shiraishi, A.; Kawakami, Y.; Sueda, S.
Immobilization of immunoglobulin-G-binding domain of Protein A on a gold surface modified with biotin ligase
Anal. Biochem.
484
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2015
Sulfurisphaera tokodaii (F9VNG7), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (F9VNG7)
brenda
Donti, T.R.; Blackburn, P.R.; Atwal, P.S.
Holocarboxylase synthetase deficiency pre and post newborn screening
Mol. Genet. Metab. Rep.
7
40-44
2016
Homo sapiens
brenda