Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity.
about
Novel roles of holocarboxylase synthetase in gene regulation and intermediary metabolismLysine biotinylation and methionine oxidation in the heat shock protein HSP60 synergize in the elimination of reactive oxygen species in human cell cultures.Effects of single-nucleotide polymorphisms in the human holocarboxylase synthetase gene on enzyme catalysis.Three promoters regulate the transcriptional activity of the human holocarboxylase synthetase gene.Holocarboxylase synthetase interacts physically with euchromatic histone-lysine N-methyltransferase, linking histone biotinylation with methylation events.Holocarboxylase synthetase synergizes with methyl CpG binding protein 2 and DNA methyltransferase 1 in the transcriptional repression of long-terminal repeats.β-Keto and β-hydroxyphosphonate analogs of biotin-5'-AMP are inhibitors of holocarboxylase synthetase.Biotinylation of lysine 16 in histone H4 contributes toward nucleosome condensation.The biotin-ligating protein BPL-1 is critical for lipid biosynthesis and polarization of the Caenorhabditis elegans embryo.
P2860
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P2860
Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity.
description
2011 nî lūn-bûn
@nan
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
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2011年论文
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2011年论文
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name
Human holocarboxylase syntheta ...... in and has catalytic activity.
@en
type
label
Human holocarboxylase syntheta ...... in and has catalytic activity.
@en
prefLabel
Human holocarboxylase syntheta ...... in and has catalytic activity.
@en
P2093
P2860
P1476
Human holocarboxylase syntheta ...... in and has catalytic activity.
@en
P2093
Baolong Bao
Janos Zempleni
Rocio Rodriguez-Melendez
Subhashinee S K Wijeratne
P2860
P304
P356
10.1016/J.BBRC.2011.07.055
P577
2011-07-23T00:00:00Z