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heterodimer
fluorescence resonance energy transfer technique and co-immunoprecipitation
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x * 55000
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all values determined by SDS-PAGE
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apparent homodimers and heterodimers of UGT2B1 and UGT1A6
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x * 54000 by chromatofocusing and affinity chromatography on UDP-hexanolamine Sepharose 4B with 4-aminobiphenyl as a specific substrate
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x * 53000 by chromatofocusing and affinity chromatography on UDP-hexanolamine Sepharose 4B with estradiol as a specific substrate
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x * 53000 estriol-UDPGT
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all values determined by SDS-PAGE
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all values determined by SDS-PAGE
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x * 58500, deduced from cDNA sequence, higher value than that obtained from SDS-PAGE electrophoresis
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x * 32000, recombinant GlcAT-P and GlcAT-S, SDS-PAGE
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x * 55000, recombinant isozyme UGT1A4, SDS-PAGE
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x * 52000-55000, SDS-PAGE
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x * 86000, CFP-tagged recombinant UGT1A enzyme, SDS-PAGE, x * 56000, HA-tagged recombinant UGT1A enzyme, SDS-PAGE
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x * 86000, CFP-tagged recombinant UGT1A1, SDS-PAGE, x * 56000, HA-tagged recombinant UGT1A1, SDS-PAGE
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x * 86000, CFP-tagged recombinant UGT1A10, SDS-PAGE, x * 56000, HA-tagged recombinant UGT1A10, SDS-PAGE
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x * 86000, CFP-tagged recombinant UGT1A3, SDS-PAGE, x * 56000, HA-tagged recombinant UGT1A3, SDS-PAGE
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x * 86000, CFP-tagged recombinant UGT1A6, SDS-PAGE, x * 56000, HA-tagged recombinant UGT1A6, SDS-PAGE
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x * 86000, CFP-tagged recombinant UGT1A7, SDS-PAGE, x * 56000, HA-tagged recombinant UGT1A7, SDS-PAGE
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x * 86000, CFP-tagged recombinant UGT1A8, SDS-PAGE, x * 56000, HA-tagged recombinant UGT1A8, SDS-PAGE
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x * 86000, CFP-tagged recombinant UGT1A9, SDS-PAGE, x * 56000, HA-tagged recombinant UGT1A9, SDS-PAGE
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x * 65000, His6-tagged recombinant enzyme, SDS-PAGE
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all values determined by SDS-PAGE
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all values determined by SDS-PAGE
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all values determined by SDS-PAGE
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4-nitrophenol UDP-glucuronyltransferase
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3alpha-hydroxysteroid UDP-glucuronyltransferase
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x * 57000, SDS-polyacrylamide gel electrophoresis
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isozymes GT-1 and GT-2, identical subunit weights, but different N-terminal amino acid sequences
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x * 56000, morphine-UDPGT
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x * 50000, Wistar strain
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x * 59000, SDS-polyacrylamide gel electrophoresis
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x * 56000, phenobarbital-inducible isozyme
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additional values for rat isozymes ranging from 51000 to 59000
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x * 56000, 4-nitrophenol-UDPGT
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x * 52000, 3alpha-hydroxysteroid-UDPGT
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x * 53000, Wistar strain
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bilirubin UDP-glucuronosyltransferase
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x * 54000, methylcholanthrene-inducible isozyme
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all values determined by SDS-PAGE
488697, 488698, 488703, 488712, 488715, 488717, 488718, 488719, 488725, 488727, 488730, 488732, 488737, 488738, 488739, 488756, 488758, 488760, 488767, 488768, 488779, 488790
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x * 50000, 17beta-hydroxysteroid-UDPGT
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x * 50000, 17-beta-hydroxysteroid UDPglucuronosyl transferase activity
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x * 50000, 17beta-hydroxysteroid UDP-glucuronyltransferase
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x * 52000, 3-alpha-hydroxysteroid UDPglucuronosyl transferase activity
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deglycosylated isozymes GT-1 and GT-2
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bilirubin UDP-glucuronosyltransferase
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all values determined by SDS-PAGE
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all values determined by SDS-PAGE
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x * 50000, 17-beta-hydroxysteroid UDPglucuronosyl transferase activity
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x * 52000, 3-alpha-hydroxysteroid UDPglucuronosyl transferase activity
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x * 56000, phenobarbital-inducible isozyme
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additional values for rat isozymes ranging from 51000 to 59000
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x * 54000, methylcholanthrene-inducible isozyme
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bilirubin UDP-glucuronosyltransferase
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isozymes GT-1 and GT-2, identical subunit weights, but different N-terminal amino acid sequences
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deglycosylated isozymes GT-1 and GT-2
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x * 57000, SDS-polyacrylamide gel electrophoresis
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monomer
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by chromatofocusing
monomer
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by chromatofocusing
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tetramer
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isozyme for conversion of bilirubin monoglucuronide to bilirubin diglucuronide, a + b + c + d, subunits a and b have a low Km for UDPglucuronide, c and d have a high Km for UDP-glucuronide, a and b can catalyze the conversion of bilirubin to bilirubin monoglucuronide, radiation inactivation
tetramer
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isozyme for conversion of bilirubin monoglucuronide to bilirubin diglucuronide, a + b + c + d, subunits a and b have a low Km for UDPglucuronide, c and d have a high Km for UDP-glucuronide, a and b can catalyze the conversion of bilirubin to bilirubin monoglucuronide, radiation inactivation
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additional information
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additional information
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additional information
hetero-oligomerization may play an important role in UDP-glucuronosyltransferases activity
additional information
hetero-oligomerization may play an important role in UDP-glucuronosyltransferases activity
additional information
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hetero-oligomerization may play an important role in UDP-glucuronosyltransferases activity
additional information
homology-based computer modeling of isozyme UGT1A10, overview
additional information
isozyme UGT1A1 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with isozymes UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9, and UGT1A10 to form heterodimers
additional information
isozyme UGT1A1 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with isozymes UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9, and UGT1A10 to form heterodimers
additional information
isozyme UGT1A1 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with isozymes UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9, and UGT1A10 to form heterodimers
additional information
isozyme UGT1A1 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with isozymes UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9, and UGT1A10 to form heterodimers
additional information
isozyme UGT1A1 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with isozymes UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9, and UGT1A10 to form heterodimers
additional information
isozyme UGT1A1 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with isozymes UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9, and UGT1A10 to form heterodimers
additional information
isozyme UGT1A1 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with isozymes UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9, and UGT1A10 to form heterodimers
additional information
isozyme UGT1A1 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with isozymes UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9, and UGT1A10 to form heterodimers
additional information
isozyme UGT1A10 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A10 to form heterodimers
additional information
isozyme UGT1A10 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A10 to form heterodimers
additional information
isozyme UGT1A10 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A10 to form heterodimers
additional information
isozyme UGT1A10 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A10 to form heterodimers
additional information
isozyme UGT1A10 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A10 to form heterodimers
additional information
isozyme UGT1A10 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A10 to form heterodimers
additional information
isozyme UGT1A10 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A10 to form heterodimers
additional information
isozyme UGT1A10 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A10 to form heterodimers
additional information
isozyme UGT1A3 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A3 to form heterodimers
additional information
isozyme UGT1A3 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A3 to form heterodimers
additional information
isozyme UGT1A3 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A3 to form heterodimers
additional information
isozyme UGT1A3 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A3 to form heterodimers
additional information
isozyme UGT1A3 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A3 to form heterodimers
additional information
isozyme UGT1A3 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A3 to form heterodimers
additional information
isozyme UGT1A3 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A3 to form heterodimers
additional information
isozyme UGT1A3 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A3 to form heterodimers
additional information
isozyme UGT1A4 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A4 to form heterodimers
additional information
isozyme UGT1A4 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A4 to form heterodimers
additional information
isozyme UGT1A4 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A4 to form heterodimers
additional information
isozyme UGT1A4 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A4 to form heterodimers
additional information
isozyme UGT1A4 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A4 to form heterodimers
additional information
isozyme UGT1A4 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A4 to form heterodimers
additional information
isozyme UGT1A4 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A4 to form heterodimers
additional information
isozyme UGT1A4 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A4 to form heterodimers
additional information
isozyme UGT1A6 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A6 to form heterodimers
additional information
isozyme UGT1A6 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A6 to form heterodimers
additional information
isozyme UGT1A6 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A6 to form heterodimers
additional information
isozyme UGT1A6 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A6 to form heterodimers
additional information
isozyme UGT1A6 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A6 to form heterodimers
additional information
isozyme UGT1A6 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A6 to form heterodimers
additional information
isozyme UGT1A6 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A6 to form heterodimers
additional information
isozyme UGT1A6 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A6 to form heterodimers
additional information
isozyme UGT1A7 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A7 to form heterodimers
additional information
isozyme UGT1A7 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A7 to form heterodimers
additional information
isozyme UGT1A7 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A7 to form heterodimers
additional information
isozyme UGT1A7 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A7 to form heterodimers
additional information
isozyme UGT1A7 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A7 to form heterodimers
additional information
isozyme UGT1A7 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A7 to form heterodimers
additional information
isozyme UGT1A7 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A7 to form heterodimers
additional information
isozyme UGT1A7 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A7 to form heterodimers
additional information
isozyme UGT1A8 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A8 to form heterodimers
additional information
isozyme UGT1A8 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A8 to form heterodimers
additional information
isozyme UGT1A8 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A8 to form heterodimers
additional information
isozyme UGT1A8 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A8 to form heterodimers
additional information
isozyme UGT1A8 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A8 to form heterodimers
additional information
isozyme UGT1A8 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A8 to form heterodimers
additional information
isozyme UGT1A8 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A8 to form heterodimers
additional information
isozyme UGT1A8 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A8 to form heterodimers
additional information
isozyme UGT1A9 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A9 to form heterodimers
additional information
isozyme UGT1A9 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A9 to form heterodimers
additional information
isozyme UGT1A9 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A9 to form heterodimers
additional information
isozyme UGT1A9 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A9 to form heterodimers
additional information
isozyme UGT1A9 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A9 to form heterodimers
additional information
isozyme UGT1A9 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A9 to form heterodimers
additional information
isozyme UGT1A9 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A9 to form heterodimers
additional information
isozyme UGT1A9 self-oligomerizes to homodimers. Isozyme UGT1A1 is capable of binding with UGT1A9 to form heterodimers
additional information
prediction of protein-protein interactions between isozymes, in silico modelling
additional information
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primary enzyme sequence comparisons and secondary structures of UGT isozymes, domain structures, structure-activity relationship, comparative modelling, overview
additional information
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substrate binding structure, homology mnodelling of wild-type and mutant isozymes UGT1A6 and UGT1A9, overview
additional information
the enzyme is composed of an N-terminal domain with an aglycon binding site, a short transmembrane sequence, a C-terminal domain with UDP-glucuronic acid binding site, a transmembrane heleix and a cytoplasmic tail, primary to quarternary structure and oligomeric state analysis of several isozymes, homo- and heterooligomerization, detailed overview
additional information
the enzyme is composed of an N-terminal domain with an aglycon binding site, a short transmembrane sequence, a C-terminal domain with UDP-glucuronic acid binding site, a transmembrane heleix and a cytoplasmic tail, primary to quarternary structure and oligomeric state analysis of several isozymes, homo- and heterooligomerization, detailed overview
additional information
the enzyme is composed of an N-terminal domain with an aglycon binding site, a short transmembrane sequence, a C-terminal domain with UDP-glucuronic acid binding site, a transmembrane heleix and a cytoplasmic tail, primary to quarternary structure and oligomeric state analysis of several isozymes, homo- and heterooligomerization, detailed overview
additional information
the enzyme is composed of an N-terminal domain with an aglycon binding site, a short transmembrane sequence, a C-terminal domain with UDP-glucuronic acid binding site, a transmembrane heleix and a cytoplasmic tail, primary to quarternary structure and oligomeric state analysis of several isozymes, homo- and heterooligomerization, detailed overview
additional information
UGT2B7 forms oligomers that affect its enzymatic activity. Proteinprotein interactions among UGT2B7 allozymes wild-type, A71S, H268Y and D398N, by performing a systematic quantitative fluorescence resonance energy transfer (FRET) analysis in combination with co-immunoprecipitation assay, UGT2B7 allozymes form homo- and hetero-dimers and show distinct features in donoracceptor distances. Both codon 71 and codon 268 in the N-terminal domain are involved in the dimeric interaction. Coimmunoprecipitation experiments also prove that UGT2B7 allozymes form stable dimers
additional information
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UGT2B7 forms oligomers that affect its enzymatic activity. Proteinprotein interactions among UGT2B7 allozymes wild-type, A71S, H268Y and D398N, by performing a systematic quantitative fluorescence resonance energy transfer (FRET) analysis in combination with co-immunoprecipitation assay, UGT2B7 allozymes form homo- and hetero-dimers and show distinct features in donoracceptor distances. Both codon 71 and codon 268 in the N-terminal domain are involved in the dimeric interaction. Coimmunoprecipitation experiments also prove that UGT2B7 allozymes form stable dimers
additional information
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the enzyme is composed of an N-terminal domain with an aglycon binding site, a short transmembrane sequence, a C-terminal domain with UDP-glucuronic acid binding site, a transmembrane helix and a cytoplasmic tail, primary to quarternary structure and oligomeric state analysis of several isozymes, detailed overview