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Integrate thermostabilized fusion protein apocytochrome b ₅₆₂ RIL and N-glycosylation mutations: A novel approach to heterologous expression of human UDP-glucuronosyltransferase (UGT) 2B7.

ABSTRACT: Human UDP-glucuronosyltransferase (UGT) 2B7 is a crucial phase II metabolic enzyme that transfers glucuronic acid from UDP-glucuronic acid (UDPGA) to endobiotic and xenobiotic substrates. Biophysical and biochemical investigations of UGT2B7 are hampered by the challenge of the integral membrane protein purification. This study focused on the expression and purification of recombinant UGT2B7 by optimizing the insertion sites for the thermostabilized fusion protein apocytochrome b ₅₆₂RIL (BRIL) and various mutations to improve the protein yields and homogeneity. Preparation of the recombinant proteins with high purity accelerated the measurement of pharmacokinetic parameters of UGT2B7. The dissociation constants (K _D) of two classical substrates (zidovudin

SUBMITTER: Xue J

PROVIDER: S-EPMC9412022 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature

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Integrate thermostabilized fusion protein apocytochrome b ₅₆₂ RIL and N-glycosylation mutations: A novel approach to heterologous expression of human UDP-glucuronosyltransferase (UGT) 2B7.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Integrate thermostabilized fusion protein apocytochrome b 562 RIL and N-glycosylation mutations: A novel approach to heterologous expression of human UDP-glucuronosyltransferase (UGT) 2B7.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Integrate thermostabilized fusion protein apocytochrome b ₅₆₂ RIL and N-glycosylation mutations: A novel approach to heterologous expression of human UDP-glucuronosyltransferase (UGT) 2B7.