Recent developments in the enzymatic modifications of steroid scaffolds

Organic & Biomolecular Chemistry, Journal Year: 2024, Volume and Issue: 22(18), P. 3559 - 3583

Published: Jan. 1, 2024

This review highlights the recent advancements in enzymatic modifications of steroid scaffolds, emphasizing hydroxylation, ketoreduction, dehydrogenation, cascade reactions, and other modifications.

Language: Английский

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Rational modification of the iron ion-binding site to improve the expression of human lactoferrin in Pichia pastoris and validation of the mutant protein function

Food Bioscience, Journal Year: 2025, Volume and Issue: unknown, P. 105984 - 105984

Published: Jan. 1, 2025

Language: Английский

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A CYP450 monooxygenase MaCYP82C169 discovered from mulberry leaves catalyzes the methyl oxidation reaction in 1-deoxynojirimycin biosynthesis

Food Bioscience, Journal Year: 2025, Volume and Issue: unknown, P. 106177 - 106177

Published: Feb. 1, 2025

Language: Английский

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Efficient Biosynthesis of Chlorogenic Acid in Escherichia coli by Optimization of Precursors Metabolic Flow and Reduction of an Unknown Byproduct

ACS Sustainable Chemistry & Engineering, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 25, 2025

Language: Английский

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Metabolic Engineering of Saccharomyces cerevisiae for High Bioproduction of (+)-Nootkatone

ACS Agricultural Science & Technology, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 28, 2025

Language: Английский

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Catalytic Mechanism of Gut Benzyl Ether Reductase for Efficient Bioconversion of Furofuran Lignans into Enterolignan Precursors

Journal of Agricultural and Food Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: March 9, 2025

Enterolignan is a vital anticancer compound, and benzyl ether reductase (BER) plays key role in its biosynthesis by facilitating lignan biotransformation. Using virtual alanine scanning site-directed mutagenesis, we identified critical residues influencing BER activity DSM 2243T. Mutations Y214A, K383A, K395A led to near-complete loss of enzymatic activity, highlighting their essential roles. Conversely, the E332Y, G393V, L515A variants demonstrated over 2-fold increase catalytic efficiency compared wild-type BER. Molecular docking dynamics simulations revealed that Y214 K383 are involved substrate recognition binding, while K395, functioning as base, forms η3 loop (residues 389–396) regulates pocket's size spatial resistance. In BER, this moves inward 5 Å upon binding. However, mutants, shifts outward 4.8, 6.1, 5.6 Å, respectively, likely enhancing accommodation efficiency. This movement also appears influence hydride transfer from cofactors pinoresinol, which crucial step mechanism. These findings offer valuable insights into BER's mechanism lay foundation for enzyme engineering optimize enterolignan biomanufacturing.

Language: Английский

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Modulating phosphate transfer process for promoting phosphorylation activity of acid phosphatase

Bioresource Technology, Journal Year: 2025, Volume and Issue: unknown, P. 132348 - 132348

Published: March 1, 2025

Language: Английский

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High-Level De Novo Production of (2S)-Naringenin in Yarrowia lipolytica Using Metabolic and Enzyme Engineering

ACS Agricultural Science & Technology, Journal Year: 2025, Volume and Issue: unknown

Published: March 12, 2025

Language: Английский

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Biocatalytic Synthesis of Corticosteroid Derivatives by Toad-Derived Steroid C21-Hydroxylase

Organic Letters, Journal Year: 2025, Volume and Issue: unknown

Published: April 17, 2025

CsCYP21A, a steroid 21-hydroxylase from Bufo bufo gargarizans, exhibits unprecedented sequential oxidations. Optimizing Pichia pastoris biotransformation conditions enhanced C21-hydroxylation selectivity, converting 14 substrates to 21-hydroxylated products, with 10 conversions of >80% and 4 yields >80%. Hydrocortisone production reached 1.5 g L-1 day-1 100 g/L wet biomass. CsCYP21A's versatility enables integration into the synthesis over steroidal drugs, offering sustainable biocatalytic platform for green pharmaceutical manufacturing.

Language: Английский

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Electron transfer engineering of artificially designed cell factory for complete biosynthesis of steroids

Nature Communications, Journal Year: 2025, Volume and Issue: 16(1)

Published: April 21, 2025

Biosynthesis of steroids by artificially designed cell factories often involves numerous nicotinamide adenine dinucleotide phosphate (NADPH)-dependent enzymes that mediate electron transfer reactions. However, the unclear mechanisms from regeneration to final delivery NADPH-dependent active centers limit systematically engineering improve production. Here, we elucidate for engineer Saccharomyces cerevisiae, including step-by-step residues 7-Dehydrocholesterol reductase (DHCR7) and P450 sterol side chain cleaving enzyme (P450scc), components directing carbon flux, NADPH pathways, high-level production cholesterol (1.78 g/L) pregnenolone (0.83 g/L). The (ETE) process makes chains shorter more stable which significantly accelerates deprotonation proton coupled process. This study underscores significance ETE strategies in biosynthesis expands synthetic biology approaches.

Language: Английский

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