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Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family.
TLDR
The discovered substrate selectivity switch is a rare example of a complete alteration of substrate specificity by a single point mutation, and the identity of the amino acid at the switch position can serve as a guide to predict substrate specificities of annotated aromatic amino acid lyases in genome sequences. Expand
Biosynthesis of plant-specific stilbene polyketides in metabolically engineered Escherichia coli
TLDR
Phenylpropionic acids, such as 4-coumaric acid and caffeic acid, can be efficiently converted to stilbene compounds by recombinant E. coli cells expressing plant biosynthetic genes and optimization of precursor conversion and cyclization of the bulky ferulic acid precursor by host metabolic engineering and protein engineering may afford the synthesis of even more structurally diverse stilBene compounds. Expand
Engineered Protein Nano-Compartments for Targeted Enzyme Localization
TLDR
Recombinant expression of Salmonella enterica ethanolamine utilization (eut) bacterial microcompartment shell proteins in E. coli results in the formation of polyhedral protein shells, providing proof-of-concept for the engineering of protein nano-compartments for biosynthesis and biocatalysis. Expand
Diversity of sesquiterpene synthases in the basidiomycete Coprinus cinereus
TLDR
Six sesquiterpene synthases (Cop1 to Cop6) and two terpene‐oxidizing cytochrome P450 monooxygenases (Cox1 and Cox2) from Coprinus cinereus are described and found to catalyse the highly specific synthesis of α‐cuprenene. Expand
Exploring Recombinant Flavonoid Biosynthesis in Metabolically Engineered Escherichia coli
TLDR
The cloning and coexpression in Escherichia coli of phenylalanine ammonia lyase, cinnamate‐4‐hydroxylase, 4‐coumarate:CoA ligase, and chalcone synthase from the model plant Arabidopsis thaliana are reported, with high‐level production of the flavanone naringenin observed for the first time. Expand
Biosynthesis of Isoprenoid Wax Ester in Marinobacter hydrocarbonoclasticus DSM 8798: Identification and Characterization of Isoprenoid Coenzyme A Synthetase and Wax Ester Synthases
TLDR
One of the Marinobacter wax ester synthases displays several orders of magnitude higher activity toward acyl substrates than any previously characterized acyl-WS and may reflect adaptations to available carbon sources in their environments. Expand
A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A.
TLDR
A rapid and continuous spectrophotometric activity assay for cytochrome P450 BM-3 based on the conversion of p-nitrophenoxycarboxylic acids (pNCA) to omega-oxycaroxydodecanoic and the chromophore p-Nitrophenolate was developed. Expand
Metabolic engineering towards biotechnological production of carotenoids in microorganisms
TLDR
This review will describe the recent progress made in metabolic engineering of non-carotenogenic microorganisms for improved carotenoid productivity and discuss the application of combinatorial and evolutionary strategies to carOTenoid pathway engineering to broaden the diversity of carotanoid structures synthesized in recombinant hosts. Expand
Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus.
TLDR
The strain Bacillus thermocatenulatus (DSM 730) produced the highest lipase activity and was purified 67-fold to homogenous state by hexane extraction, methanol precipitation and ion-exchange chromatography on Q-Sepharose. Expand
High-Level Formation of Active Pseudomonas cepaciaLipase after Heterologous Expression of the Encoding Gene and Its Modified Chaperone in Escherichia coli and Rapid In Vitro Refolding
TLDR
With this chaperone, it was possible to obtain for the first time in a simple refolding procedure a highly active Pseudomonas lipase (classes I and II) expressed in E. coli with a specific activity of up to 4,850 U/mg and a yield of 314,000 U/g of E. Escherichia coli wet cells. Expand
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