Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Engineered Biosynthesis of β-Alkyl Tryptophan Analogues.

Angewandte Chemie (International ed. in English) - 5 Nov 2018

Boville Christina E, Scheele Remkes A, Koch Philipp, Brinkmann-Chen Sabine, Buller Andrew R, Arnold Frances H

Abstract excerpt

Noncanonical amino acids (ncAAs) with dual stereocenters at the α and β positions are valuable precursors to natural products and therapeutics. Despite the potential applications of such bioactive β-branched ncAAs, their availability is limited due to the inefficiency of the multistep methods used to prepare them. Herein we report a stereoselective biocatalytic synthesis of β-branched tryptophan analogues using...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biocatalysis
Share to Biological Products

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Crystallography, X-Ray

Share to Protein Engineering

Share to Pyrococcus furiosus

Share to Tryptophan

Share to Tryptophan Synthase

Source

Identifiers

PMID: 30215880
DOI: 10.1002/anie.201807998

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Engineered Biosynthesis of β-Alkyl Tryptophan Analogues.PMID 30215880Read ↗

An Engineered Tryptophan Synthase Opens New Enzymatic Pathways to β-Methyltryptophan and Derivatives.Semantic proximity Read ↗

Directed evolution of the tryptophan synthase β-subunit for stand-alone function recapitulates allosteric activation.Semantic proximity Read ↗

Directed Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational Ensemble.Semantic proximity Read ↗

Scalable continuous evolution for the generation of diverse enzyme variants encompassing promiscuous activities.Semantic proximity Read ↗

Reprogramming Substrate and Catalytic Promiscuity of Tryptophan Prenyltransferases.Semantic proximity Read ↗

One step synthesis of unnatural β-arylalanines using mutant phenylalanine aminomutase from Taxus chinensis with high β-regioselectivity.Semantic proximity Read ↗

Characterization of a Tryptophan 6-Halogenase from Streptomyces albus and Its Regioselectivity Determinants.Semantic proximity Read ↗

Reshaping the substrate binding region of (R)-selective ω-transaminase for asymmetric synthesis of (R)-3-amino-1-butanol.Semantic proximity Read ↗

Bio-inspired engineering of thiopeptide antibiotics advances the expansion of molecular diversity and utility.Semantic proximity Read ↗

A diversity oriented synthesis of natural product inspired molecular libraries.Semantic proximity Read ↗

Continuous evolution of a halogenase enzyme with improved solubility and activity for sustainable bioproduction.Semantic proximity Read ↗

Substrate specificity engineering of leucine dehydrogenase for efficient synthesis of aromatic L-homophenylalanine.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.