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

Efficient biocatalyst of L-DOPA with Escherichia coli expressing a tyrosine phenol-lyase mutant from Kluyvera intermedia.

Applied biochemistry and biotechnology - 1 Apr 2020

Yuan Wei, Zhong Shuang, Xiao Yanming, Wang Zhao, Sun Jie

Abstract excerpt

L-DOPA (L-dihydroxyphenylalanine) is a promising drug for Parkinson's disease and thereby has a growing annual demand. Tyrosine phenol-lyase (TPL)-based catalysis is considered to be a low-cost yet efficient route for biosynthesis of L-DOPA. TPL is a tetrameric enzyme that catalyzes the synthesis of L-DOPA from pyrocatechol, sodium pyruvate, and ammonium acetate. The implementation of TPL for L-DOPA production...

Read the complete abstract on PubMed

Topics

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

Share to Acetates
Share to Biocatalysis
Share to Catechols

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Levodopa

Share to Pyridoxal Phosphate

Share to Pyruvic Acid

Share to Sodium

Source

Identifiers

PMID: 31729696
DOI: 10.1007/s12010-019-03164-1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Efficient biocatalyst of L-DOPA with Escherichia coli expressing a tyrosine phenol-lyase mutant from Kluyvera intermedia.PMID 31729696Read ↗

Identification and enhanced activity of the tyrosine phenol-lyase from Mycobacterium tuberculosis.Semantic proximity Read ↗

An efficient colorimetric high-throughput screening method for synthetic activity of tyrosine phenol-lyase.Semantic proximity Read ↗

An engineered dual-functional L-DOPA decarboxylase enables a minimized hydroxytyrosol cascade.Semantic proximity Read ↗

Hyperproduction of 3,4-dihydroxyphenyl-L-alanine (L-Dopa) using Erwinia herbicola cells carrying a mutant transcriptional regulator TyrR.Semantic proximity Read ↗

A computational strategy to improve the activity of tyrosine phenol-lyase for the synthesis of L-DOPA.Semantic proximity Read ↗

Melanin Biosynthesis and Omics: Homogentisate Pathway Dysfunction Drives Pyomelanin Production in Mutant Bacillus thuringiensis var. israelensis MB-24.Semantic proximity Read ↗

Efficient production of salvianic acid A from L-dihydroxyphenylalanine through a tri-enzyme cascadeSemantic proximity Read ↗

Microbial production of L-tyrosine: a review.Semantic proximity Read ↗

Genetic engineering of Escherichia coli to improve L-phenylalanine production.Semantic proximity Read ↗

Semi-rational design of L-amino acid deaminase for production of pyruvate and D-alanine by Escherichia coli whole-cell biocatalyst.Semantic proximity Read ↗

Expanding metabolism for total biosynthesis of the nonnatural amino acid L-homoalanine.Semantic proximity Read ↗

Rational, combinatorial, and genomic approaches for engineering L-tyrosine production in Escherichia coli.Semantic proximity Read ↗

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