Tyrosine phenol lyase. I. Purification, crystallization, and properties.
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Insights into the Catalytic Mechanism of Tyrosine Phenol-lyase from X-ray Structures of Quinonoid IntermediatesCrystallographic Snapshots of Tyrosine Phenol-lyase Show That Substrate Strain Plays a Role in C–C Bond CleavageBiodegradation of aromatic compounds by Escherichia coliEngineering of solvent-tolerant Pseudomonas putida S12 for bioproduction of phenol from glucose.Evaluation of Various Factors Affecting Bioconversion of l-Tyrosine to l-DOPA by Yeast Yarrowia lipolytica-NCIM 3450 Using Response Surface Methodology.Cloning and random mutagenesis of the Erwinia herbicola tyrR gene for high-level expression of tyrosine phenol-lyase.Reversibility of the tryptophanase reaction: synthesis of tryptophan from indole, pyruvate, and ammonia.Tyrosine phenol-lyase and tryptophan indole-lyase encapsulated in wet nanoporous silica gels: Selective stabilization of tertiary conformationsMetabolic responses of Lactobacillus plantarum strains during fermentation and storage of vegetable and fruit juices.Microbial production of isoquinoline alkaloids as plant secondary metabolites based on metabolic engineering research.Functional analysis of the Erwinia herbicola tutB gene and its product.Partial Purification and Some Properties of Tyrosine Phenol-Lyase from Aeromonas phenologenes ATCC 29063.The tpl promoter of Citrobacter freundii is activated by the TyrR protein.Cloning, nucleotide sequences, and overexpression in Escherichia coli of tandem copies of a tryptophanase gene in an obligately symbiotic thermophile, Symbiobacterium thermophilum.Degradation of tyrosine in anaerobically stored piggery wastes and in pig feces.Monophenol monooxygenase and lincomysin biosynthesis in Streptomyces lincolnensis.Transcriptome analysis of a phenol-producing Pseudomonas putida S12 construct: genetic and physiological basis for improved production.Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions.Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine.In Silico Analysis of Putrefaction Pathways in Bacteria and Its Implication in Colorectal Cancer.
P2860
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P2860
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
description
1970 nî lūn-bûn
@nan
1970 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1970 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1970年の論文
@ja
1970年論文
@yue
1970年論文
@zh-hant
1970年論文
@zh-hk
1970年論文
@zh-mo
1970年論文
@zh-tw
1970年论文
@wuu
name
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
@ast
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
@en
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
@nl
type
label
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
@ast
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
@en
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
@nl
prefLabel
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
@ast
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
@en
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
@nl
P2093
P1476
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
@en
P2093
P304
P407
P577
1970-04-01T00:00:00Z