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Modeling of the spatial structure of eukaryotic ornithine decarboxylasesInsights 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 CleavageStructural trees for protein superfamilies.C-S bond cleavage by a polyketide synthase domain.Simultaneous improvement of catalytic activity and thermal stability of tyrosine phenol-lyase by directed evolution.Evaluation of Various Factors Affecting Bioconversion of l-Tyrosine to l-DOPA by Yeast Yarrowia lipolytica-NCIM 3450 Using Response Surface Methodology.Stereospecificity for the hydrogen transfer of pyridoxal enzyme reactions.Tyrosine phenol-lyase and tryptophan indole-lyase encapsulated in wet nanoporous silica gels: Selective stabilization of tertiary conformationsRole of Na+ and K+ in enzyme function.Cloning, purification, and crystallization of Escherichia coli cystathionine beta-lyase.NCS-constrained exhaustive search using oligomeric models.The tryptophanase gene cluster of Haemophilus influenzae type b: evidence for horizontal gene transfer.Integration host factor and cyclic AMP receptor protein are required for TyrR-mediated activation of tpl in Citrobacter freundiiInhibition of tyrosine phenol-lyase by tyrosine homologues.The tpl promoter of Citrobacter freundii is activated by the TyrR protein.Stereochemical constraint in the evolution of pyridoxal-5'-phosphate-dependent enzymes. A hypothesis.Molecular dynamics simulations of a helicase.Aromatic L-amino acid decarboxylase: conformational change in the flexible region around Arg334 is required during the transaldimination process.Structural motifs for pyridoxal-5'-phosphate binding in decarboxylases: an analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase.Similarity between pyridoxal/pyridoxamine phosphate-dependent enzymes involved in dideoxy and deoxyaminosugar biosynthesis and other pyridoxal phosphate enzymesRole of Arg-401 of cytosolic serine hydroxymethyltransferase in subunit assembly and interaction with the substrate carboxy group.Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions.Mutation of cysteine 111 in Dopa decarboxylase leads to active site perturbation.The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis.Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine.Structures of Escherichia coli tryptophanase in holo and 'semi-holo' forms.Crystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes.Stereospecificity of isotopic exchange of C-α-protons of glycine catalyzed by three PLP-dependent lyases: the unusual case of tyrosine phenol-lyase.Plasticity of the Tryptophan Synthase Active Site Probed by31P NMR Spectroscopy
P2860
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P2860
description
1993 nî lūn-bûn
@nan
1993 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Three-dimensional structure of tyrosine phenol-lyase
@ast
Three-dimensional structure of tyrosine phenol-lyase
@en
Three-dimensional structure of tyrosine phenol-lyase
@nl
type
label
Three-dimensional structure of tyrosine phenol-lyase
@ast
Three-dimensional structure of tyrosine phenol-lyase
@en
Three-dimensional structure of tyrosine phenol-lyase
@nl
prefLabel
Three-dimensional structure of tyrosine phenol-lyase
@ast
Three-dimensional structure of tyrosine phenol-lyase
@en
Three-dimensional structure of tyrosine phenol-lyase
@nl
P2093
P356
P1433
P1476
Three-dimensional structure of tyrosine phenol-lyase
@en
P2093
A A Antson
E H Harutyunyan
K S Wilson
P Gollnick
R L von Tersch
R S Phillips
S N Berezhnoy
T V Demidkina
P304
P356
10.1021/BI00067A006
P407
P577
1993-04-27T00:00:00Z