How does an enzyme evolved in vitro compare to naturally occurring homologs possessing the targeted function? Tyrosine aminotransferase from aspartate aminotransferase.
about
Janus: Prediction and Ranking of Mutations Required for Functional Interconversion of EnzymesStructural Analysis and Mutant Growth Properties Reveal Distinctive Enzymatic and Cellular Roles for the Three Major L-Alanine Transaminases of Escherichia coliLaboratory evolution of one disulfide isomerase to resemble anotherMolecular signatures-based prediction of enzyme promiscuity.Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity.Molecular evolution of B6 enzymes: binding of pyridoxal-5'-phosphate and Lys41Arg substitution turn ribonuclease A into a model B6 protoenzyme.Engineering monolignol 4-O-methyltransferases to modulate lignin biosynthesisLatent phenotypes pervade gene regulatory circuits.Directed evolution of the substrate specificity of dialkylglycine decarboxylaseAssessing directed evolution methods for the generation of biosynthetic enzymes with potential in drug biosynthesis.Origins of specificity and promiscuity in metabolic networks.Identification of functional paralog shift mutations: conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase.A compromise required by gene sharing enables survival: Implications for evolution of new enzyme activitiesUsing Evolution to Guide Protein Engineering: The Devil IS in the Details.Aspartate aminotransferase: an old dog teaches new tricks.Recombinant expression of twelve evolutionarily diverse subfamily Ialpha aminotransferasesDirected evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase.Engineering homooligomeric proteins to detect weak intersite allosteric communication: aminotransferases, a case study.Molecular function prediction for a family exhibiting evolutionary tendencies toward substrate specificity swapping: recurrence of tyrosine aminotransferase activity in the Iα subfamily.A Three-Ring Circus: Metabolism of the Three Proteogenic Aromatic Amino Acids and Their Role in the Health of Plants and Animals.Evolution AfterandBefore Gene Duplication?
P2860
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P2860
How does an enzyme evolved in vitro compare to naturally occurring homologs possessing the targeted function? Tyrosine aminotransferase from aspartate aminotransferase.
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
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2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
How does an enzyme evolved in ...... om aspartate aminotransferase.
@ast
How does an enzyme evolved in ...... om aspartate aminotransferase.
@en
type
label
How does an enzyme evolved in ...... om aspartate aminotransferase.
@ast
How does an enzyme evolved in ...... om aspartate aminotransferase.
@en
prefLabel
How does an enzyme evolved in ...... om aspartate aminotransferase.
@ast
How does an enzyme evolved in ...... om aspartate aminotransferase.
@en
P1476
How does an enzyme evolved in ...... om aspartate aminotransferase.
@en
P2093
Jack F Kirsch
Steven C Rothman
P304
P356
10.1016/S0022-2836(03)00095-0
P407
P577
2003-03-01T00:00:00Z