scholarly article | Q13442814 |
P2093 | author name string | J C Wootton | |
B G Hall | |||
P W Betts | |||
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Novel stereospecificity of the L-arabinose-binding protein | Q27729139 | ||
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A mutant Ebg enzyme that converts lactose into an inducer of the lac operon. | Q34136838 | ||
The ebg operon consists of at least two genes | Q34165956 | ||
Number of mutations required to evolve a new lactase function in Escherichia coli | Q34169110 | ||
Sequence of the ebgA gene of Escherichia coli: comparison with the lacZ gene | Q34195974 | ||
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Experimental evolution of a new enzymatic function. Kinetic analysis of the ancestral (ebg) and evolved (ebg) enzymes | Q34324582 | ||
Nucleotide sequence of Klebsiella pneumoniae lac genes | Q36365090 | ||
Transgalactosylation activity of ebg beta-galactosidase synthesizes allolactose from lactose. | Q36384865 | ||
Evolution of a new enzymatic function by recombination within a gene | Q36394222 | ||
Sequence-directed mutagenesis: evidence from a phylogenetic history of human alpha-interferon genes | Q37540329 | ||
Regulation of newly evolved enzymes. III Evolution of the ebg repressor during selection for enhanced lactase activity | Q40772725 | ||
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Regulation of newly evolved enzymes. I. Selection of a novel lactase regulated by lactose in Escherichia coli | Q42973472 | ||
Sequence of the ebgR gene of Escherichia coli: evidence that the EBG and LAC operons are descended from a common ancestor | Q44371914 | ||
Multiple substitutions create biased estimates of divergence times and small increases in the variance to mean ratio. | Q52870975 | ||
Predicted structure of the sugar-binding site of the lac repressor | Q64517266 | ||
Atomic protein structures reveal basic features of binding of sugars and ionic substrates, and calcium cation | Q68715068 | ||
Multiple base-pair mutations in yeast | Q69837312 | ||
UK nutrition. Government chokes on report | Q71774105 | ||
P433 | issue | 4 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 635-648 | |
P577 | publication date | 1989-12-01 | |
P1433 | published in | Genetics | Q3100575 |
P1476 | title | DNA sequence analysis of artificially evolved ebg enzyme and ebg repressor genes | |
P478 | volume | 123 |
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Q41844922 | Catalytic consequences of experimental evolution: catalysis by a 'third-generation' evolvant of the second beta-galactosidase of Escherichia coli, ebgabcde, and by ebgabcd, a 'second-generation' evolvant containing two supposedly 'kinetically silent |
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Q37059813 | Functions of the gene products of Escherichia coli. |
Q42021013 | Large changes of transition-state structure during experimental evolution of an enzyme |
Q42987018 | Larger increases in sensitivity to paracatalytic inactivation than in catalytic competence during experimental evolution of the second beta-galactosidase of Escherichia coli |
Q37056213 | Linkage map of Escherichia coli K-12, edition 8 |
Q33847662 | Mechanisms of stationary phase mutation: a decade of adaptive mutation |
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Q41819829 | On the specificity of adaptive mutations. |
Q39494235 | Spectra of spontaneous growth-dependent and adaptive mutations at ebgR. |
Q24532456 | Spontaneous point mutations that occur more often when advantageous than when neutral |
Q34351811 | The catalytic consequences of experimental evolution. Studies on the subunit structure of the second (ebg) beta-galactosidase of Escherichia coli, and on catalysis by ebgab, an experimental evolvant containing two amino acid substitutions |
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