Similar articles for PMID: 1540130

Year	Number of Results
1959	1
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1976	4
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2000	2
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2016	1
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1

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.

Elliott AC, K S, Sinnott ML, Smith PJ, Bommuswamy J, Guo Z, Hall BG, Zhang Y. Elliott AC, et al. Biochem J. 1992 Feb 15;282 ( Pt 1)(Pt 1):155-64. doi: 10.1042/bj2820155. Biochem J. 1992. PMID: 1540130 Free PMC article.

2

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' mutations.

Krishnan S, Hall BG, Sinnott ML. Krishnan S, et al. Biochem J. 1995 Dec 15;312 ( Pt 3)(Pt 3):971-7. doi: 10.1042/bj3120971. Biochem J. 1995. PMID: 8554546 Free PMC article.

3

Catalysis by the large subunit of the second beta-galactosidase of Escherichia coli in the absence of the small subunit.

Calugaru SV, Hall BG, Sinnott ML. Calugaru SV, et al. Biochem J. 1995 Nov 15;312 ( Pt 1)(Pt 1):281-6. doi: 10.1042/bj3120281. Biochem J. 1995. PMID: 7492325 Free PMC article.

4

The catalytic consequences of experimental evolution. Transition-state structure during catalysis by the evolved beta-galactosidases of Escherichia coli (ebg enzymes) changed by a single mutational event.

Li BF, Holdup D, Morton CA, Sinnott ML. Li BF, et al. Biochem J. 1989 May 15;260(1):109-14. doi: 10.1042/bj2600109. Biochem J. 1989. PMID: 2505746 Free PMC article.

5

Experimental evolution of Ebg enzyme provides clues about the evolution of catalysis and to evolutionary potential.

Hall BG. Hall BG. FEMS Microbiol Lett. 1999 May 1;174(1):1-8. doi: 10.1111/j.1574-6968.1999.tb13542.x. FEMS Microbiol Lett. 1999. PMID: 10234816 Review.

6

Changes in the substrate specificities of an enzyme during directed evolution of new functions.

Hall BG. Hall BG. Biochemistry. 1981 Jul 7;20(14):4042-9. doi: 10.1021/bi00517a015. Biochemistry. 1981. PMID: 6793063

7

Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 2. Reactions of the galactosyl-enzyme intermediate with alcohols and azide ion.

Richard JP, Westerfeld JG, Lin S, Beard J. Richard JP, et al. Biochemistry. 1995 Sep 19;34(37):11713-24. doi: 10.1021/bi00037a008. Biochemistry. 1995. PMID: 7547903

8

A solvent-isotope-effect study of proton transfer during catalysis by Escherichia coli (lacZ) beta-galactosidase.

Selwood T, Sinnott ML. Selwood T, et al. Biochem J. 1990 Jun 1;268(2):317-23. doi: 10.1042/bj2680317. Biochem J. 1990. PMID: 2114090 Free PMC article.

9

Evolution of a new enzymatic function by recombination within a gene.

Hall BG, Zuzel T. Hall BG, et al. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3529-33. doi: 10.1073/pnas.77.6.3529. Proc Natl Acad Sci U S A. 1980. PMID: 6774339 Free PMC article.

10

Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 4. Mechanism for reaction of nucleophiles with the galactosyl-enzyme intermediates of E461G and E461Q beta-galactosidases.

Richard JP, Huber RE, Heo C, Amyes TL, Lin S. Richard JP, et al. Biochemistry. 1996 Sep 24;35(38):12387-401. doi: 10.1021/bi961029b. Biochemistry. 1996. PMID: 8823174

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