Year |
Citation |
Score |
2011 |
Schärer MA, Eliot AC, Grütter MG, Capitani G. Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy. Febs Letters. 585: 111-4. PMID 21075107 DOI: 10.1016/J.Febslet.2010.11.013 |
0.523 |
|
2005 |
Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grütter MG. Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine. Febs Letters. 579: 2458-62. PMID 15848188 DOI: 10.1016/J.Febslet.2005.03.048 |
0.602 |
|
2004 |
Eliot AC, Kirsch JF. Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Annual Review of Biochemistry. 73: 383-415. PMID 15189147 DOI: 10.1146/Annurev.Biochem.73.011303.074021 |
0.622 |
|
2004 |
Sandmark J, Eliot AC, Famm K, Schneider G, Kirsch JF. Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis. Biochemistry. 43: 1213-22. PMID 14756557 DOI: 10.1021/Bi0358059 |
0.684 |
|
2004 |
Ko S, Eliot AC, Kirsch JF. S-methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthase. Archives of Biochemistry and Biophysics. 421: 85-90. PMID 14678788 DOI: 10.1016/J.Abb.2003.10.017 |
0.675 |
|
2003 |
Eliot AC, Kirsch JF. Avoiding the road less traveled: how the topology of enzyme-substrate complexes can dictate product selection. Accounts of Chemical Research. 36: 757-65. PMID 14567709 DOI: 10.1021/Ar0202767 |
0.667 |
|
2003 |
Capitani G, Eliot AC, Gut H, Khomutov RM, Kirsch JF, Grütter MG. Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding. Biochimica Et Biophysica Acta. 1647: 55-60. PMID 12686108 DOI: 10.1016/S1570-9639(03)00049-9 |
0.647 |
|
2002 |
Eliot AC, Sandmark J, Schneider G, Kirsch JF. The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation. Biochemistry. 41: 12582-9. PMID 12379100 DOI: 10.1021/Bi026339A |
0.653 |
|
2002 |
Eliot AC, Kirsch JF. Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues. Biochemistry. 41: 3836-42. PMID 11888303 DOI: 10.1021/Bi016084L |
0.575 |
|
2000 |
Feng L, Geck MK, Eliot AC, Kirsch JF. Aminotransferase activity and bioinformatic analysis of 1-aminocyclopropane-1-carboxylate synthase. Biochemistry. 39: 15242-9. PMID 11106504 DOI: 10.1021/Bi002092A |
0.636 |
|
1999 |
Milne JC, Roy RS, Eliot AC, Kelleher NL, Wokhlu A, Nickels B, Walsh CT. Cofactor requirements and reconstitution of microcin B17 synthetase: a multienzyme complex that catalyzes the formation of oxazoles and thiazoles in the antibiotic microcin B17. Biochemistry. 38: 4768-81. PMID 10200165 DOI: 10.1021/Bi982975Q |
0.431 |
|
1998 |
Milne JC, Eliot AC, Kelleher NL, Walsh CT. ATP/GTP hydrolysis is required for oxazole and thiazole biosynthesis in the peptide antibiotic microcin B17. Biochemistry. 37: 13250-61. PMID 9748332 DOI: 10.1021/Bi980996E |
0.45 |
|
Show low-probability matches. |