These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Journal Abstract Search
93 related items for PubMed ID: 12686108
1. Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding. Capitani G, Eliot AC, Gut H, Khomutov RM, Kirsch JF, Grütter MG. Biochim Biophys Acta; 2003 Apr 11; 1647(1-2):55-60. PubMed ID: 12686108 [Abstract] [Full Text] [Related]
2. Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms. Huai Q, Xia Y, Chen Y, Callahan B, Li N, Ke H. J Biol Chem; 2001 Oct 12; 276(41):38210-6. PubMed ID: 11431475 [Abstract] [Full Text] [Related]
3. An insight into the sequential, structural and phylogenetic properties of banana 1-aminocyclopropane-1-carboxylate synthase 1 and study of its interaction with pyridoxal-5'-phosphate and aminoethoxyvinylglycine. Choudhury SR, Singh SK, Roy S, Sengupta DN. J Biosci; 2010 Jun 12; 35(2):281-94. PubMed ID: 20689184 [Abstract] [Full Text] [Related]
4. Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine. Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grütter MG. FEBS Lett; 2005 Apr 25; 579(11):2458-62. PubMed ID: 15848188 [Abstract] [Full Text] [Related]
5. Structural analysis of Pseudomonas 1-aminocyclopropane-1-carboxylate deaminase complexes: insight into the mechanism of a unique pyridoxal-5'-phosphate dependent cyclopropane ring-opening reaction. Karthikeyan S, Zhou Q, Zhao Z, Kao CL, Tao Z, Robinson H, Liu HW, Zhang H. Biochemistry; 2004 Oct 26; 43(42):13328-39. PubMed ID: 15491139 [Abstract] [Full Text] [Related]
6. The multiple roles of conserved arginine 286 of 1-aminocyclopropane-1-carboxylate synthase. Coenzyme binding, substrate binding, and beyond. Zhou H, Wang HW, Zhu K, Sui SF, Xu P, Yang SF, Li N. Plant Physiol; 1999 Nov 26; 121(3):913-9. PubMed ID: 10557240 [Abstract] [Full Text] [Related]
7. Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant. McCarthy DL, Capitani G, Feng L, Gruetter MG, Kirsch JF. Biochemistry; 2001 Oct 16; 40(41):12276-84. PubMed ID: 11591146 [Abstract] [Full Text] [Related]
8. S-methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthase. Ko S, Eliot AC, Kirsch JF. Arch Biochem Biophys; 2004 Jan 01; 421(1):85-90. PubMed ID: 14678788 [Abstract] [Full Text] [Related]
9. Specificity of S-adenosyl-L-methionine in the inactivation and the labeling of 1-aminocyclopropane-1-carboxylate synthase isolated from tomato fruits. Satoh S, Yang SF. Arch Biochem Biophys; 1989 May 15; 271(1):107-12. PubMed ID: 2712568 [Abstract] [Full Text] [Related]
10. Substitutions of alanine for cysteine at a reactive thiol site and for lysine at a pyridoxal phosphate binding site of 1-aminocyclopropane-1-carboxylate deaminase. Murakami T, Kiuchi M, Ito H, Matsui H, Honma M. Biosci Biotechnol Biochem; 1997 Mar 15; 61(3):506-9. PubMed ID: 9095553 [Abstract] [Full Text] [Related]
11. Avoiding the road less traveled: how the topology of enzyme-substrate complexes can dictate product selection. Eliot AC, Kirsch JF. Acc Chem Res; 2003 Oct 15; 36(10):757-65. PubMed ID: 14567709 [Abstract] [Full Text] [Related]
12. Aminotransferase activity and bioinformatic analysis of 1-aminocyclopropane-1-carboxylate synthase. Feng L, Geck MK, Eliot AC, Kirsch JF. Biochemistry; 2000 Dec 12; 39(49):15242-9. PubMed ID: 11106504 [Abstract] [Full Text] [Related]
13. Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus. Yao M, Ose T, Sugimoto H, Horiuchi A, Nakagawa A, Wakatsuki S, Yokoi D, Murakami T, Honma M, Tanaka I. J Biol Chem; 2000 Nov 03; 275(44):34557-65. PubMed ID: 10938279 [Abstract] [Full Text] [Related]
14. Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues. Eliot AC, Kirsch JF. Biochemistry; 2002 Mar 19; 41(11):3836-42. PubMed ID: 11888303 [Abstract] [Full Text] [Related]
15. Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms. White MF, Vasquez J, Yang SF, Kirsch JF. Proc Natl Acad Sci U S A; 1994 Dec 20; 91(26):12428-32. PubMed ID: 7809054 [Abstract] [Full Text] [Related]
16. Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate. Capitani G, McCarthy DL, Gut H, Grütter MG, Kirsch JF. J Biol Chem; 2002 Dec 20; 277(51):49735-42. PubMed ID: 12228256 [Abstract] [Full Text] [Related]
17. Inactivation of 1-Aminocyclopropane-1-Carboxylate Synthase by l-Vinylglycine as Related to the Mechanism-Based Inactivation of the Enzyme by S-Adenosyl-l-Methionine. Satoh S, Yang SF. Plant Physiol; 1989 Nov 20; 91(3):1036-9. PubMed ID: 16667107 [Abstract] [Full Text] [Related]
18. Kinetic and spectroscopic investigations of wild-type and mutant forms of apple 1-aminocyclopropane-1-carboxylate synthase. Li Y, Feng L, Kirsch JF. Biochemistry; 1997 Dec 09; 36(49):15477-88. PubMed ID: 9398277 [Abstract] [Full Text] [Related]
19. Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene. Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN. J Mol Biol; 1999 Dec 03; 294(3):745-56. PubMed ID: 10610793 [Abstract] [Full Text] [Related]
20. L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthase. Feng L, Kirsch JF. Biochemistry; 2000 Mar 14; 39(10):2436-44. PubMed ID: 10704193 [Abstract] [Full Text] [Related] Page: [Next] [New Search]