Conformational Changes during Enzyme Catalysis: Role of Water in the Transition State
The entropy of activation for the synthesis of Ile-tRNA is high and positive. The only likely source of a high Δ S‡is the loss of structured water as the enzyme· substrate complex moves toward the transition state. This requires a change in the orientation or nature of water-organizing residues in t...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1980-06, Vol.77 (6), p.3374-3378 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 77 |
| creator | Loftfield, Robert B. Eigner, E. Ann Pastuszyn, Andrzej Timo Nils Erik Lovgren Jakubowski, Hieronim |
| description | The entropy of activation for the synthesis of Ile-tRNA is high and positive. The only likely source of a high Δ S‡is the loss of structured water as the enzyme· substrate complex moves toward the transition state. This requires a change in the orientation or nature of water-organizing residues in the interface between the enzyme· substrate complex and the water. Such changes, which may be some distance from the ``active site,'' are coupled to the active site in such a way that the increased entropy and decreased free energy of the water-enzyme interface is available at the ``active site'' to reduce the free energy of activation. The effects of Hofmeister anions on Kms and kcats are consistent with the entropy data. |
| doi_str_mv | 10.1073/pnas.77.6.3374 |
| format | Article |
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Ann</creatorcontrib><creatorcontrib>Pastuszyn, Andrzej</creatorcontrib><creatorcontrib>Timo Nils Erik Lovgren</creatorcontrib><creatorcontrib>Jakubowski, Hieronim</creatorcontrib><title>Conformational Changes during Enzyme Catalysis: Role of Water in the Transition State</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The entropy of activation for the synthesis of Ile-tRNA is high and positive. The only likely source of a high Δ S‡is the loss of structured water as the enzyme· substrate complex moves toward the transition state. This requires a change in the orientation or nature of water-organizing residues in the interface between the enzyme· substrate complex and the water. Such changes, which may be some distance from the ``active site,'' are coupled to the active site in such a way that the increased entropy and decreased free energy of the water-enzyme interface is available at the ``active site'' to reduce the free energy of activation. The effects of Hofmeister anions on Kms and kcats are consistent with the entropy data.</description><subject>Acetates</subject><subject>Active sites</subject><subject>Amino Acyl-tRNA Synthetases - metabolism</subject><subject>Anions</subject><subject>Anions - pharmacology</subject><subject>Biochemistry</subject><subject>Chlorides</subject><subject>Entropy</subject><subject>Enzyme substrates</subject><subject>Enzymes</subject><subject>Isoleucine - metabolism</subject><subject>Isoleucine-tRNA Ligase - antagonists & inhibitors</subject><subject>Isoleucine-tRNA Ligase - metabolism</subject><subject>Kinetics</subject><subject>Mathematics</subject><subject>Models, Biological</subject><subject>Protein Conformation</subject><subject>RNA, Transfer, Amino Acyl - biosynthesis</subject><subject>Salts</subject><subject>Thermodynamics</subject><subject>Transfer RNA</subject><subject>Transfer RNA Aminoacylation</subject><subject>Water - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkc-L1DAUx4Mo6-zqVfAg5OStNU3zU_CwlF0VFgTdxWNIO68zXdJkTFJx_OttmXEYwdM7fD_f73u8L0KvKlJWRNbvdt6mUspSlHUt2RO0qoiuCsE0eYpWhFBZKEbZc3SZ0iMhRHNFLtCF0DUllK_QQxN8H-Jo8xC8dbjZWr-BhNdTHPwG3_jf-xFwY7N1-zSk9_hrcIBDj7_bDBEPHuct4PtofRqWCPwtz8IL9Ky3LsHL47xCD7c3982n4u7Lx8_N9V3RMc5zwVWrGYW20i2nPROUVzVvmSCUyVave9EJ3SmoGShJO61AsI5y0dM1g44xUV-hD4fc3dSOsO7A52id2cVhtHFvgh3Mv4oftmYTfpqaaVGp2f_26I_hxwQpm3FIHThnPYQpGcmpYETIGSwPYBdDShH6046KmKUHs_RgpDTCLD3Mhjfnl53w4-PPNi--v-rJb_rJuQy_8lnQf8FZf33QH1MO8QQopav6D06QpU8</recordid><startdate>19800601</startdate><enddate>19800601</enddate><creator>Loftfield, Robert B.</creator><creator>Eigner, E. 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Such changes, which may be some distance from the ``active site,'' are coupled to the active site in such a way that the increased entropy and decreased free energy of the water-enzyme interface is available at the ``active site'' to reduce the free energy of activation. The effects of Hofmeister anions on Kms and kcats are consistent with the entropy data.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>6932025</pmid><doi>10.1073/pnas.77.6.3374</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1980-06, Vol.77 (6), p.3374-3378 |
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| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Acetates Active sites Amino Acyl-tRNA Synthetases - metabolism Anions Anions - pharmacology Biochemistry Chlorides Entropy Enzyme substrates Enzymes Isoleucine - metabolism Isoleucine-tRNA Ligase - antagonists & inhibitors Isoleucine-tRNA Ligase - metabolism Kinetics Mathematics Models, Biological Protein Conformation RNA, Transfer, Amino Acyl - biosynthesis Salts Thermodynamics Transfer RNA Transfer RNA Aminoacylation Water - metabolism |
| title | Conformational Changes during Enzyme Catalysis: Role of Water in the Transition State |
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