| Kinetic analysis of three activated phenylalanyl intermediates generated by the initiation module PheATE of gramicidin S synthetase. | |
MedLine Citation:
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PMID: 11330995 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The three-domain initiation module PheATE (GrsA) of Bacillus brevis gramicidin S synthetase catalyzes the activation, thiolation and epimerization of L-phenylalanine (L-Phe), the first amino acid incorporated into the decapeptide antibiotic gramicidin S. There are three activated intermediates in the PheATE catalyzed chemical pathway: L-phenylalanyl-adenosine-5'-monophosphate diester (L-Phe-AMP), L-Phe-S-4'-phosphopantetheine(Ppant)- and D-Phe-S-4'-Ppant-acyl enzyme. In this study, we examined PheATE in single-turnover catalysis using rapid chemical quench techniques. Kinetic modeling of the process of disappearance of the substrate L-Phe, transient appearance and disappearance of L-Phe-AMP and the ad seriatim formation and equilibration of the L- and D-Phe-S-Ppant-acyl enzyme adducts allowed evaluation of the microscopic rate constants for the three chemical reactions in the initiation module PheATE. This study provides the first transient-state kinetic analysis of a nonribosomal peptide synthetase (NRPS) module. |
Authors:
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L Luo; C T Walsh |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Biochemistry Volume: 40 ISSN: 0006-2960 ISO Abbreviation: Biochemistry Publication Date: 2001 May |
Date Detail:
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Created Date: 2001-05-01 Completed Date: 2001-07-26 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: United States |
Other Details:
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Languages: eng Pagination: 5329-37 Citation Subset: IM |
Affiliation:
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Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Monophosphate
/
analogs & derivatives,
metabolism Alanine / genetics Amino Acid Isomerases / genetics, metabolism* Amino Acid Motifs / genetics Aminoacylation* Apoenzymes / metabolism Bacillus / enzymology, genetics Carbon Radioisotopes Catalysis Gramicidin / biosynthesis* Histidine / genetics Holoenzymes / genetics, metabolism Kinetics Mutagenesis, Site-Directed Pantetheine / analogs & derivatives*, metabolism Peptide Chain Initiation, Translational* Phenylalanine / metabolism* Protein Structure, Tertiary / genetics |
| Grant Support | |
ID/Acronym/Agency:
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GM20011/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Apoenzymes; 0/Carbon Radioisotopes; 0/Holoenzymes; 0/phenylalanyl-AMP anhydride; 1405-97-6/Gramicidin; 2226-71-3/4'-phosphopantetheine; 496-65-1/Pantetheine; 56-41-7/Alanine; 61-19-8/Adenosine Monophosphate; 63-91-2/Phenylalanine; 71-00-1/Histidine; EC 5.1.1.-/Amino Acid Isomerases; EC 5.1.1.11/phenylalanine racemase (ATP-hydrolyzing) |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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