Expression of an active adenylate-forming domain of peptide synthetases corresponding to acyl-CoA-synthetases
| Autor: | Yoen-Ok Lee, Henk van Liempt, Horst Kleinkauf, Hans von Döhren, Ralf Dieckmann |
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| Rok vydání: | 1995 |
| Předmět: |
Pantetheine
Stereochemistry Phenylalanine Molecular Sequence Data Biophysics Adenylate kinase Biology Acyl-CoA-synthetase medicine.disease_cause Biochemistry Peptide synthetase Phosphates chemistry.chemical_compound Adenosine Triphosphate Tyrocidine synthetase Structural Biology Tyrocidine Panthetheine Coenzyme A Ligases Genetics medicine Escherichia coli Amino Acid Sequence Binding site Amino Acids Peptide Synthases Molecular Biology Peptide sequence Sequence Deletion chemistry.chemical_classification Cofactor binding Binding Sites Sequence Homology Amino Acid CoA Cell Biology Adenosine Monophosphate Recombinant Proteins Amino acid chemistry Multienzyme |
| Zdroj: | FEBS letters. 357(2) |
| ISSN: | 0014-5793 |
| Popis: | Peptide synthetases and acyl-CoA-synthetases form acyl adenylates which are transferred to CoA or enzyme-bound pantetheine. To verify the existence of an adenylate domain in peptide synthetases, a 60.8 kDa fragment of tyrocidine 1-synthetase was constructed by a 1629 bp deletion, expressed in Escherichia coli, and characterized. The truncated multienzyme activated phenylalanine and substrate analogues with comparable kinetics as the over-expressed synthetase, as judged by ATP-[32P]PPi exchange reaction. Thus the N-terminal domain resembling an acyl-CoA-synthetase is an autonomous structural element. This N-terminal domain is followed by a cofactor binding domain, resembling acyl carrier proteins involved in polyketide formation. |
| Databáze: | OpenAIRE |
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