| Characterization of three-fraction mycobacillin synthetase. | |
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MedLine Citation:
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PMID: 3753434 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Mycobacillin synthetase lacks aspartic acid racemase, alanine racemase and glutamic acid racemase activities. The enzyme also does not respond to ATP-[32P]Pi exchange, nor does it catalyse the antibiotic synthesis in presence of amino acids of configuration opposite to that present in the molecule. Preincubation with optical isomers of opposite configuration inhibited the ATP-[32P]Pi exchange reaction to the extent of 60-90%. None of the three fractions of mycobacillin synthetase contained a pantothenic acid arm. Two molecules of ATP are required to synthesize one peptide bond of mycobacillin. Intermediate peptides of mycobacillin are not covalently linked to the three-fraction mycobacillin synthetase. |
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Authors:
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N K Mukhopadhyay; S Majumder; S K Ghosh; S K Bose |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Biochemical journal Volume: 235 ISSN: 0264-6021 ISO Abbreviation: Biochem. J. Publication Date: 1986 May |
Date Detail:
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Created Date: 1986-10-01 Completed Date: 1986-10-01 Revised Date: 2010-09-13 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 639-43 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphate
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metabolism Amino Acids / metabolism Multienzyme Complexes / metabolism* Mycobacillin / metabolism Peptide Synthases / metabolism* Phosphates / metabolism Protein Conformation Racemases and Epimerases / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Multienzyme Complexes; 0/Phosphates; 18524-67-9/Mycobacillin; 56-65-5/Adenosine Triphosphate; EC 5.1.-/Racemases and Epimerases; EC 6.3.2.-/Peptide Synthases; EC 6.3.2.-/mycobacillin synthetase |
| Comments/Corrections | |
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