Document Detail

Characterization of three-fraction mycobacillin synthetase.
MedLine Citation:
PMID:  3753434     Owner:  NLM     Status:  MEDLINE    
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.
N K Mukhopadhyay; S Majumder; S K Ghosh; S K Bose
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  235     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1986 May 
Date Detail:
Created Date:  1986-10-01     Completed Date:  1986-10-01     Revised Date:  2010-09-13    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  639-43     Citation Subset:  IM    
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MeSH Terms
Adenosine Triphosphate / metabolism
Amino Acids / metabolism
Multienzyme Complexes / metabolism*
Mycobacillin / metabolism
Peptide Synthases / metabolism*
Phosphates / metabolism
Protein Conformation
Racemases and Epimerases / metabolism
Reg. No./Substance:
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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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