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Synthesis of malformin by an enzyme preparation from Aspergillus niger
Abstract:
Yukioka, M. (University of Hawaii, Honolulu), and T. Winnick. Synthesis of malformin by an enzyme preparation from Aspergillus niger. J. Bacteriol. 91:2237-2244. 1966.-An enzyme fraction derived from disrupted Aspergillus cells was able to utilize each of the component labeled amino acids of malformin for the synthesis of this cyclic pentapeptide. The process was stimulated by adenosine triphosphate, K(+), and Mg(++), and was optimal at approximately pH 8.5. It was not affected by inhibitors of protein synthesis (ribonuclease, chloramphenicol, puromycin). There is evidence that cysteine, rather than cystine, was incorporated into peptide linkage, so that the disulfide bridge of malformin was formed subsequently. Although only the d isomers of cysteine and leucine occur in the malformin molecule, the l, as well as the d form of these amino acids, was readily utilized by the enzyme preparation. As in the case of several other microbial peptide systems, it appears that the d enantiomorph can arise from the l isomer at an intermediate stage of polypeptide synthesis.
Insights
Researchers discovered an enzyme from Aspergillus niger that synthesizes the cyclic pentapeptide malformin using amino acids. This process is energy-dependent and does not involve typical protein synthesis machinery.
Area of Science:
- Biochemistry
- Microbiology
- Enzymology
Background:
- Malformin is a cyclic pentapeptide produced by Aspergillus niger.
- The biosynthesis pathway of malformin was not fully understood.
Purpose of the Study:
- To investigate the enzymatic synthesis of malformin.
- To elucidate the role of amino acids and cofactors in malformin production.
Main Methods:
- Utilized a cell-free enzyme preparation from Aspergillus niger.
- Employed labeled amino acids to track incorporation into malformin.
- Assessed the effects of cofactors (ATP, K+, Mg++) and pH on the synthesis.
Main Results:
- An enzyme fraction synthesized malformin from component amino acids.
- Adenosine triphosphate, K+, and Mg++ stimulated the synthesis, optimal at pH 8.5.
- Inhibitors of protein synthesis did not affect malformin production.
- Evidence suggests cysteine incorporation followed by disulfide bridge formation.
- Both L- and D-isomers of cysteine and leucine were utilized, indicating potential D-isomer formation from L-isomers.
Conclusions:
- Aspergillus niger possesses an enzyme system for direct malformin synthesis.
- The pathway differs from canonical protein synthesis, involving post-translational disulfide bond formation.
- The system can interconvert L-amino acids to D-amino acids during synthesis.
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