Functional characterization of constituent enzyme fractions of mycobacillin synthetase.
The enzyme fraction A, a constituent enzyme of the three-fraction enzyme mycobacillin synthetase, independently and sequentially activated five amino acids starting from L-proline, producing the pentapeptide Pro(Asp1,Glu1,Tyr1)Asp. The fractions B and C were unable to function independently. However, the fraction B synthesized the nonapeptide Pro(Asp3,Glu1,Tyr2,Ser1)Leu, sequentially activating the pentapeptide and next four amino acids, whereas the fraction C synthesized mycobacillin by the sequential activation of the nonapeptide and the remaining four amino acids. The pH optima of the above enzymes are almost identical (pH 7.8), but their Km values are a little different.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009097:Multienzyme Complexes / Q000378:metabolism*; D009158:Mycobacillin / Q000096:biosynthesis; D010452:Peptide Biosynthesis; D010453:Peptide Synthases / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism
D000596:Amino Acids; D009097:Multienzyme Complexes; D010710:Phosphates; D009158:Mycobacillin; D000255:Adenosine Triphosphate; D010453:Peptide Synthases; C042173:mycobacillin synthetase