Proteinchemical and kinetic features of gramicidin S synthetase.
The amino-acid compositions of both enzymes of gramicidin S synthetase were determined. These proteins contain a high number of acidic amino-acid residues. Phenylalanine racemase, the light enzyme, was sequenced from the N-terminus until position 10. The kinetics of the thioester formation reactions were studied. The half-life times of these processes under substrate saturation conditions were found in the range between seconds and a few minutes. The valine activation at the heavy enzyme was detected as one of the rate-limiting steps of the biosynthesis of gramicidin S.
Vater
J
J
Institut für Biochemie und Molekulare Biologie, Technische Universität Berlin.
Schlumbohm
W
W
Salnikow
J
J
Irrgang
K D
KD
Miklus
M
M
Choli
T
T
Kleinkauf
H
H
D000591:Amino Acid Isomerases / Q000032:analysis / Q000378:metabolism*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000032:analysis / Q000378:metabolism*; D010453:Peptide Synthases / Q000032:analysis / Q000378:metabolism*; D013438:Sulfhydryl Compounds
D000596:Amino Acids; D009097:Multienzyme Complexes; D013438:Sulfhydryl Compounds; D000591:Amino Acid Isomerases; C022343:phenylalanine racemase (ATP-hydrolyzing); D010453:Peptide Synthases; C020831:gramicidin-S-synthetase 2