Structural analysis of new syringopeptins by tandem mass spectrometry.
New syringopeptins SP(SC)-1 and -2 were isolated from culture filtrates of phytopathogenic bacterium strain SC1 of Pseudomonas syringae pv. syringae. These syringopeptins were composed of a beta-hydroxy fatty acid, a long sequence of aliphatic amino acids. and a lactone moiety of eight amino acids. The amino acid sequences were deduced from a comparison of their tandem mass sepctra with those of known syringopeptins SP-22a and SP-25a. SP(SC)-1 and SP(SC)-2 resembled SP-22a, but differed from the latter by 3 amino acids.
Isogai
A
A
Graduate School of Biological Sciences, Nara Institute of Science and Technology, Japan.
Iguchi
H
H
Nakayama
J
J
Kusai
A
A
Takemoto
J Y
JY
Suzuki
A
A
D000595:Amino Acid Sequence; D003470:Culture Media; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000096:biosynthesis / Q000737:chemistry*; D011549:Pseudomonas / Q000737:chemistry / Q000378:metabolism*
D003470:Culture Media; D010456:Peptides, Cyclic; C095647:syringopeptin SP(SC)-1