The pyoverdins of Pseudomonas sp. 96-312 and 96-318.
The structures of the pyoverdins isolated from the Pseudomonas spp. 96-312 and 96-318 were elucidated by spectroscopic and degradation techniques. As observed before for Pseudomonas spp. producing pyoverdins with a C-terminal cyclopeptidic substructure, the two strains can recognize to some extent structurally different pyoverdins as long as they have also a similar cyclopeptidic C-terminus.
Schlegel
K
K
Institut für Organische Chemie der Universität zu Köln, Germany. aco88@uni-koeln.de
Fuchs
R
R
Schäfer
M
M
Taraz
K
K
Budzikiewicz
H
H
Geoffroy
V
V
Meyer
J M
JM
D000595:Amino Acid Sequence; D003619:Dansyl Compounds; D007501:Iron / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides; D010860:Pigments, Biological / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism; D011549:Pseudomonas / Q000145:classification / Q000502:physiology*; D017262:Siderophores / Q000737:chemistry / Q000378:metabolism
D003619:Dansyl Compounds; D009842:Oligopeptides; D010860:Pigments, Biological; D020033:Protein Isoforms; D017262:Siderophores; C042453:pyoverdin; D007501:Iron