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H Budzikiewicz

Publications and source records attributed to H Budzikiewicz.

87 records · Page 5Linked to original sources
PubMedDate not supplied

Can the peptide chain of a pyoverdin be bound by an ester bond to the chromophore?--The old problem of pseudobactin 7SR1.

The structure which had been proposed for the pyoverdin named pseudobactin 7SR1 (Yang and Leong, 1984) differed from those of all other pyoverdins investigated so far: its peptide chain was supposedly linked to the chromophore not by an amide bond originating from its N-terminal amino acid, but rather by an ester bond involving one of the three Ser. It will be shown that the peptide chain of pseudobactin 7SR1 is actually bound to the chromophore amidically by its N-terminal Ser and that it comprises a cyclodepsipeptidic substructure with an ester bond between the C-terminal Thr and the OH-group of the second Ser in the chain.

Esters↗
PubMedDate not supplied

The siderophores of Pseudomonas fluorescens 18.1 and the importance of cyclopeptidic substructures for the recognition at the cell surface.

The structure of the pyoverdin siderophore of Pseudomonas fluorescens 18.1 was elucidated by spectroscopic methods and chemical degradation. By cross feeding studies structurally closely related pyoverdins containing a C-terminal cyclopeptidic substructure were tested regarding the mutual recognition by the producing strains. Partial recognition of foreign pyoverdins was observed.

Amino Acid Sequence↗
PubMedDate not supplied

Anachelin, the siderophore of the cyanobacterium Anabaena cylindrica CCAP 1403/2A.

A catecholate siderophore - anachelin - has been isolated from the cyanobacterium Anabaena cylindrica CCAP 1403/2A. The central part of the siderophore is a tripeptide consisting of L-Thr, D-Ser and L-Ser. Its C-terminus is linked amidically to a 1,1-dimethyl-3-amino-1,2,3,4-tetrahydro-7,8-dihydroxyquinolinium system and its N-terminus to 6-amino-3,5,7-trihydroxyheptanoic acid. The 7-hydroxyl group of the latter is esterified with salicylic acid whose carboxyl group is condensed with the 6-amino group to an oxazoline ring. Anachelin is the first genuine siderophore of a cyanobacterium whose structure has been elucidated.

Anabaena↗
PubMedDate not supplied

The complex structure of ferri-ferribactins.

By comparison of the NMR data of the ferribactins from Pseudomonas chlororaphis ATCC 9446 and of P. fluorescens 18.1 with those of their Ga3+-complexes as models for the Fe3+-complexes it will be shown that only two bidentate ligands are provided for complexation, both located in the peptide chain. The two remaining free sites of the octahedral metal ion are probably occupied by solvent molecules.

Gallium↗
PubMedDate not supplied

A new pyoverdin from Pseudomonas aeruginosa R'.

From a Pseudomonas aeruginosa hospital isolate a new pyoverdin was isolated. It is identical with that of Pseudomonas aeruginosa strain R except that in the peptide chain L-Gln is missing.

Amino Acids↗
PubMedDate not supplied

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.

Amino Acid Sequence↗
PubMedDate not supplied

The structure of the pyoverdin isolated from various Pseudomonas syringae pathovars.

From seven different pathovars of Pseudomonas syringae representing various genetic subgroups, and one strain of Pseudomonas viridiflava the same pyoverdin siderophore (1) was isolated, probably identical with the pyoverdin whose amino acid composition (but not their sequence) had been reported before. 1 is the first pyoverdin where two of the ligands for Fe3+ are beta-hydroxy Asp units. Its remarkably high complexing constant for Fe3+ at pH 5 as compared with other pyoverdins offers a definite advantage in plant infection. The structure elucidation of 1 will be described and the taxonomical implications regarding pyoverdins with different structures ascribed previously to P. syringae strains will be discussed.

Amino Acid Sequence↗
PubMedDate not supplied

[Pseudobactin and pseudobactin A variants: new pyoverdin type peptide siderophores from Pseudomonas fluorescens "E2"].

From a strain of Pseudomonas fluorescens pseudobactin and several related compounds were isolated and their structures were elucidated. In this way a reference compound (5) could be obtained for the unambiguous determination of the absolute configuration of C-1 of the pyoverdin chromophore in newly isolated representatives of this class.

Amino Acid Sequence↗