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. 2003 Feb;69(2):878–883. doi: 10.1128/AEM.69.2.878-883.2003

TABLE 1.

TPT degradation by solid-phase extract from fluorescent pseudomonads

Fluorescent pseudomonad TPT degradation activitya (μmol of product/μmol of pyoverdines) Peptide sequence of pyoverdineb Reference
P. chlororaphis CNR 15 0.37 Chr-S-K-G-FoOHOrn-c(K-FoOHOrn-S)c This study
P. chlororaphis ATCC 9446 0.23 Chr-S-K-G-FoOHOrn-c(K-FoOHOrn-S) 15
P. fluorescens ATCC 13525 0.55 Chr-S-K-G-FoOHOrn-c(K-FoOHOrn-S) 22
P. aeruginosa ATCC 15692 0.20 Chr-S-R-S-FoOHOrn-c(K-FoOHOrn-T-T) 6
P. aeruginosa NCIMB 5940 0.28 Chr-S-Dab-FoOHOrn-Q-O-FoOHOrn-G 26
P. aeruginosa NCIMB 12469 0.43 Chr-S-FoOHOrn-Orn-G-aT-S-cOHOrn 26
P. fluorescens NCIMB 10460 0.10 Chr-A-K-G-G-OHAsp-O/Dab-S-A-cOHOrn 5
a

The reaction mixture (400 μl) containing the solid-phase extract and 200 μM TPT was incubated for 12 h, and the total amount of DPT and monophenyltin produced was determined as the product. The concentration of pyoverdines in the solid-phase extract was estimated spectrophotometrically as described in Materials and Methods.

b

Italicized amino acid residues correspond to a d-configuration. Chr, common chromophore part of pyoverdine; aT, allothreonine; Q/Dab, a condensation product of 2,4-diaminobutyric acid and glutamine; c(amino acids), cyclic structure for the amino acids in parentheses.

c

The configurations of the amino acid residues were not determined in this study.