 | | PRD_002555 | | Name: | Paenilamicin B2 | | Formula: | C42 H86 N16 O13 | | Description: | Nonribosomally synthesized peptide-polyketide hybrid | | Definition date: | 2024-07-24 | | Last modified: | 2024-07-24 |
|
 | | PRD_000727 | | Name: | PYOVERDIN G173 Fe Complex | | Formula: | C49 H66 Fe N13 O21 | | Description: | IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS
AERUGINOSA SECRETES A MAJOR FLUORESCENT
SIDEROPHORE NAMED PYOVERDIN (PVD),
WHICH AFTER CHELATING IRON(III) IS TRANSPORTED
BACK INTO THE CELL VIA ITS OUTER MEMBRANE RECEPTOR
FPVA. FPVA IS A TONB-DEPENDENT TRANSPORT PROTEIN
AND HAS THE ABILITY TO BIND PVD IN ITS APO-
OR IRON-LOADED FORM. | | Definition date: | 2012-12-12 | | Last modified: | 2023-11-03 |
|
 | | PRD_000117 | | Name: | ARYLOMYCIN A2 | | Formula: | C42 H60 N6 O11 | | Description: | ARYLOMYCIN A2 IS A BIARYL-BRIDGED LIPOPEPTIDE. THE SCAFFOLD IS MADE OF TWO PARTS: (1) N-TERM EXOCYCLIC TRIPEPTIDE (2)
A TRICYCLIC PEPTIDE, WITH [3,3] BIARYL BOND BETWEEN RESIDUE 4 AND 6 AN ISO-C12 FATTY ACID IS LINKED TO RESIDUE 1. | | Definition date: | 2012-12-12 | | Last modified: | 2023-09-20 |
|
 | | PRD_000223 | | Name: | THIOSTREPTON | | Formula: | C72 H84 N19 O18 S5 | | Description: | Thiostrepton is a hetrocyclic thiopeptide belonging to the
thiocillin family, consisting of four thiazole, one thiozoline and one
piperideine rings. A modified quinoline linked to main-chain residue 1
and side-chain of residue 12. Post translational maturation of
thiazole and oxazole containing antibiotics involves the enzymic
condensation of a Cys or Ser with the alpha-carbonyl of the preceding
amino acid to form a thioether or ether bond, then dehydration to form
a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline
ring are dehydrogenated to form thiazole or oxazole rings. the
pyridinyl involves the cross-linking of a Ser and a Cys-Ser pair
usually separated by 7 or 8 residues along the peptide chain. The Ser
residues are dehydrated to didehydroalanines, then bonded between
their beta carbons. The alpha carbonyl of the Cys condenses with alpha
carbon of the first Ser to form a pyridinyl ring. The ring may be
mutiply dehydrogenated to form a pyridine ring with loss of the amino
nitrogen of the first Ser. The amidation of Ser-17 probably does not
occur by the same mechanism, oxidative cleavage of glycine, as in
eukaryotes. | | Definition date: | 2012-12-12 | | Last modified: | 2023-09-20 |
|
 | | PRD_000225 | | Name: | GE2270a | | Formula: | C56 H58 N15 O10 S6 | | Description: | GEA2270A IS A THIOPEPTIDE CONSISTING OF ONE
PYRIDINE, ONE OXAZOLE AND FIVE THIAZOLE RINGS.
THE OBSERVED C-TERMINAL AMINO GROUP NH2(15) IS
LIKELY TO BE A POST-TRANSLATIONAL DECARBOXYLATED
REMNANT OF A SER C-TERMINAL RESIDUE. | | Definition date: | 2012-12-12 | | Last modified: | 2023-09-20 |
|
 | | PRD_000507 | | Name: | PYOVERDIN C-E CHROMOPHORE | | Formula: | C55 H86 N17 O22 | | Description: | IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS AERUGINOSA SECRETES A MAJOR FLUORESCENT SIDEROPHORE NAMED PYOVERDIN (PVD),
WHICH AFTER CHELATING IRON(III) IS TRANSPORTED BACK INTO THE CELL VIA ITS OUTER MEMBRANE RECEPTOR FPVA. FPVA IS A
TONB-DEPENDENT TRANSPORT PROTEIN AND HAS THE ABILITY TO BIND PVD IN ITS APO- OR IRON-LOADED FORM. | | Definition date: | 2012-12-12 | | Last modified: | 2023-09-20 |
|
 | | PRD_000723 | | Name: | PYOVERDIN C-E Fe Complex | | Formula: | C55 H82 Fe N17 O22 | | Description: | IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS
AERUGINOSA SECRETES A MAJOR FLUORESCENT
SIDEROPHORE NAMED PYOVERDIN (PVD),
WHICH AFTER CHELATING IRON(III) IS TRANSPORTED
BACK INTO THE CELL VIA ITS OUTER MEMBRANE RECEPTOR
FPVA. FPVA IS A TONB-DEPENDENT TRANSPORT PROTEIN
AND HAS THE ABILITY TO BIND PVD IN ITS APO-
OR IRON-LOADED FORM. | | Definition date: | 2012-12-12 | | Last modified: | 2023-09-20 |
|
 | | PRD_000724 | | Name: | PYOVERDIN 18-1 Fe Complex | | Formula: | C57 H84 Fe N17 O24 | | Description: | IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS
AERUGINOSA SECRETES A MAJOR FLUORESCENT
SIDEROPHORE NAMED PYOVERDIN (PVD),
WHICH AFTER CHELATING IRON(III) IS TRANSPORTED
BACK INTO THE CELL VIA ITS OUTER MEMBRANE RECEPTOR
FPVA. FPVA IS A TONB-DEPENDENT TRANSPORT PROTEIN
AND HAS THE ABILITY TO BIND PVD IN ITS APO-
OR IRON-LOADED FORM. | | Definition date: | 2012-12-12 | | Last modified: | 2023-09-20 |
|
 | | PRD_000725 | | Name: | PYOVERDIN R Fe Complex | | Formula: | C48 H64 Fe N15 O21 | | Description: | IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS
AERUGINOSA SECRETES A MAJOR FLUORESCENT
SIDEROPHORE NAMED PYOVERDIN (PVD),
WHICH AFTER CHELATING IRON(III) IS TRANSPORTED
BACK INTO THE CELL VIA ITS OUTER MEMBRANE RECEPTOR
FPVA. FPVA IS A TONB-DEPENDENT TRANSPORT PROTEIN
AND HAS THE ABILITY TO BIND PVD IN ITS APO-
OR IRON-LOADED FORM. | | Definition date: | 2012-12-12 | | Last modified: | 2023-09-20 |
|
 | | PRD_000726 | | Name: | PYOVERDIN 13525 Fe Complex | | Formula: | C49 H71 Fe N14 O19 | | Description: | IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS
AERUGINOSA SECRETES A MAJOR FLUORESCENT
SIDEROPHORE NAMED PYOVERDIN (PVD),
WHICH AFTER CHELATING IRON(III) IS TRANSPORTED
BACK INTO THE CELL VIA ITS OUTER MEMBRANE RECEPTOR
FPVA. FPVA IS A TONB-DEPENDENT TRANSPORT PROTEIN
AND HAS THE ABILITY TO BIND PVD IN ITS APO-
OR IRON-LOADED FORM. | | Definition date: | 2012-12-12 | | Last modified: | 2023-09-20 |
|
 | | PRD_000728 | | Name: | Synthetic PYOVERDINE Fe Complex | | Formula: | C56 H81 Fe N17 O24 | | Description: | IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS
AERUGINOSA SECRETES A MAJOR FLUORESCENT
SIDEROPHORE NAMED PYOVERDIN (PVD),
WHICH AFTER CHELATING IRON(III) IS TRANSPORTED
BACK INTO THE CELL VIA ITS OUTER MEMBRANE RECEPTOR
FPVA. FPVA IS A TONB-DEPENDENT TRANSPORT PROTEIN
AND HAS THE ABILITY TO BIND PVD IN ITS APO-
OR IRON-LOADED FORM. | | Definition date: | 2012-12-12 | | Last modified: | 2023-09-20 |
|
 | | PRD_000813 | | Name: | Glyco-Arylomycin | | Formula: | C53 H78 N6 O16 | | Description: | BAL4850C IS A VARIANT OF THE LIPOGLYCO ARYLOMYCIN HERE BAL4850C IS REPRESENTED BY GROUPING TOGETHER THE SEQUENCE, THE LIPID (O2U) AND RHAMNOSE. | | Definition date: | 2012-12-12 | | Last modified: | 2013-07-02 |
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