Structure of Plumbemycin A and B, Antagonists ofl-Threonine fromStreptomyces plumbeus

Abstract

The structure of plumbemycin A and B, new antimetabolites from Streptomyces plumbeus, which are antagonist of L-threonine, were assigned to be L-a1any1-L-aspartyl-D-2-amino-5phosphono-3-cis-pentenoic acid and L-alanyl-L-asparaginyl-D-2-amino-5-phosphono-3-cispentenoic acid, respectively.

Synthesen, chemische Reaktionen und NMR‐spektroskopische Untersuchungen substituierter Phosphonopyruvate

“…:C49,24,H8,28,N5,. Aus 1,80 (4)) ;3,6 (m,(MeCHJ2N);4,04,2 (m. 2 MeCH20,). ',43 MHz,CDCI,): 12,4,14,O (23,(MeCH,),N); 12,7 (d, ,J(P,C) = 14,7, C(5)); 16,3 (cl, ,J(P,C) = 5 3 ,MeCH,O);40,0,42,4 (2s,(MeCH,) (4)) ;3,5 (m,(MeCHJ2N);4,054,15 (m,2 MeCH,O).…”

“…-In den letzten Jahren wurden einige Antibiotika sowie physiologisch aktive P-haltige Verbindungen wie Fosfomycin [ 11,Bialaphos,, Plumbemycin [3] und Fosfazinomycin [4] beschrieben, die als gemeinsames Strukturmerkmal eine (C-P)-Bindung aufweisen. Biosynthetische Studien [5] deuten darduf hin, dass beispielsweise die (C-P)-Bindung von Fosfomycin durch eine intramolekulare Umlagerung von 0 -Phosphoenolpyruvat ( = 2-(Phosphoryloxy)prop-2-enoat) 1 zu 3-Phosphonopyruvat ( = 2-0x0-3-phosphorylpropanoat) 2 gebildet wird (Schema I ).…”

Isolation of Indolmycin and Its Derivative as Antagonists ofl-Tryptophan

“…The seed culture thus obtained was transferred at a rate of 180 ml per flask into 5 IiterErlenmeyer's flasks each containing 1.8 liters of the same medium, and these flasks were incubated under rotatory cultivation at 30°C for 48 hr. (1) and 927-A substance (11).…”

Reassignment of the Structure of the Antibiotic A53868 Reveals an Unusual Amino Dehydrophosphonic Acid

“…Upon translocation, these peptides are hydrolyzed to release the active phosphonate-containing amino acids that target cellular enzymes such as glutamine and glutamate synthetase (phosphinothricin), [18,19] alanine racemase (alafosfalin), [20,21] or threonine synthase (plumbemycin). [22] Hydrolysis of the C-terminal peptide linkage of A53868 would result in an enamine that is expected to hydrolyze to methyl acetylphosphonate, which is a structural analogue of pyruvate and could inhibit pyruvate-utilizing enzymes. [23] On the other hand, the reactive vinyl phosphonate moiety in A53868 may inhibit a cellular process directly, analogous to the activity of the phosphonotripeptide K-26, which inhibits angiotensinconverting enzymes without the requirement of hydrolysis.…”