SB-203207 and SB-203208, Too Novel Isoleucyl tRNA Synthetase Inhibitors from a Streptomyces sp. II. Structure Determination.

Houge‐Frydrych, Catherine S. V.; Gilpin, Martin L.; Skett, Peter W.; Tyler, John W.

doi:10.7164/antibiotics.53.364

Cited by 49 publications

(35 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the presence of Pb(OAc)4, amide 15 evolved into the final isocyanate 16 through the Baumgarten variant of the Hoffmann rearrangement. SB-203207 (25), an alkaloid isolated from a Streptomices species by researchers in the SmithKline Beecham group, was found to show marked isoleucyl tRNA synthetase inhibition activity [39,40]. Very recently, Kan and co-workers described a total synthesis of this compound starting from lactam 22, in which the primary amide unit was generated by catalytic hydration of nitrile intermediate 23 with complex 1 (Scheme 8) [41].…”

Section: Preparation Of Complex [Pth{(pme 2 O) 2 H}(pme 2 Oh)] Firstmentioning

confidence: 99%

“…As shown in the scheme, almost quantitative yields were achieved in both cases, performing the reactions at 80 °C with low catalyst loading (5 mol%). In the context of their synthetic studies on the icetaxane family of diterpenoids, the hydration of nitrile 38 by complex 1 was successfully employed by Sarpong and co-workers to prepare primary amide 39, from which the formal synthesis of icetexone (40) and epi-icetexone (41) could be completed (Scheme 11) [51,52]. Figure 3) has attracted a great deal of attention since its discovery in 2004 due to its complex architecture, biological properties, and paucity in nature.…”

Section: Preparation Of Complex [Pth{(pme 2 O) 2 H}(pme 2 Oh)] Firstmentioning

confidence: 99%

See 1 more Smart Citation

Synthetic Applications of the Parkins Nitrile Hydration Catalyst [PtH{(PMe2O)2H}(PMe2OH)]: A Review

Cadierno

2015

Applied Sciences

View full text Add to dashboard Cite

Abstract:The air-stable hydride-platinum(II) complex [PtH{(PMe2O)2H}(PMe2OH)], reported by Parkins and co-workers in 1995, is the most versatile catalyst currently available for the hydration of C≡N bonds. It features remarkable activity under relatively mild conditions and exceptionally high functional group compatibility, facts that have allowed the implementation of this complex in the synthesis of a large number of structurally complex, biologically active molecules and natural products. In this contribution, synthetic applications of the Parkins catalyst are reviewed.

show abstract

Section: Preparation Of Complex [Pth{(pme 2 O) 2 H}(pme 2 Oh)] Firstmentioning

confidence: 99%

Section: Preparation Of Complex [Pth{(pme 2 O) 2 H}(pme 2 Oh)] Firstmentioning

confidence: 99%

Synthetic Applications of the Parkins Nitrile Hydration Catalyst [PtH{(PMe2O)2H}(PMe2OH)]: A Review

Cadierno

2015

Applied Sciences

View full text Add to dashboard Cite

show abstract

“…CNB-091 [60] and daldinin F from Hypoxylonfuscum [61]. Likewise, βMePhe is an unusual non-proteinogenic amino acid previously described as part of the altemicidin derivative SB-203208 [62], bottromycins [63], AK toxin [64], homaomycin [65] and mannopeptimycin [66]. However, only the latter two compounds share with JAs the 3R configuration of the βMePhe stereocenter.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the Jomthonic Acids Biosynthesis Pathway and Isolation of Novel Analogues in Streptomyces caniferus GUA-06-05-006A

et al. 2018

View full text Add to dashboard Cite

Jomthonic acids (JAs) are a group of natural products (NPs) with adipogenic activity. Structurally, JAs are formed by a modified β-methylphenylalanine residue, whose biosynthesis involves a methyltransferase that in Streptomyces hygroscopicus has been identified as MppJ. Up to date, three JA members (A–C) and a few other natural products containing β-methylphenylalanine have been discovered from soil-derived microorganisms. Herein, we report the identification of a gene (jomM) coding for a putative methyltransferase highly identical to MppJ in the chromosome of the marine actinobacteria Streptomyces caniferus GUA-06-05-006A. In its 5’ region, jomM clusters with two polyketide synthases (PKS) (jomP1, jomP2), a nonribosomal peptide synthetase (NRPS) (jomN) and a thioesterase gene (jomT), possibly conforming a single transcriptional unit. Insertion of a strong constitutive promoter upstream of jomP1 led to the detection of JA A, along with at least two novel JA family members (D and E). Independent inactivation of jomP1, jomN and jomM abolished production of JA A, JA D and JA E, indicating the involvement of these genes in JA biosynthesis. Heterologous expression of the JA biosynthesis cluster in Streptomyces coelicolor M1152 and in Streptomyces albus J1074 led to the production of JA A, B, C and F. We propose a pathway for JAs biosynthesis based on the findings here described.

show abstract

“…[1][2][3][4] (2S,3S)-b-Methylphenylalanine (bmPhe) is a nonproteinogenic residue in mannopepti-A C H T U N G T R E N N U N G mycin (produced by Streptomyces hygroscopicus NRRL3085) and is occasionally found in some other secondary metabolites. [5] Mannopeptimycin mainly consists of three mannose units and a six-membered cyclic peptide core, in which yet another unusual amino acid, b-hydroxy-enduracididine (bhEnd, Scheme 1 A), can be found. [6,7] Mannopeptimycin has drawn much attention because it is a potent drug lead.…”

Section: Introductionmentioning

confidence: 99%

In vitro Characterization of Enzymes Involved in the Synthesis of Nonproteinogenic Residue (2S,3S)‐β‐Methylphenylalanine in Glycopeptide Antibiotic Mannopeptimycin

et al. 2009

View full text Add to dashboard Cite

Mannopeptimycin, a potent drug lead, has superior activity against difficult-to-treat multidrug-resistant Gram-positive pathogens such as methicillin-resistant Staphylococcus aureus (MRSA). (2S,3S)-beta-Methylphenylalanine is a residue in the cyclic hexapeptide core of mannopeptimycin, but the synthesis of this residue is far from clear. We report here on the reaction order and the stereochemical course of reaction in the formation of (2S,3S)-beta-methylphenylalanine. The reaction is executed by the enzymes MppJ and TyrB, an S-adenosyl methionine (SAM)-dependent methyltransferase and an (S)-aromatic-amino-acid aminotransferase, respectively. Phenylpyruvic acid is methylated by MppJ at its benzylic position at the expense of one equivalent of SAM. The resulting beta-methyl phenylpyruvic acid is then converted to (2S,3S)-beta-methylphenylalanine by TyrB. MppJ was further determined to be regioselective and stereoselective in its catalysis of the formation of (3S)-beta-methylphenylpyruvic acid. The binding constant (K(D)) of MppJ versus SAM is 26 microM. The kinetic constants with respect to k(cat Ppy) and K(M Ppy), and k(cat SAM) and K(M SAM) are 0.8 s(-1) and 2.5 mM, and 8.15 s(-1) and 0.014 mM, respectively. These results suggest SAM has higher binding affinity for MppJ than Ppy, and the C--C bond formation in betamPpy might be the rate-limiting step, as opposed to the C--S bond breakage in SAM.

show abstract

SB-203207 and SB-203208, Too Novel Isoleucyl tRNA Synthetase Inhibitors from a Streptomyces sp. II. Structure Determination.

Cited by 49 publications

References 9 publications

Synthetic Applications of the Parkins Nitrile Hydration Catalyst [PtH{(PMe2O)2H}(PMe2OH)]: A Review

Synthetic Applications of the Parkins Nitrile Hydration Catalyst [PtH{(PMe2O)2H}(PMe2OH)]: A Review

Characterization of the Jomthonic Acids Biosynthesis Pathway and Isolation of Novel Analogues in Streptomyces caniferus GUA-06-05-006A

In vitro Characterization of Enzymes Involved in the Synthesis of Nonproteinogenic Residue (2S,3S)‐β‐Methylphenylalanine in Glycopeptide Antibiotic Mannopeptimycin

Contact Info

Product

Resources

About