Streptomyces chromofuscus

Goszczynski S, A Paszczynski, MB Pasti-Grigsby, RL Crawford, DL Crawford (1994) New pathways for degradation of sulfonated azo dyes by microbial peroxidases of Phanerochaete chrysosporium and Streptomyces chromofuscus. J Bacterial YIU. 1339-1347. 

Paszczynski A, Pasti-Grigsby MB, Goszczynski S et al (1992) Mineralization of sulfonated azo dyes and sulfanilic acid by Phanerochaete chrysosporium and Streptomyces chromofuscus. Appl Environ Microbiol 58 3598-3604... 

Extracellular peroxidases are produced by Streptomyces chromofuscus, with the capability to decolorize azo dyes associated to ligninolytic activity in aerobiosis. Azo dyes are converted to cationic radicals, which are subjected to nucleophilic attack by water or hydrogen peroxide molecules, producing reactive compounds that undergo redox reactions that result in a more stable intermediate [37]. 

In 1989, Kato et al. reported the isolation of carazostatin (247) from Streptomyces chromofuscus. Carazostatin represents a novel radical scavenger more active than butylated hydroxytoluene (BHT) (226). Moreover, it exhibits strong inhibitory activity against the free radical-induced, lipid peroxidation in liposomal membranes, and shows stronger antioxidant activity than ot-tocopherol (227). 

Phospholipase D. This enzyme will attack phosphatidylserine with the liberation of serine and formation of phosphatidic acid. The methodology is exactly the same as the one outlined in Chapter 4. The source of enzyme can be Streptomyces chromofuscus or cabbage, and products of its action are recovered in a chloroform-soluble and a water-soluble fraction. All of the lipid P should be in the chloroform-soluble fraction, and all of the serine should be in the water-soluble fraction. The phosphatidic acid can be identified by its thin-layer chromatographic behavior and its fast atom bombardment-mass spectrometric pattern. Serine can be identified by the procedures outlined earlier. 

A58365AandA58365B Streptomyces chromofuscus Inhibitors of angiotensin converting enzyme... 

A polyketide secondary metabolite, herboxidiene, produced by Streptomyces chromofuscus, shows potent and selective herbicidal activity [87] against weeds but not against wheat. Rice and soybean are more affected than wheat but are still relatively resistant to the microbial herbicide. 

In almost all of the transphosphatidylation reactions used in the synthesis of novel PLs, PLD from Streptomyces sp. has been used. Several reports showed PLD from cabbage, peanuts, and Streptomyces chromofuscus have low activity for transphosphatidylation [39,40,42,52], although they are able to transphosphatidylate PC to PE and PG. In these few reports, PLD from cabbage catalyzed transphosphatidylation with PC and ethanolamine derivatives [51]. Compared to PLD from Streptomyces sp., PLD from cabbage may possess a more rigid substrate specificity. 

A phospholipase D from Streptomyces chromofuscus has recently been reported to be an Fe " "-dependent enzyme with possible structural and mechanistic similarities to the purple acid phosphatases. ... 

Pentalenolactones. A group of sesquiterpene antibiotics, P. A-P, from Streptomyces chromofuscus, S. arenae, S. omiyaensis, S. UC 5319, and others. ... 

In contrast, Streptomyces chromofuscus was able to degrade only three of the five < es to CO, and the extent of degradation was only 1.1 - 3.6%. Nev iheless, this observation is significant, as it demonstrates that a complete pathway for the biodegradation of some azo dyes appears to exist in S. chromofuscus. Unlike P. chrysosporium, however, S. chromofuscus was unable to d ade -sulfanilic add to... 

L-Tryptophan metabolites have also been implicated in the biosynthesis of the two antibiotics questiomycin A (94) and questio-mycin B. Thus when ring labelled 3-hydroxykynurenine (88) was administered to Streptomyces chromofuscus, tJhe antibiotic (94) was found to incorporate the label to the same extent as o-aminophenol (questiomycin This result was interpreted to suggest that the side chain of 3-hydroxykynurenine (88) was eliminated prior to the oxidative condensation of two molecules to give questiomycin A (94). 

In what cellular compartment is NAPE localized Again, we can provide only a very partial answer to this question. Experiments in which the membranes of intact neurons were probed with bacterial PLD Streptomyces chromofuscus) suggest that a large portion of NAPE (at least 40%) is collected in the plasma membrane, where one would expect a precursor for an intercellular signaling molecule. " ... 

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