Substrate tests

Biomass Main Substrate Tested HCHO (mg/L) ic50 (mg/L) Reference... 

The data reported identifies sulfur substrates tested for growth as sole sulfur source for the various strains. The strains may metabolize other sulfur compounds (not listed). A complete name of listed strains in Table 3 comprises Rhodococcus sp. SY1 Rhodococ-cus sp. H-2 Rhodococcus sp. D-l Rhodococcus ECRD-1 Gordona CYKS1 Nocar-dia sp. CYKS2 Paenibacillus All-2 Mycobacterium sp. WU-F1 Mycobacterium sp. WU-0103 Mycobacterium phlei sp. GTIS10 and Agrobacterium MC501. 

Polarographic studies of a mitochondrial fraction from Hymenolepis diminuta showed that of four substrates tested, DL-glycerol-3-phosphate was the most rapidly oxidized, but the highest respiratory control ratio (1.7) was obtained with dl-isocitric acid. With isocitrate as substrate oxyclozanide at 1.61 nM stimulated O uptake and relieved oligomycin inhibition of adinosine diphosphate-stimulated respiration, but at concentrations above 2 pM progressively inhibited O uptake. Rafoxanide, niclosamide, 3,4,5-tribromo-salicylanilide, nitroxynil, resorantel, di-chlorophen, and 2,4-dinitrophenol exhibited effects similar to those of oxyclozanide on the respiration in cestode mitochondria. The relative potencies were compared and the possible mode of action discussed [38]. 

The molecular masses of heme catalases are usually significantly higher as compared with peroxidases. If expressed in Lg-1s-1, rate constants for the Fem-TAML activators when compared with catalase from beef liver, which has a molecular weight 250,000 gmol-1 (Table IV, entry 13) (89), look very impressive, viz. 17 L g 1 s-1 for 11 vs. 22 L g 1 s 1 for the enzyme. Nevertheless, the catalase-like activity of the Fem-TAML activators can be suppressed by the addition of electron donors -it is negligible in the presence of the substrates tested in this work. In Nature, catalases display only minor peroxidase-like activity (79) because electron donors bulkier than H202 cannot access the deeply buried active sites of these massive enzymes (90). The comparatively unprotected Fem-TAML active sites are directly exposed to electron donors such that the overall behavior is determined by the inherent relative reactivity of the substrates. 

The substrates tested alone have substantially different values. Polycarbonate (1/4 inch) structural foam has an of 27.5, modified-polyphenylene oxide (1/4 inch), 84.4, and RIM polyurethane (1/2 inch), 173.3. These values compare with 164.4 for 1/4 inch hardboard and 139.1 for 1/4 inch plywood. A comparison of graphite, nickel, and copper/aciylic coatings on polycarbonate and modified-polyphenylene oxide substrates illustrate a dramatic result. Despite a factor of 3 difference in substrate performance, the Q and Fs values for the coated samples are very similar. The Q for the modified-polyphenylene oxide samples are 0.7 to 0.5 that of the uncoated sample. One would expect a similarity in Fs for the coated sample, but such a reduction in Q is dramatic. Both Q and Fs are determined by the 2 mil surface. 

Enzymes of the hepatic microsomes of most marine organisms, with the notable exception of certain molluscs, metabolize xeno-biotic substrates however, as much as 600-fold variations in enzyme activities have been noted between different species of marine teleosts (40). The hepatic enzyme activities of aquatic species are generally lower, with most substrates tested, than the hepatic enzymes of mammals (40). The mixed function oxidase enzymes in marine organisms are inducible by hydrocarbons, such as 3-methylcholanthrene or benzo[a]pyrene. Moreover, it is known... 

After extensive screening of various aldehydes to optimize the reaction conditions, it was found that aromatic aldehydes were able to serve as a carbon monoxide source, in which the electronic nature of the aldehydes is responsible for their ability to transfer CO efficiently [24]. Consequently, aldehydes bearing electron-withdrawing substituents are more effective than those bearing electron-donating substituents, with pentafluoro-benzaldehyde providing optimal reactivity. Interestingly, for all substrates tested the reaction is void of any complications from hydroacylation of either the alkene or alkyne of the enyne. Iridium and ruthenium complexes, which are known to decarboxylate aldehydes and catalyze the PK reaction, demonstrated inferior efficiency as compared to... 

Methyltransferase enzymes are widespread in the plant kingdom, but they are frequently very substrate specific. The substrate specificity of the methyl transferase from the onion enzyme system was tested with 18 different substrates (Table I). Pentachlorothiophenol was the best substrate tested however, four other substrates showed high levels of activity and only nine substrates showed less than 5% of the activity of pentachlorothiophenol. The three most active substrates were ortho substituted thlophenols. 

Another application of ruthenium indenylidene complexes was the atom transfer radical addition of carbon tetrachloride to vinyl monomers reported by Verpoort [61]. This Kharasch reaction afforded good yields for all substrates tested, especially with the catalyst VIII (Equation 8.11, Table 8.8). 

Figure 13.3 Amine substrates tested in the SCRAM -catalyzed racemization.

The PGase activity of the unknown enzyme preparation, in terms of reducing groups generated per unit time, is based on the corrected rate of increase in galacturonic acid equivalents for the experimental enzyme/substrate test solutions. One unit of enzyme activity (katals) is defined as that amount of enzyme that liberates I mole of reducing sugar per second under the defined conditions. 

Assays were carried out at 37° and pH 5.5. Each mixture contained 500 /imoles of sodium acetate, 5 /imoles of EDTA, 1.7 /ig of step VII phosphatase, and 20 /imoles of substrate in a volume of 5.0 ml. Controls lacking enzyme were run together with each of the substrates tested. At 1, 2, 5, 10, and 20 min, 500 /il portions were removed and added to 4.5 ml of 0.6 N H2SO4. Inorganic phosphatase was determined colorimetrically, and the initial rates were compared to that obtained with p-nitrophenyl phosphate. 

From the above, it is apparent that variables related to the substrate (test chemical), organism(s), or environment may affect rates of biodegradation. Table 12.3 summarizes the variables. 

The asymmetric hydrogenation of aryl ketones is an important step in the synthesis of many pharmaceutical intermediates. Blaser and co-workers showed that Ru complexes with Fe-cyclopentadienyl sandwich complexes are good catalysts for this reaction [63]. Figure 1.26 shows the different substrates tested, along with the time, conversion, and substrate/catalyst ratio. Using these data, calculate the catalyst TON and TOF in each case. 

Trypsin and factor Xa (fXa) are two members of the chymotrypsin family that have 38% sequence identity on the amino acid level and have distinguishable substrate specificities. Recently, the N-terminal 13-barrel of fXa and the C-terminal /3-barrel of trypsin were fused at a rationally designed site in the linker region between the two domains in order to create a hybrid fXa-trypsin protease (Hopfner et al., 1998). The fXa-trypsin hybrid was highly active and more active than either parent on three of the ten substrates assayed, as determined by k /Km. For most substrates, the activity of fXa-trypsin was an admixture of the two parents, probably because trypsin had higher activity than fXa for all the substrates tested. 

It is possible that a metabolite produced in liquid culture will not be produced at the same level on a solid substrate. Testing for metabolite production on solid medium is best achieved by application of the nutrients from the liquid medium to an inert solid, preferably one which could be used as a carrier for field application. 

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