Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Drug
Enzyme
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Query: UNIPROT:P50583 (
asymmetrical
)
12,197
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The thermophilic bacterium Paenibacillus sp. A11-2, which can utilize dibenzothiophene (DBT) as the sole sulfur source at high temperature (45-55 degrees C), was investigated for its ability to cleave carbon-sulfur bonds in the dibenzothiophene (DBT) ring with
asymmetrical
alkyl substitution, such as methyl, dimethyl, trimethyl, ethyl and propyl DBTs. The biodesulfurization products of each of these alkylated DBTs (Cx-DBTs) were identified and quantitatively determined. The results suggested that each of the Cx-DBTs was desulfurized at a low rate, then converted to alkylated hydroxybiphenyls containing the isomers, and molar ratios of these metabolic isomers were altered in terms of not only the positions but also the numbers and lengths of the alkyl substituents. Moreover, these ratios were compared with those obtained using the mesophilic desulfurizing bacterium Rhodococcus erythropolis
KA2
-5-1. Consequently, biodesulfurization reactions of these microbes could be characterized using asymmetrically Cx-DBTs and their molecular shape parameters (length and length-to-breadth ratio), indicating differences in the selectivity of the microbial enzymic systems between the two bacterial strains.
...
PMID:Desulfurization characteristics of thermophilic Paenibacillus sp. strain A11-2 against asymmetrically alkylated dibenzothiophenes. 1623 84