Substrate specificity of chlorophenoxyalkanoic acid-degrading bacteria is not dependent upon phylogenetically related tfdA gene types

2001 ◽  
Vol 33 (6) ◽  
pp. 507-513 ◽  
Author(s):  
Christopher Smejkal ◽  
Tatiana Vallaeys ◽  
Sara Burton ◽  
Hilary Lappin-Scott
Keyword(s):  
Substrate Specificity ◽  
Degrading Bacteria ◽  
Tfda Gene

Isolation and description of carbazole-degrading bacteria

1996 ◽  
Vol 42 (1) ◽  
pp. 79-82 ◽  
Author(s):  
Joanna Shotbolt-Brown ◽  
David W. F. Hunter ◽  
Jackie Aislabie
Keyword(s):  
Substrate Specificity ◽  
Fossil Fuels ◽  
Bacterial Isolates ◽  
Enrichment Cultures ◽  
Plate Assay ◽  
Degrading Bacteria

Carbazole is a nitrogen hetrocyclic compound associated with fossil fuels and their products. Enrichment cultures were established to isolate bacteria able to degrade carbazole and a plate assay was developed to select carbazole-degrading microorganisms from the enrichments. Three different bacterial isolates capable of mineralizing carbazole were obtained. No intermediates of carbazole degradation were detected. The bacteria had a limited substrate specificity; all used benzoate for growth but were unable to utilize the analogues of carbazole, fluorene, or dibenzothiophene.Key words: carbazole, biodegradation, bacteria.

scholarly journals Isolation and Characterization of Halotolerant 2,4- Dichlorophenoxyacetic Acid Degrading Bacteria From Sulfidic, Low Salinity Salt Springs

Fine Focus ◽  
2014 ◽  
Vol 1 (1) ◽  
pp. 39-50
Author(s):  
Michael G. Willis ◽  
David S. Treves
Keyword(s):  
Bacterial Communities ◽  
Dichlorophenoxyacetic Acid ◽  
Growth Strategies ◽  
Low Salinity ◽  
Isolation And Characterization ◽  
Degrading Bacteria ◽  
History Of ◽  
2,4 Dichlorophenoxyacetic Acid ◽  
Tfda Gene

The bacterial communities at two sulfidic, low salinity springs with no history of herbicide contamination were screened for their ability to grow on 2,4-dichlorophenoxyacetic acid (2,4-D). Nineteen isolates, closely matching the genera Bacillus, Halobacillus, Halomonas, Georgenia and Kocuria, showed diverse growth strategies on NaCl-supplemented and NaCl-free 2,4-D medium. The majority of isolates were halotolerant, growing best on nutrient rich broth with 0% or 5% NaCl; none of the isolates thrived in medium with 20% NaCl. The tfdA gene, which codes for an a – ketoglutarate dioxygenase and catalyzes the first step in 2,4-D degradation, was detected in nine of the salt spring isolates. The tfdAa gene, which shows ~60% identity to tfdA, was present in all nineteen isolates. Many of the bacteria described here were not previously associated with 2,4-D degradation suggesting these salt springs may contain microbial communities of interest for bioremediation.

Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Recent Work ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Transforming Growth Factor ◽  
Intrinsic Activity ◽  
Converting Enzyme ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.

Substrate Specificity of Leukocyte and Platelet Elastases

1978 ◽  
Vol 39 (03) ◽  
pp. 785-786 ◽  
Author(s):  
Y Legrand ◽  
J Caen ◽  
L Robert
Keyword(s):  
Substrate Specificity

PRKACA mutations in adrenal Cushing can alter substrate specificity

2017 ◽  
Author(s):  
Kerstin Bathon ◽  
Isabel Weigand ◽  
Jens T Vanselow ◽  
Cristina L Ronchi ◽  
Dalmazi Guido Di ◽  
...  
Keyword(s):  
Substrate Specificity
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