scholarly journals Identification and quantification of amino acids and related compounds based on Differential Mobility Spectrometry

The Analyst ◽  
2020 ◽  
Vol 145 (14) ◽  
pp. 4889-4900 ◽  
Author(s):  
Francis Berthias ◽  
Yali Wang ◽  
Eskander Alhajji ◽  
Bernard Rieul ◽  
Fathi Moussa ◽  
...  
Keyword(s):  
Amino Acids ◽  
Metabolic Diseases ◽  
Differential Mobility Spectrometry ◽  
Differential Mobility ◽  
Related Compounds ◽  
Identification And Quantification

A new metabolite descriptor allowing fast quantification for the diagnosis of metabolic diseases.

scholarly journals Directed Evolution of Biphenyl Dioxygenase: Emergence of Enhanced Degradation Capacity for Benzene, Toluene, and Alkylbenzenes

2001 ◽  
Vol 183 (18) ◽  
pp. 5441-5444 ◽  
Author(s):  
Hikaru Suenaga ◽  
Mariko Mitsuoka ◽  
Yuko Ura ◽  
Takahito Watanabe ◽  
Kensuke Furukawa
Keyword(s):  
Amino Acids ◽  
Aromatic Hydrocarbons ◽  
Burkholderia Cepacia ◽  
Large Subunit ◽  
Site Directed Mutagenesis ◽  
Biphenyl Dioxygenase ◽  
Pseudomonas Pseudoalcaligenes ◽  
Benzene Toluene ◽  
Related Compounds ◽  
Enhanced Degradation

ABSTRACT Biphenyl dioxygenase (Bph Dox) catalyzes the initial oxygenation of biphenyl and related compounds. Bph Dox is a multicomponent enzyme in which a large subunit (encoded by the bphA1 gene) is significantly responsible for substrate specificity. By using the process of DNA shuffling of bphA1 of Pseudomonas pseudoalcaligenes KF707 and Burkholderia cepaciaLB400, a number of evolved Bph Dox enzymes were created. Among them, anEscherichia coli clone expressing chimeric Bph Dox exhibited extremely enhanced benzene-, toluene-, and alkylbenzene-degrading abilities. In this evolved BphA1, four amino acids (H255Q, V258I, G268A, and F277Y) were changed from the KF707 enzyme to those of the LB400 enzyme. Subsequent site-directed mutagenesis allowed us to determine the amino acids responsible for the degradation of monocyclic aromatic hydrocarbons.

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