ChemInform Abstract: Synthesis of Amino Acids and Related Compounds. Part 44. A Facile Preparation of Amino(diethoxyphosphoryl)acetic Esters: Transformation of Phosphoranes to Phosphonic Esters.

ChemInform ◽  
2010 ◽  
Vol 27 (35) ◽  
pp. no-no
Author(s):  
M. SEKI ◽  
K. MATSUMOTO
Keyword(s):  
Amino Acids ◽  
Facile Preparation ◽  
Related Compounds

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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