Literature DB >> 22461423

Thermal bifunctionality of bacterial phenylalanine aminomutase and ammonia lyase enzymes.

Christopher Chesters1, Matthew Wilding, Mark Goodall, Jason Micklefield.   

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Year:  2012        PMID： 22461423     DOI： 10.1002/anie.201200669

Source DB:  PubMed          Journal:  Angew Chem Int Ed Engl        ISSN： 1433-7851            Impact factor:   15.336


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  4 in total

1.  Directed evolution of Anabaena variabilis phenylalanine ammonia-lyase (PAL) identifies mutants with enhanced activities.

Authors:  Zachary Js Mays; Karishma Mohan; Vikas D Trivedi; Todd C Chappell; Nikhil U Nair
Journal:  Chem Commun (Camb)       Date:  2020-04-09       Impact factor: 6.222

2.  A new member of the 4-methylideneimidazole-5-one-containing aminomutase family from the enediyne kedarcidin biosynthetic pathway.

Authors:  Sheng-Xiong Huang; Jeremy R Lohman; Tingting Huang; Ben Shen
Journal:  Proc Natl Acad Sci U S A       Date:  2013-04-30       Impact factor: 11.205

3.  Discovery and Investigation of Mutase-like Activity in a Phenylalanine Ammonia Lyase from Anabaena variabilis.

Authors:  Nicholas J Weise; Fabio Parmeggiani; Syed T Ahmed; Nicholas J Turner
Journal:  Top Catal       Date:  2018-01-25       Impact factor: 2.910

4.  Expression and properties of the highly alkalophilic phenylalanine ammonia-lyase of thermophilic Rubrobacter xylanophilus.

Authors:  Klaudia Kovács; Gergely Bánóczi; Andrea Varga; Izabella Szabó; András Holczinger; Gábor Hornyánszky; Imre Zagyva; Csaba Paizs; Beáta G Vértessy; László Poppe
Journal:  PLoS One       Date:  2014-01-27       Impact factor: 3.240
  4 in total

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