M. Auxiliadora Prieto

M. Auxiliadora Prieto

orcid

Research Focus & Metrics

Academic Career Length

30Years (1997-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 December 2001 in Microbiology and Molecular Biology Reviews
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EDEduardo Díaz
Eduardo Díaz
AFAbel Ferrández
Abel Ferrández
MPM. Auxiliadora Prieto
M. Auxiliadora Prieto
JGJosé Luis García
José Luis García
SUMMARY: Although Escherichia coli has long been recognized as the best-understood living organism, little was known about its abilities to use aromatic compounds as sole carbon and energy sources. This review gives an extensive overview of the current knowledge of the catabolism of aromatic compounds by E. coli. After giving a general overview of the aromatic compounds that E. coli strains encounter and mineralize in the different habitats that they colonize, we provide an up-to-date status report on the genes and proteins involved in the catabolism of such compounds, namely, several aromatic acids (phenylacetic acid, 3- and 4-hydroxyphenylacetic acid, phenylpropionic acid, 3-hydroxyphenylpropionic acid, and 3-hydroxycinnamic acid) and amines (phenylethylamine, tyramine, and dopamine). Other enzymatic activities acting on aromatic compounds in E. coli are also reviewed and evaluated. The review also reflects the present impact of genomic research and how the analysis of the whole E. coli genome reveals novel aromatic catabolic functions. Moreover, evolutionary considerations derived from sequence comparisons between the aromatic catabolic clusters of E. coli and homologous clusters from an increasing number of bacteria are also discussed. The recent progress in the understanding of the fundamentals that govern the degradation of aromatic compounds in E. coli makes this bacterium a very useful model system to decipher biochemical, genetic, evolutionary, and ecological aspects of the catabolism of such compounds. In the last part of the review, we discuss strategies and concepts to metabolically engineer E. coli to suit specific needs for biodegradation and biotransformation of aromatics and we provide several examples based on selected studies. Finally, conclusions derived from this review may serve as a lead for future research and applications.

11 February 2015 in Environmental Microbiology
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Journal Article
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MPM. Auxiliadora Prieto
M. Auxiliadora Prieto
IEIsabel F. Escapa
Isabel F. Escapa
VMVirginia Martínez
Virginia Martínez
NDNina Dinjaski
Nina Dinjaski
CHCristina Herencias
Cristina Herencias
OROlga Revelles
Olga Revelles

1 February 2000 in Journal of Bacteriology
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Journal Article
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BSBeatriz Galán Sicilia
Beatriz Galán Sicilia
EDEduardo Díaz
Eduardo Díaz
MPM. Auxiliadora Prieto
M. Auxiliadora Prieto
JGJosé Luis García
José Luis García
Escherichia coliW uses the aromatic compound 4-hydroxyphenylacetate (4-HPA) as a sole source of carbon and energy for growth. The monooxygenase which converts 4-HPA into 3,4-dihydroxyphenylacetate, the first intermediate of the pathway, consists of two components, HpaB (58.7 kDa) and HpaC (18.6 kDa), encoded by thehpaBandhpaCgenes, respectively, that form a single transcription unit. Overproduction of the small HpaC component inE. coliK-12 cells has facilitated the purification of the protein, which was revealed to be a homodimer that catalyzes the reduction of free flavins by NADH in preference to NADPH. Subsequently, the reduced flavins diffuse to the large HpaB component or to other electron acceptors such as cytochromecand ferric ion. Amino acid sequence comparisons revealed that the HpaC reductase could be considered the prototype of a new subfamily of flavin:NAD(P)H reductases. The construction of a fusion protein between the large HpaB oxygenase component and the choline-binding domain of the major autolysin ofStreptococcus pneumoniaeallowed us to develop a rapid method to efficiently purify this highly unstable enzyme as a chimeric CH-HpaB protein, which exhibited a 4-HPA hydroxylating activity only when it was supplemented with the HpaC reductase. These results suggest the 4-HPA 3-monooxygenase ofE. coliW as a representative member of a novel two-component flavin-diffusible monooxygenase (TC-FDM) family. Relevant features on the evolution and structure-function relationships of these TC-FDM proteins are discussed.

25 August 2015 in Microbial Biotechnology
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NWNick Wierckx
Nick Wierckx
MPM. Auxiliadora Prieto
M. Auxiliadora Prieto
PPPablo Pomposiello
Pablo Pomposiello
VLVictor De Lorenzo
Victor De Lorenzo
KOKevin O'COnnor
Kevin O'COnnor
Lars M. BlankLars M. Blank
Lars M. Blank
4 p.The authors have received funding from the\ud European Union’s Horizon 2020 research and innovation programme\ud under grant agreement no. 633962 for the project P4SB.Peer reviewe

8 November 2018 in Microbial Biotechnology
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ODOliver Drzyzga
Oliver Drzyzga
MPM. Auxiliadora Prieto
M. Auxiliadora Prieto

25 August 2017 in Microbial Biotechnology
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KTKenneth Timmis
Kenneth Timmis
WVWillem M. de Vos
Willem M. de Vos
JRJuan Luis Ramos
Juan Luis Ramos
SVSiegfried Vlaeminck
Siegfried Vlaeminck
MPM. Auxiliadora Prieto
M. Auxiliadora Prieto
BSBrajesh K. Singh
Brajesh K. Singh
The signature and almost unique characteristic of microbial technology is the exceptional diversity of applications it can address, and the exceptional range of human activities and needs to which it is and can be applied. Precisely because sustainability goals have very diverse and complex components and requirements, microbial technology has the ability to contribute substantively on many levels in many arenas to global efforts to achieve sustainability. Indeed, microbial technology could be viewed as a unifying element in our progress towards sustainability.