Rhizophere analysis of auxin producers harboring the phenylpyruvate decarboxylase pathway

2022 ◽  
Vol 173 ◽  
pp. 104363
Author(s):  
Cécile Gruet ◽  
Andréa Oudot ◽  
Danis Abrouk ◽  
Yvan Moënne-Loccoz ◽  
Daniel Muller
1999 ◽  
Vol 10 (24) ◽  
pp. 4667-4675 ◽  
Author(s):  
Zhiwei Guo ◽  
Animesh Goswami ◽  
K.David Mirfakhrae ◽  
Ramesh N Patel

FEBS Journal ◽  
2007 ◽  
Vol 274 (9) ◽  
pp. 2363-2375 ◽  
Author(s):  
Wim Versées ◽  
Stijn Spaepen ◽  
Jos Vanderleyden ◽  
Jan Steyaert

FEBS Journal ◽  
2011 ◽  
Vol 278 (11) ◽  
pp. 1842-1853 ◽  
Author(s):  
Malea M. Kneen ◽  
Razvan Stan ◽  
Alejandra Yep ◽  
Ryan P. Tyler ◽  
Choedchai Saehuan ◽  
...  

2011 ◽  
Vol 11 (2) ◽  
pp. 238-249 ◽  
Author(s):  
Tânia Veiga ◽  
Daniel Solis-Escalante ◽  
Gabriele Romagnoli ◽  
Angela ten Pierick ◽  
Mark Hanemaaijer ◽  
...  

ABSTRACTThe industrial production of penicillin G byPenicillium chrysogenumrequires the supplementation of the growth medium with the side chain precursor phenylacetate. The growth ofP. chrysogenumwith phenylalanine as the sole nitrogen source resulted in the extracellular production of phenylacetate and penicillin G. To analyze this natural pathway for penicillin G production, chemostat cultures were switched to [U-13C]phenylalanine as the nitrogen source. The quantification and modeling of the dynamics of labeled metabolites indicated that phenylalanine was (i) incorporated in nascent protein, (ii) transaminated to phenylpyruvate and further converted by oxidation or by decarboxylation, and (iii) hydroxylated to tyrosine and subsequently metabolized via the homogentisate pathway. The involvement of the homogentisate pathway was supported by the comparative transcriptome analysis ofP. chrysogenumcultures grown with phenylalanine and with (NH4)2SO4as the nitrogen source. This transcriptome analysis also enabled the identification of two putative 2-oxo acid decarboxylase genes (Pc13g9300 and Pc18g01490). cDNAs of both genes were cloned and expressed in the 2-oxo-acid-decarboxylase-freeSaccharomyces cerevisiaestrain CEN.PK711-7C (pdc1 pdc5 pdc6Δ aro10Δ thi3Δ). The introduction of Pc13g09300 restored the growth of thisS. cerevisiaemutant on glucose and phenylalanine, thereby demonstrating that Pc13g09300 encodes a dual-substrate pyruvate and phenylpyruvate decarboxylase, which plays a key role in an Ehrlich-type pathway for the production of phenylacetate inP. chrysogenum. These results provide a basis for the metabolic engineering ofP. chrysogenumfor the production of the penicillin G side chain precursor phenylacetate.


Microbiology ◽  
2014 ◽  
Vol 160 (12) ◽  
pp. 2694-2709 ◽  
Author(s):  
Muktak Aklujkar ◽  
Carla Risso ◽  
Jessica Smith ◽  
Derek Beaulieu ◽  
Ryan Dubay ◽  
...  

Ferroglobus placidus was discovered to oxidize completely the aromatic amino acids tyrosine, phenylalanine and tryptophan when Fe(III) oxide was provided as an electron acceptor. This property had not been reported previously for a hyperthermophilic archaeon. It appeared that F. placidus follows a pathway for phenylalanine and tryptophan degradation similar to that of mesophilic nitrate-reducing bacteria, Thauera aromatica and Aromatoleum aromaticum EbN1. Phenylacetate, 4-hydroxyphenylacetate and indole-3-acetate were formed during anaerobic degradation of phenylalanine, tyrosine and tryptophan, respectively. Candidate genes for enzymes involved in the anaerobic oxidation of phenylalanine to phenylacetate (phenylalanine transaminase, phenylpyruvate decarboxylase and phenylacetaldehyde : ferredoxin oxidoreductase) were identified in the F. placidus genome. In addition, transcription of candidate genes for the anaerobic phenylacetate degradation, benzoyl-CoA degradation and glutaryl-CoA degradation pathways was significantly upregulated in microarray and quantitative real-time-PCR studies comparing phenylacetate-grown cells with acetate-grown cells. These results suggested that the general strategies for anaerobic degradation of aromatic amino acids are highly conserved amongst bacteria and archaea living in both mesophilic and hyperthermophilic environments. They also provided insights into the diverse metabolism of Archaeoglobaceae species living in hyperthermophilic environments.


2017 ◽  
Vol 12 (8) ◽  
pp. 2008-2014
Author(s):  
Xiaoshu Xu ◽  
Chao Wang ◽  
Jun Chen ◽  
Sheng Yang

2007 ◽  
Vol 189 (21) ◽  
pp. 7626-7633 ◽  
Author(s):  
Stijn Spaepen ◽  
Wim Versées ◽  
Dörte Gocke ◽  
Martina Pohl ◽  
Jan Steyaert ◽  
...  

ABSTRACT Azospirillum brasilense belongs to the plant growth-promoting rhizobacteria with direct growth promotion through the production of the phytohormone indole-3-acetic acid (IAA). A key gene in the production of IAA, annotated as indole-3-pyruvate decarboxylase (ipdC), has been isolated from A. brasilense, and its regulation was reported previously (A. Vande Broek, P. Gysegom, O. Ona, N. Hendrickx, E. Prinsen, J. Van Impe, and J. Vanderleyden, Mol. Plant-Microbe Interact. 18:311-323, 2005). An ipdC-knockout mutant was found to produce only 10% (wt/vol) of the wild-type IAA production level. In this study, the encoded enzyme is characterized via a biochemical and phylogenetic analysis. Therefore, the recombinant enzyme was expressed and purified via heterologous overexpression in Escherichia coli and subsequent affinity chromatography. The molecular mass of the holoenzyme was determined by size-exclusion chromatography, suggesting a tetrameric structure, which is typical for 2-keto acid decarboxylases. The enzyme shows the highest k cat value for phenylpyruvate. Comparing values for the specificity constant k cat/Km , indole-3-pyruvate is converted 10-fold less efficiently, while no activity could be detected with benzoylformate. The enzyme shows pronounced substrate activation with indole-3-pyruvate and some other aromatic substrates, while for phenylpyruvate it appears to obey classical Michaelis-Menten kinetics. Based on these data, we propose a reclassification of the ipdC gene product of A. brasilense as a phenylpyruvate decarboxylase (EC 4.1.1.43).


1987 ◽  
Vol 42 (4) ◽  
pp. 319-332 ◽  
Author(s):  
Martina Rueffer ◽  
Meinhart H. Zenk

The incorporation rates of labelled tyrosine, DOPA. tyramine. and dopamine have been inves­tigated during the in vivo formation of the protoberberine alkaloid, jatrorrhizine, in callus cul­tures of Berberis canadensis. While tyrosine was equally well incorporated into both the iso­quinoline (54%) and benzyl (46%) portions of the alkaloid, DOPA was almost exclusively (91%) transformed into the isoquinoline moiety. However, tyramine (25%) and to a lesser extent, dopamine (15%) were incorporated into the aldehyde-derived, benzylic half of the isoquinoline molecule as well. In order to investigate further the precursory roles of these compounds, select enzymes involved in tyrosine metabolism in alkaloid-producing cell cultures have been studied. The occurrence of tyrosine decarboxylase, phenolase, transaminase, p-hydroxyphenylpyruvate decarboxylase, amineoxidase and methionine adenosyl transferase was demonstrated in suspen­sion cells of Berberis. These enzymes were partially purified and a preliminary characterization was performed. In the light of these and previous data, the differential metabolism of tyrosine and DOPA in the early steps of isoquinoline alkaloid biosynthesis is discussed. Conclusive evidence as to the biosynthetic origin of the phenylacetaldehydes which furnish the benzylic moiety of the alkaloids is precluded by the presence of both amineoxidase and phenylpyruvate decarboxylase activities in these cultures.


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