Biochemical Evaluation of the Decarboxylation and Decarboxylation-Deamination Activities of Plant Aromatic Amino Acid Decarboxylases

Torrens-Spence, Michael P.; Liu, Pingyang; Ding, Huanjun; Harich, Kim; Gillaspy, Glenda E.; Li, Jianyong

doi:10.1074/jbc.m112.401752

Cited by 58 publications

(74 citation statements)

References 36 publications

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“…The peak dimension increased proportionally as the incubation time increased (Figure 1A-C), indicating that the broad peak corresponds to the reaction product. The product peak in the recombinant enzymes and tryptophan reaction mixtures appeared to be an aromatic acetaldehyde based on its similar chromatographic behavior to previously investigated aromatic acetaldehydes [13,15,16]. This acetaldehyde-like peak suggested that the MtAAS and CaAAS enzymes might function as aromatic aldehyde synthases rather than a SDC.…”

Section: Resultssupporting

confidence: 66%

“…MtAAS and CaAAS were initially assayed using known group II amino acid decarboxylase substrates (serine, histidine, glutamate, tyrosine, dopa, tryptophan, and 5-hydroxytryptophan) via an high-performance liquid chromatography electrochemical detection assay (HPLC-EC) [10,13,14]. Despite demonstrating no measurable amine product formation from any of the tested substrates, a broad peak was detected in the tryptophan reaction mixtures for each enzyme.…”

Section: Resultsmentioning

confidence: 99%

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Diverse functional evolution of serine decarboxylases: identification of two novel acetaldehyde synthases that uses hydrophobic amino acids as substrates

et al. 2014

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BackgroundType II pyridoxal 5′-phosphate decarboxylases are an important group of phylogenetically diverse enzymes involved in amino acid metabolism. Within plants, this group of enzymes is represented by aromatic amino acid decarboxylases, glutamate decarboxylases and serine decarboxylases. Additional evolutionary divergence of plant aromatic amino acid decarboxylases has resulted in further subcategories with distinct substrate specificities and enzymatic activities. Despite shared homology, no such evolutionary divergence has been characterized within glutamate decarboxylases or serine decarboxylases (SDC).ResultsComparative analysis of two previously characterized serine decarboxylase-like (SDC-like) enzymes demonstrates distinct substrate specificities despite their highly conserved primary sequence. The alternate substrate preference of these homologous SDC-like proteins indicated that functional divergence might have occurred with in SDC-like proteins. In an effort to identify additional SDC-like functional divergence, two uncharacterized SDC-like enzymes were recombinantly expressed and characterized.ConclusionsAn extensive biochemical analysis of two serine decarboxylases-like recombinant proteins led to an interesting discovery; both proteins catalyze the formation of acetaldehyde derivatives from select hydrophobic amino acids substrates. Specifically, Medicago truncatula [GenBank: XP_003592128] and Cicer arietinum [GenBank: XP_004496485] catalyze the decarboxylation and oxidative deamination of phenylalanine, methionine, leucine and tryptophan to generate their corresponding acetaldehydes. The promiscuous aldehyde synthase activity of these proteins yields novel products of 4-(methylthio) butanal, 3-methylbutanal (isovaleraldehyde) and indole-3-acetaldehyde from methionine, leucine and tryptophan respectively. A comparative biochemical analysis of the Medicago truncatula and Cicer arietinum enzymes against two previously characterized SDC-like enzymes further emphasizes the unusual substrate specificity and activity of these novel aldehyde synthases. Due to the strong substrate preference towards phenylalanine, it is likely that both enzymes function as phenylacetaldehyde synthesis in vivo. However, due to their significant sequence divergence and unusual substrate promiscuity these enzymes are functionally and evolutionary divergent from canonical phenylacetaldehyde synthesis enzymes. This work further elaborates on the functional complexity of plant type II PLP decarboxylases and their roles in secondary metabolite biosynthesis.Electronic supplementary materialThe online version of this article (doi:10.1186/s12870-014-0247-x) contains supplementary material, which is available to authorized users.

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Section: Resultssupporting

confidence: 66%

Section: Resultsmentioning

confidence: 99%

Diverse functional evolution of serine decarboxylases: identification of two novel acetaldehyde synthases that uses hydrophobic amino acids as substrates

et al. 2014

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“…AAS is a bifunctional enzyme that converts tyrosine into 4-HPAA oxidation 15–17 . In E. coli , 4-HPAA is converted to tyrosol by alcohol dehydrogenase(s) 14 .…”

Section: Resultsmentioning

confidence: 99%

Production of three phenylethanoids, tyrosol, hydroxytyrosol, and salidroside, using plant genes expressing in Escherichia coli

Chung

Kim

Ahn

2017

Sci Rep

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Polyphenols, which include phenolic acids, flavonoids, stilbenes, and phenylethanoids, are generally known as useful antioxidants. Tyrosol, hydroxytyrosol, and salidroside are typical phenylethanoids. Phenylethanoids are found in plants such as olive, green tea, and Rhodiola and have various biological activities, including the prevention of cardiovascular diseases, cancer, and brain damage. We used Escherichia coli to synthesize three phenylethanoids, tyrosol, hydroxytyrosol, and salidroside. To synthesize tyrosol, the aromatic aldehyde synthase (AAS) was expressed in E. coli. Hydroxytyrosol was synthesized using E. coli harboring AAS and HpaBC, which encodes hydroxylase. In order to synthesize salidroside, 12 uridine diphosphate-dependent glycosyltransferases (UGTs) were screened and UGT85A1 was found to convert tyrosol to salidroside. Using E. coli harboring AAS and UGT85A1, salidroside was synthesized. Through the optimization of these three E. coli strains, we were able to synthesize 531 mg/L tyrosol, 208 mg/L hydroxytyrosol, and 288 mg/L salidroside, respectively.

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“…tomato AADC, producing phenylethylamine (route c). Torrens-Spence et al proposed that a single key amino acid residue of decarboxylase (Phe at 348 in rose AADC) is responsible for the determination of route a or c. 42) However, this remains controversial because the petunia PAAS has Valine residue at the same site, but shows the decarboxylation-oxidative deamination (route a). 32) Tandem transgenic poplar expressing rose AADC/PAld reductase (PAR) showed higher levels of 2PE production and mRNA expression of rose AADC and petunia PAAS than plants expressing petunia PAAS/PAR.…”

Section: III Biosynthetic Enzymes Involved In the Production Of [ 2mentioning

confidence: 99%

Biosynthesis of floral scent 2-phenylethanol in rose flowers

Hirata

Ohnishi

Watanabe

2016

Bioscience, Biotechnology, and Biochemistry

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Plants emit chemically diverse volatile compounds for attracting pollinators or putting up a chemical defense against herbivores. 2-Phenylethanol (2PE) is one of the abundantly emitted scent compounds in rose flowers. Feeding experiments with l-[(2)H8]phenylalanine into rose flowers and subsequent analysis using gas chromatography-mass spectrometry analysis revealed the hypothetical biosynthetic intermediates to [(2)H8]-2PE, and the biochemical and genetic analyses elucidated the principal pathway to [(2)H8]-2PE. We recently found season-specific 2PE pathway producing [(2)H7]-2PE from l-[(2)H8]phenylalanine. This is a unique example where the dominant pathway to a specific compound changes with the seasons. This review focuses on the biosynthesis of floral volatiles and their regulation to adapt to the changes in the environment.

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Biochemical Evaluation of the Decarboxylation and Decarboxylation-Deamination Activities of Plant Aromatic Amino Acid Decarboxylases

Cited by 58 publications

References 36 publications

Diverse functional evolution of serine decarboxylases: identification of two novel acetaldehyde synthases that uses hydrophobic amino acids as substrates

Diverse functional evolution of serine decarboxylases: identification of two novel acetaldehyde synthases that uses hydrophobic amino acids as substrates

Production of three phenylethanoids, tyrosol, hydroxytyrosol, and salidroside, using plant genes expressing in Escherichia coli

Biosynthesis of floral scent 2-phenylethanol in rose flowers

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