Biochemical evaluation of a parsley tyrosine decarboxylase results in a novel 4-hydroxyphenylacetaldehyde synthase enzyme

Torrens-Spence, Michael P.; Gillaspy, Glenda E.; Zhao, Bingyu; Harich, Kim; White, Robert H.; Li, Jianyong

doi:10.1016/j.bbrc.2011.12.124

Cited by 28 publications

(36 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…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%

“…This acetaldehyde-like peak suggested that the MtAAS and CaAAS enzymes might function as aromatic aldehyde synthases rather than a SDC. Aldehydes can be reduced to their corresponding alcohol by borohydride [13,15]. When the recombinant protein and tryptophan reaction mixtures were treated with NaBH 4 prior to HPLC-ED analysis, the broad product peak (Figure 1A-C) was converted to a sharp peak (Figure 1D-F).…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

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

et al. 2014

Self Cite

View full text Add to dashboard Cite

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.

show abstract

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

Self Cite

View full text Add to dashboard Cite

show abstract

“…These products include 4-hydroxyphenylacetaldehyde, phenylethylamine, indole-3-acetaldehyde, and 5-hydroxy indole-3-acetaldehyde. 4-Hydroxyphenylacetaldehyde has only been documented as a product from a single AAS enzyme (12). Thus far the physiological function of this AAS product remains unknown.…”

Section: Discussionmentioning

confidence: 99%

“…Additionally, our recent study showed that even experimentally investigated AAAD enzymes are capable of inaccurate characterization. In the aforementioned study we demonstrate that the previously characterized Petroselinum crispum TyDC (Q06086) (15) is actually an AAS that principally catalyzes the conversion of tyrosine to p-hydroxyphenylacetaldehyde (12).…”

mentioning

confidence: 98%

See 1 more Smart Citation

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

Torrens-Spence

Liu

Ding

et al. 2013

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Background: Plant arylalkylamine and aldehyde synthesizing aromatic amino acid decarboxylases (AAAD) are effectively indistinguishable. Results: Mutagenesis of a single AAAD residue enables the interconversion of activities. Conclusion: A single residue is primarily responsible for differentiating plant AAAD decarboxylase and aldehyde synthase activities. Significance: AAAD activity differentiation enables primary sequence activity identification, generation of unusual AAAD enzyme products, and AAAD mechanistic insights.

show abstract

Oxygen reactivity with pyridoxal 5′-phosphate enzymes: biochemical implications and functional relevance

et al. 2020

View full text Add to dashboard Cite

The versatility of reactions catalyzed by pyridoxal 5′-phosphate (PLP) enzymes is largely due to the chemistry of their extraordinary catalyst. PLP is necessary for many reactions involving amino acids. Reaction specificity is controlled by the orientation of the external aldimine intermediate that is formed upon addition of the amino acidic substrate to the coenzyme. The breakage of a specific bond of the external aldimine gives rise to a carbanionic intermediate. From this point, the different reaction pathways diverge leading to multiple activities: transamination, decarboxylation, racemization, elimination, and synthesis. A significant novelty appeared approximately 30 years ago when it was reported that some PLP-dependent decarboxylases are able to consume molecular oxygen transforming an amino acid into a carbonyl compound. These side paracatalytic reactions could be particularly relevant for human health, also considering that some of these enzymes are responsible for the synthesis of important neurotransmitters such as γ-aminobutyric acid, dopamine, and serotonin, whose dysregulation under oxidative conditions could have important implications in neurodegenerative states. However, the reactivity of PLP enzymes with dioxygen is not confined to mammals/animals. In fact, some plant PLP decarboxylases have been reported to catalyze oxidative reactions producing carbonyl compounds. Moreover, other recent reports revealed the existence of new oxidase activities catalyzed by new PLP enzymes, MppP, RohP, Ind4, CcbF, PvdN, Cap15, and CuaB. These PLP enzymes belong to the bacterial and fungal kingdoms and are present in organisms synthesizing bioactive compounds. These new PLP activities are not paracatalytic and could only scratch the surface on a wider and unexpected catalytic capability of PLP enzymes.

show abstract

Biochemical evaluation of a parsley tyrosine decarboxylase results in a novel 4-hydroxyphenylacetaldehyde synthase enzyme

Cited by 28 publications

References 18 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

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

Oxygen reactivity with pyridoxal 5′-phosphate enzymes: biochemical implications and functional relevance

Contact Info

Product

Resources

About