Phenylalanine ammonia lyase fromSporidiobolus pararoseus andRhodosporidium toruloides: Application for phenylalanine and tyrosine deamination

Watanabe, Shigeru; Hernandez-Velazco, G.; Iturbe-Chiñas, F. A.; Munguía, Agustín López

doi:10.1007/bf01198755

Cited by 23 publications

(3 citation statements)

References 18 publications

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“…In the food industry, this enzyme is used in the production of l -phenylalanine and para-hydroxycinnamic acid (Cui et al 2015 ), and in medicine in phenylketonuria therapy (Longo et al 2014 ; Sarkissian and Gámez 2005 ) and neoplastic cancers in mice (D’Cunha 2005 ). Furthermore, the activity of PAL is used to determine the concentration of l -phenylalanine in blood plasma (Watanabe et al 1992 ).…”

Section: Biosynthesis Of Phenylalanine Ammonia Lyase By R mentioning

confidence: 99%

Rhodotorula glutinis—potential source of lipids, carotenoids, and enzymes for use in industries

Kot

Błażejak

Kurcz

et al. 2016

Appl Microbiol Biotechnol

201

120

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Rhodotorula glutinis is capable of synthesizing numerous valuable compounds with a wide industrial usage. Biomass of this yeast constitutes sources of microbiological oils, and the whole pool of fatty acids is dominated by oleic, linoleic, and palmitic acid. Due to its composition, the lipids may be useful as a source for the production of the so-called third-generation biodiesel. These yeasts are also capable of synthesizing carotenoids such as β-carotene, torulene, and torularhodin. Due to their health-promoting characteristics, carotenoids are commonly used in the cosmetic, pharmaceutical, and food industries. They are also used as additives in fodders for livestock, fish, and crustaceans. A significant characteristic of R. glutinis is its capability to produce numerous enzymes, in particular, phenylalanine ammonia lyase (PAL). This enzyme is used in the food industry in the production of l-phenylalanine that constitutes the substrate for the synthesis of aspartame—a sweetener commonly used in the food industry.

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Section: Biosynthesis Of Phenylalanine Ammonia Lyase By R mentioning

confidence: 99%

Rhodotorula glutinis—potential source of lipids, carotenoids, and enzymes for use in industries

Kot

Błażejak

Kurcz

et al. 2016

Appl Microbiol Biotechnol

201

120

View full text Add to dashboard Cite

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“…Despite large differences in the primary sequence of proteins, PAL functions as a tetramer, similar to HAL in vivo . Presumably, PAL developed from HAL when fungi and plants diverged from the other kingdoms [7,25]. …”

Section: Introductionmentioning

confidence: 99%

Molecular evolution and functional characterisation of an ancient phenylalanine ammonia-lyase gene (NnPAL1) from Nelumbo nucifera: novel insight into the evolution of the PAL family in angiosperms

Gui

Wang

et al. 2014

BMC Evol Biol

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BackgroundPhenylalanine ammonia-lyase (PAL; E.C.4.3.1.5) is a key enzyme of the phenylpropanoid pathway in plant development, and it catalyses the deamination of phenylalanine to trans-cinnamic acid, leading to the production of secondary metabolites. This enzyme has been identified in many organisms, ranging from prokaryotes to higher plants. Because Nelumbo nucifera is a basal dicot rich in many secondary metabolites, it is a suitable candidate for research on the phenylpropanoid pathway.ResultsThree PAL members, NnPAL1, NnPAL2 and NnPAL3, have been identified in N. nucifera using genome-wide analysis. NnPAL1 contains two introns; however, both NnPAL2 and NnPAL3 have only one intron. Molecular and evolutionary analysis of NnPAL1 confirms that it is an ancient PAL member of the angiosperms and may have a different origin. However, PAL clusters, except NnPAL1, are monophyletic after the split between dicots and monocots. These observations suggest that duplication events remain an important occurrence in the evolution of the PAL gene family. Molecular assays demonstrate that the mRNA of the NnPAL1 gene is 2343 bp in size and encodes a 717 amino acid polypeptide. The optimal pH and temperature of the recombinant NnPAL1 protein are 9.0 and 55°C, respectively. The NnPAL1 protein retains both PAL and weak TAL catalytic activities with Km values of 1.07 mM for L-phenylalanine and 3.43 mM for L-tyrosine, respectively. Cis-elements response to environmental stress are identified and confirmed using real-time PCR for treatments with abscisic acid (ABA), indoleacetic acid (IAA), ultraviolet light, Neurospora crassa (fungi) and drought.ConclusionsWe conclude that the angiosperm PAL genes are not derived from a single gene in an ancestral angiosperm genome; therefore, there may be another ancestral duplication and vertical inheritance from the gymnosperms. The different evolutionary histories for PAL genes in angiosperms suggest different mechanisms of functional regulation. The expression patterns of NnPAL1 in response to stress may be necessary for the survival of N. nucifera since the Cretaceous Period. The discovery and characterisation of the ancient NnPAL1 help to elucidate PAL evolution in angiosperms.

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“…Moreover, PAL is one of the few nonhydrolytic enzymes that have important commercial applications [ 68 ], being useful for the production of l -phenylalanine ( l -Phe) from trans-cinnamic acid through the reverse physiological reaction [ 69 ]. In addition, PAL is effective in the treatment of certain mouse tumors [ 70 ] and useful in quantitative analysis of serum L-Phe in monitoring patients with phenylketonuria [ 71 ] and may be a very interesting target for biotechnological applications.…”

Section: Biotechnological Potential Of P Brasilianummentioning

confidence: 99%

Insights into Penicillium brasilianum Secondary Metabolism and Its Biotechnological Potential

et al. 2017

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Over the past few years Penicillium brasilianum has been isolated from many different environmental sources as soil isolates, plant endophytes and onion pathogen. All investigated strains share a great ability to produce bioactive secondary metabolites. Different authors have investigated this great capability and here we summarize the metabolic potential and the biological activities related to P. brasilianum’s metabolites with diverse structures. They include secondary metabolites of an alkaloid nature, i.e., 2,5-diketopiperazines, cyclodepsipeptides, meroterpenoids and polyketides. Penicillium brasilianum is also described as a great source of enzymes with biotechnological application potential, which is also highlighted in this review. Additionally, this review will focus on several aspects of Penicillium brasilianum and interesting genomic insights.

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Phenylalanine ammonia lyase fromSporidiobolus pararoseus andRhodosporidium toruloides: Application for phenylalanine and tyrosine deamination

Cited by 23 publications

References 18 publications

Rhodotorula glutinis—potential source of lipids, carotenoids, and enzymes for use in industries

Rhodotorula glutinis—potential source of lipids, carotenoids, and enzymes for use in industries

Molecular evolution and functional characterisation of an ancient phenylalanine ammonia-lyase gene (NnPAL1) from Nelumbo nucifera: novel insight into the evolution of the PAL family in angiosperms

Insights into Penicillium brasilianum Secondary Metabolism and Its Biotechnological Potential

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