Results 11 to 20 of about 32,058 (267)

Phenylalanine ammonia-lyase through evolution: A bioinformatic approach [PDF]

Trends in Pharmaceutical Sciences, 2015
Phenylalanine ammonia-lyase (PAL) is the first entry enzyme of the phenylpropanoid pathway that converts phenylalanine to cinnamic acid which is the precursor of various secondary metabolites.
Shiva Hemmati
doaj   +5 more sources

A Phenylalanine Ammonia Lyase Capacitive Sensor for Phenylalanine Detection

Proceedings
In this paper, an easy-to-use and fast biosensor for phenylalanine quantification in patients affected by phenylketonuria is investigated. The phenylalanine concentration was indirectly estimated through the ammonia released as a by-product of an ...
Bruno Andò, Salvatore Castorina, Ludovica Maugeri, Salvatore Petralia, Maria Anna Messina, Martino Ruggieri, Giovanni Neri, Angelo Ferlazzo, Emilio Sardini, Mauro Serpelloni   +9 more
doaj   +2 more sources

STUDY OF PHYSICOCHEMICAL AND THERMAL PROPERTIES OF L-PHENYLALANINE AMMONIA-LYASE

Foods and Raw Materials, 2013
Physicochemical and thermal properties of L-phenylalanine ammonia-lyase preparation were studied. Thermal gravimetric analysis of physical and chemical phenomena occurring in the enzyme upon heating was conducted. Heating curves were registered.
Babich O.O., Ulrikh E.V.
doaj   +3 more sources

Biochemical Characterization of a Prokaryotic Phenylalanine Ammonia Lyase [PDF]

Journal of Bacteriology, 2006
ABSTRACT The committed biosynthetic reaction to benzoyl-coenzyme A in the marine bacterium “ Streptomyces maritimus ” is carried out by the novel prokaryotic phenylalanine ammonia lyase (PAL) EncP, which converts the primary amino acid l -phenylalanine to trans
Longkuan Xiang, Bradley S. Moore
openalex   +6 more sources

Phenylalanine Ammonia-Lyase in Sliced Sweet Potato Roots

Agricultural and Biological Chemistry, 1965
A marked rise in the phenylalanine ammonia-lyase activity and the polyphenol synthesis was observed in sliced roots of a sweet potato. The enzyme activity was found to be localized in the root tissue adjacent to the sliced surface. In this region, the synthesis of polyphenols was much higher compared to the inner tissues.
Takao Minamikawa, Ikuzō Uritani
openalex   +5 more sources

Switching Enantioselectivity in Phenylalanine Ammonia Lyase for the Synthesis of Electron-Deficient Aromatic d-Amino Acids. [PDF]

Angew Chem Int Ed Engl
Phenylalanine ammonia lyases (PALs) were engineered to switch enantioselectivity, enabling hydroamination for the direct synthesis of electron‐deficient aromatic d‐amino acids (d‐AA). Structure‐guided engineering provided PAL variants with broad substrate scope, high activity, and excellent d‐selectivity, broadening the utility of PALs in asymmetric ...
Buslov I, Desmons S, Wang W, Massaad LE, Hu X.   +4 more
europepmc   +3 more sources

Fungal and Plant Phenylalanine Ammonia-lyase [PDF]

Mycobiology, 2011
L-Phenylalanine is one of the essential amino acids that cannot be synthesized in mammals in adequate amounts to meet the requirements for protein synthesis. Fungi and plants are able to synthesize phenylalanine via the shikimic acid pathway. L-Phenylalanine, derived from the shikimic acid pathway, is used directly for protein synthesis in plants or ...
Seong Hwan Kim, Jun Young Kim, Yeo Hong Yun, Min Woo Hyun   +3 more
openaire   +3 more sources

Phenylalanine Ammonia-lyase of Bamboo Shoots [PDF]

Agricultural and Biological Chemistry, 1988
Phenylalanine ammonia-lyase (PAL) was purified from bamboo shoots (Bambusa oldhami Munro) through steps of DEAE-Sephacel column chromatography, Sepharose CL-6B gel filtration, and a second DEAE-Sephacel column chromatography. Polyacrylamide gel electrophoresis showed that the purified enzyme (Mr 360, 000) still contained two minor bands with much ...
Ming-Sai Liu, Tsung-Chain Chang, Ru-Yin Chen   +2 more
openaire   +3 more sources

A Blast-Resistant NLR Gene Confers Drought Resistance by Competitively Interacting with an E3 Ligase to Protect Phenylalanine Ammonia-Lyase in Rice. [PDF]

Adv Sci (Weinh)
The NLR protein PibH8 interacts with phenylalanine ammonia‐lyase OsPAL1 and E3 ubiquitin ligase OsFBK16. Through competitive binding, PibH8 weakens the interaction between OsFBK16 and OsPAL1, thereby reducing the degradation of OsPAL1 by OsFBK16. The Hap1 allele of PibH8 exhibits a higher expression level than Hap2, thus accumulating more PibH8 protein,
Xiang D, Tu H, Yuan Y, Yao Y, Liao W, Wang H, Yan Y, Wang Y, Chen Y, Liu D, Lv Q, He H, Hu H, Lai X, Yuan M, Xiong H, Dong F, Xiong L.   +17 more
europepmc   +2 more sources

Yeast Phenylalanine Ammonia-lyase [PDF]

Journal of Biological Chemistry, 1971
Abstract Phenylalanine ammonia-lyase from the yeast Rhodotorula glutinis was purified by salt fractionations and Sephadex chromatography. Density gradient centrifugation and Sephadex chromatography indicated its molecular weight to be about 275,000.
Daniel S. Hodgins
openalex   +3 more sources