نتایج جستجو برای: phenylalanine ammonia lyase enzyme

تعداد نتایج: 284924  

2017
Pan Liu Jan Wysocki Peter Serfozo Minghao Ye Tomokazu Souma Daniel Batlle Jing Jin

Degradation of the biologically potent octapeptide angiotensin Ang II-(1-8) is mediated by the activities of several peptidases. The conversion of Ang II to the septapeptide Ang-(1-7) is of particular interest as the latter also confers organ protection. The conversion is catalyzed by angiotensin-converting enzyme 2 and other enzymes that selectively cleave the peptide bond between the proline ...

Journal: :Clinical chemistry 1982
F W Spierto W Whitfield M Apetz W H Hannon

With phenylalanine ammonia-lyase (EC 4.3.1.5) we converted phenylalanine (Phe) and tyrosine (Tyr) to transcinnamic acid and p-coumaric acid, respectively. These were separated by "high-performance" liquid chromatography and detected at 280 nm. We measured the Phe and Tyr content of human serum by adding 100 mU of the enzyme to a 20-microL serum aliquot, mixing for 2 h at 24 degrees C, then stop...

2013
W. Noé H. U. Seitz

Phenylalanine Ammonia-Lyase, Protein Metabolism, Regulation, /ra/js-Cinnamic Acid, Daucus carota, Suspension Culture In vivo and in vitro experiments were performed in order to study the regulatory role of transcinnamic acid and its hydroxylated derivatives (p-coumaric acid, caffeic acid) on the deamina­ tion of phenylalanine catalyzed by PAL (EC 4.3.1.5). 7>arts-cinnamic acid inhibits growth a...

2013
Bruno Boni Guidotti Bruno Ribeiro Gomes Rita de Cássia Siqueira-Soares Anderson Ricardo Soares Osvaldo Ferrarese-Filho

In the present study, we investigated the effects of dopamine, an allelochemical exuded from the velvetbean (Mucuna pruriens L DC. var utilis), on the growth and cell viability of soybean (Glycine max L. Merrill) roots. We analyzed the effects of dopamine on superoxide dismutase, phenylalanine ammonia-lyase and cell wall-bound peroxidase activities as well as its effects on lignin contents in t...

Journal: :Structure 2002
C W Levy P A Buckley S Sedelnikova Y Kato Y Asano D W Rice P J Baker

Methylaspartate ammonia lyase (MAL) catalyzes the magnesium-dependent reversible alpha,beta-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid. The 1.3 A MAD crystal structure of the dimeric Citrobacter amalonaticus MAL shows that each subunit comprises two domains, one of which adopts the classical TIM barrel fold, with the active site at the C-terminal end of ...

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