Phenylalanine Ammonia-Lyase from Loblolly Pine

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Yeast Phenylalanine Ammonia-lyase

I?henyialanine ammonia-lyase from the yeast Rhodotorula gluiinis was purified by salt fractionations and Sephadex chromatography. Density gradient centrifugation and Sephadex chromatography indicated its molecular weight to be about 275,000. Enzymatic deamination of several ring-substituted phenylalanine analogues and n-phenylalanine was studied. While cinnamic acid, a product of deamination, a...

متن کامل

Fungal and Plant Phenylalanine Ammonia-lyase

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 metabolized through the phenylpropanoid pathw...

متن کامل

Purification and Characterization of Phenylalanine Ammonia Lyase from Trichosporon cutaneum

Trichosporon cutaneum phenylalanine ammonia lyase was selected as a model to investigate the dual substrate activity of this family of enzymes. Sequencing of the PAL gene identified an extensive intron region at the N-terminus. Five amino acid residues differing from a prior report were identified. Highest Phe : Tyr activities (1.6  ± 0.3 : 0.4 ± 0.1  μ mol/h g wet weight) were induced by Tyr. ...

متن کامل

Functional properties of a phenylalanine ammonia-lyase promoter from Arabidopsis.

Phenylalanine ammonia-lyase (PAL) is encoded by a small family of genes in Arabidopsis. We cloned and partially characterized one of these genes, PAL1. The deduced amino acid sequence is highly similar to PAL from bean, parsley, and rice. The promoter contains sequence elements homologous to two putative regulatory elements conserved among several phenylpropanoid genes. The regulation of the PA...

متن کامل

Ethylene-induced Phenylalanine Ammonia-Lyase Activity in Carrot Roots.

Ethylene enhanced the activity of phenylalanine ammonialyase in carrot (Daucus carota L., var. "Nauty") root tissue. Slight increase in enzyme activity was exhibited by root discs incubated in ethylene-free air. It was probably due to the ethylene formed within the sliced tissue. Addition of ethylene to the air stream increased phenylalanine ammonia-lyase activity and the total protein content ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Plant Physiology

سال: 1992

ISSN: 0032-0889,1532-2548

DOI: 10.1104/pp.98.1.380