STUDY OF PHYSICOCHEMICAL AND THERMAL PROPERTIES OF L-PHENYLALANINE AMMONIA-LYASE
نویسندگان
چکیده
منابع مشابه
Thermal bifunctionality of bacterial phenylalanine aminomutase and ammonia lyase enzymes.
Phenylalanine aminomutases (PAMs) are 4-methylideneimidazol-5-one (MIO)-dependent enzymes that catalyze the isomerization of (S)-a-phenylalanine to give (S)or (R)-bphenylalanine, which are precursors in the biosynthesis of various natural products. Several related tyrosine aminomutases (TAMs) have also been characterized. Furthermore, the mechanistically related MIO-dependent phenylalanine, tyr...
متن کاملYeast 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 کاملl-Phenylalanine Ammonia-Lyase Activity During Germination of Phaseolus vulgaris.
l-Phenylalanine ammonia-lyase (PAL) activity develops in excised bean axes after approximately 5 hours of incubation and reaches a maximum level after 14 hours of incubation. Light does not affect the development of activity, but puromycin, cycloheximide, actinomycin D, and 5-fluorouracil inhibit.During this period of incubation both d- and l-p-fluorophenylalanine stimulate fresh weight increas...
متن کاملl-Phenylalanine Ammonia-lyase (Maize): Partial Purification and Response to Gibberellic Acid and Cycloheximide of l-Phenylalanine and l-Tyrosine Ammonia-lyase Activities.
Extracts of maize leaf sheath tissue deaminate both l-phenylalanine and l-tyrosine. The activities with both substrates are enhanced by treating the plant with gibberellic acid. Both activities decrease rapidly at the same rate when tissue is incubated in a moist atmosphere, and this decrease can be slowed by treatment with cycloheximide. The ratio of the activities was constant throughout a se...
متن کاملFunctional 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...
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ژورنال
عنوان ژورنال: Foods and Raw Materials
سال: 2013
ISSN: 2308-4057
DOI: 10.12737/2056