کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5169981 | 1380518 | 2016 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and properties of β-cyano-l-alanine synthase from Spinacia oleracea
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
β-Cyano-l-alanine synthase was purified ca 6200-fold to homogeneity from the leaves of spinach (Spinacia oleracea). The purified enzyme has an apparent Mr of 60 000 and can be dissociated into identical subunits of Mr 30 000. The subunits each contain one molecule of pyridoxal 5â²-phosphate. The Km value is 2.3 mM for l-cysteine and 0.73 mM for cyanide. β-Cyano-l-alanine synthase from S. oleracea also catalyses the formation of some S-substituted l-cysteines and some heterocyclic β-substituted alanines from l-cysteine or O-acetyl-l-serine. The specificity of these additional catalytic activities of the purified enzyme are compared with those of cysteine synthase purified from the same plant, and with those of β-cyano-l-alanine synthase purified from other sources. Some other properties, including the amino acid composition of the purified enzyme, are also described.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Phytochemistry - Volume 27, Issue 7, 1988, Pages 2011-2016
Journal: Phytochemistry - Volume 27, Issue 7, 1988, Pages 2011-2016
نویسندگان
Fumio Ikegami, Kyoko Takayama, Chcho Tajima, Isamu Murakoshi,