ACTION OF PHOSPHOGLUCOMUTASE ON d-GLUCOSAMINE-6-PHOSPHATE
نویسندگان
چکیده
منابع مشابه
Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate.
Studies in viva on the biosynthesis of n-glucosamine, with the use of specifically labeled glucose in the rat (1,2) and in group A streptococci (3-5) showed that the glucose carbon chain was preserved during its conversion to the hexosamine. Leloir and Cardini (6, 7) noted that extracts obtained from Neurospora crassa converted glutamine and hexose phosphate to glutamic acid and a product tenta...
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A d-glucosamine 6-phosphate N-acetyltransferase from Blastocladiella emersonii zoospores was partially purified to a specific activity of 2.41 IU per mg of protein. Its pH optimum was 8.05 and its K(m) values were 2.4 x 10(-4) M d-glucosamine 6-phosphate and 0.38 x 10(-4) M Na(3)S-acetyl coenzyme A.
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d-Glucosamine-6-P N-acetyltransferase (EC 2.3.1.4) from mung bean seeds (Phaseolus aureus) was purified 313-fold by protamine sulfate and isoelectric precipitation, ammonium sulfate and acetone fractionation, and CM Sephadex column chromatography. The partially purified enzyme was highly specific for d-glucosamine-6-P. Neither d-glucosamine nor d-galactosamine could replace this substrate. The ...
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A partially purified enzyme (120-fold) from Leuconostoc mesenteroides catalyzed the reversible N-acetylation of d-glucosamine-6-phosphate. Coenzyme A was not required and inhibited the reaction rate. Neither d-glucosamine nor N-acetyl-d-glucosamine served as a substrate for the reversible reaction. The enzyme preparation retained 50% of its original activity after 5 min at 100 C. The K(m) for a...
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When rats were subjected to partial hepatectomy, glucosamine 6-phosphate synthase (EC 5.3.1.19) of the remaining liver underwent alterations both in activity and in molecular form. To study the molecular alterations, glucosamine 6-phosphate synthase was purified from regenerating as well as control liver and was analyzed by isoelectric focusing. Although control liver exhibited only one form of...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1953
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)66092-2