Purification of glucosamine 6-phosphate deaminase from human brain

Pattabiraman, T. N. ; Bachhawat, B. K. (1961) Purification of glucosamine 6-phosphate deaminase from human brain Biochimica et Biophysica Acta, 54 (2). pp. 273-283. ISSN 0006-3002

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000630...

Related URL: http://dx.doi.org/10.1016/0006-3002(61)90366-3


Glucosamine 6-phosphate deaminase, which degrades glucosamine 6-phosphate reversibly to fructose 6-phosphate and ammonia, has been purified 66-fold from human brain. The enzyme has an optimum pH in the range of 8.5-8.7. N-acetyl-glucosamine 6-phosphate activated the enzyme for both synthesis and degradation of glucosamine 6-phosphate. Pyrophosphate, cysteine and ethylene diamine tetracetic acid inhibited the activity of the enzyme. Certain divalent metal ions also activated the enzyme, Mn2+ and Hg2+ being the most effective, but Cd2+ markedly inhibited it. It was found that fructose 6-phosphate and ammonia are the specific substrates for the formation of glucosamine 6-phosphate. The Km values in the presence of N-acetyl-glucosamine 6-phosphate and Mn2+ were, for glucosamine 6-phosphate, 2.5 . 10-4 M; for fructose 6-phosphate, 3.5 . 10-3 M and for (NH4)2CO3, 1.6 . 10-2 M.

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