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Allosteric regulation of serine hydroxymethyltransferase from mung bean (Phaseolus aureus)

Rao, Desirazu Narasimha and Rao, N Appaji (1980) Allosteric regulation of serine hydroxymethyltransferase from mung bean (Phaseolus aureus). In: Biochemical and Biophysical Research Communications, 92 (4). pp. 1166-1171.

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Serine hydroxymethyltransferase, the first enzyme in the pathway for the interconversion of one carbon compounds was purified from mung bean seedlings by ammonium sulfate fractionation, DEAE-Sephadex, Blue Sepharose CL-6B affinity chromatography and gel filteration on Sephacryl S-200. The specific activity of the enzyme, 0.73 (u mol HCHO formed/min/mg protein) was 104 times larger than the highest value reported hitherto. Saturation of tetrahydrofolate was sigmoid, whereas with serine was hyperbolic, with nH values of 1.9 and 1.0 respectively. Reduced nicotinamide adenine dinucleotide, lysine and methionine decreased, whereas nicotinamide adenine dinucleotide, adenosine 5′-monophosphate and adenosine 5′-triphosphate increased the sigmoidicity. These results suggest that serine hydroxymethyltransferase from mung bean is a regulatory enzyme. H4folate; (±)-L-tetrahydrofolate

Item Type: Journal Article
Publication: Biochemical and Biophysical Research Communications
Publisher: Elsevier Science
Additional Information: Copyright of this article belongs to Elsevier Science.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 09 Sep 2009 09:57
Last Modified: 19 Sep 2010 05:43
URI: http://eprints.iisc.ac.in/id/eprint/22920

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