Allosteric serine hydroxymethyltransferase from monkey liver: Temperature induced conformational transitions

Ramesh, Kashi S. ; Ananthanarayanan, V. S. ; Appaji Rao, N. (1981) Allosteric serine hydroxymethyltransferase from monkey liver: Temperature induced conformational transitions Journal of Biosciences, 3 (2). pp. 179-190. ISSN 0250-5991

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Abstract

The homogeneous serine hydroxymethyltransferase from monkey liver was optimally activate at 60° C and the Arrhenius plot for the enzyme was nonlinear with a break at 15° C. The monkey liver enzyme showed high thermal stability of 62°C, as monitored by circular dichroism at 222 nm, absorbance at 280 nm and enzyme activity. The enzyme exhibited a sharp co-operative thermal transition in the range of 50°-70° (Tm= 65°C), as monitored by circular dichroism. L-Serine protected the enzyme against both thermal inactivation and thermal disruption of the secondary structure. The homotropic interactions of tetrahydrofolate with the enzyme was abolished at high temperatures (at 70°C, the Hill coefficient value was 1.0). A plot of h values vs. assay temperature of tetrahydrofolate saturation experiments, showed the presence of an intermediate conformer with an h value of 1.7 in the temperature range of 45°-60°C. Inclusion of a heat denaturation step in the scheme employed for the purification of serine hydroxymethyltransferase resulted in the loss of cooperative interactions with tetrahydrofolate. The temperature effects on the serine hydroxylmethyltransferase, reported for the first time, lead to a better understanding of the heat induced alterations in conformation and activity for this oligomeric protein.

Item Type:Article
Source:Copyright of this article belongs to Indian Academy of Sciences.
Keywords:Serine Hydroxymethyltransferase; Circular Dichroism; Thermal Stability; Conformational Transitions
ID Code:85211
Deposited On:01 Mar 2012 08:52
Last Modified:19 May 2016 01:21

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