biologia plantarum

International journal on Plant Life established by Bohumil Němec in 1959

Biologia plantarum 49:59-63, 2005 | DOI: 10.1007/s10535-005-0063-0

L-myo-inositol-1-phosphate synthase: partial purification and characterisation from Gleichenia glauca

D. R. Chettri1, M. Choudhuri1, A. K. Mukherjee2,*, J. Adhikari3
1 Botany Department, Darjeeling Govt. College, Darjeeling, India
2 Botany Department, Burdwan University, Burdwan, India
3 Botany Department, Presidency College, Calcutta, India

A screening for the enzyme L-myo-inositol-1-phosphate synthase [EC 5.5.1.4] has been made first time in both vegetative and reproductive parts of the representative members of pteridophytes: Lycopodium, Selaginella, Equisetum, Polypodium, Dryopteris, and Gleichenia. The enzyme has been partially purified following low-speed centrifugation, streptomycin sulphate precipitation, ammonium sulphate fractionation, chromatography on DEAE-cellulose and gel-filtration through Sephadex G-200, and characterised from the reproductive pinnules of Gleichenia glauca Smith. The enzyme has a pH optimum at 7.5. The Km for glucose-6-P and NAD+ were 0.922 × 10-3 M and 0.9 × 10-4 M, respectively. A basal activity of the enzyme has been recorded in absence of exogenous NAD+. The enzyme activity was augmented with NH4Cl, but heavy metals like Hg2+, Cu2+ and Zn2+ inactivated it.

Keywords: inositol synthase; myo-inositol; pteridophytes
Subjects: Dryopteris schemperiana; Equisetum elongatum; Gleichenia glauca; heavy metals; inositol synthase; L-myo-inositol-1-phosphate synthase; Lycopodium clavatum; myo-inositol; Polypodium wallichii; pteridophytes; Selaginella microphylla; I-1-P synthase

Received: September 25, 2002; Accepted: August 12, 2004; Published: March 1, 2005  Show citation

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Chettri, D.R., Choudhuri, M., Mukherjee, A.K., & Adhikari, J. (2005). L-myo-inositol-1-phosphate synthase: partial purification and characterisation from Gleichenia glauca. Biologia plantarum, 49(1), 59-63. doi: 10.1007/s10535-005-0063-0
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