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Biosynthesis of myo-inositol in jycopods: characteristics of the pteridophytic L-Myo-inositol-1-phosphate synthase and myo-inositol-1-phosphate phosphatase from the strobili of Lycopodium clavatum and Selaginella monospora

100%

Basak A., Jha T. B., Adhikari J.

Acta Physiologiae Plantarum

2012

tom 34

nr 4

Two key enzymes of myo-inositol metabolism [L-myo-inositol-1-phosphate synthase (MIPS) and myoinositol-1-phosphate-phosphatase (MIPP)] were identified for the first time in Pteridophyta in Lycopodium clavatum and Selaginella monospora. Both enzymes from both plants were partly purified and the degree of purity obtained from 47 to 75 folds. MIPS preparations specifically utilized D-glucose-6-phosphate and NAD⁺ as its substrate and coenzyme with the Km values for G-6-P and NAD⁺ were 1.74 and 0.34 mM in L. clavatum; 2.32 and 0.37 mM in S. monospora. MIPP preparations used D/Lmyo-inositol-1-phosphate as its principal substrate with the Km values for MIP was 0.068 mM in L. clavatum and 0.076 mM in S. monospora. The pH reliance of all the preparations was around 7.0–7.5 and different cations had variable role.

Partial purification and characterization of L-myo-inositol-1-phosphate synthase of pteridophytic origin

100%

Chhetri D. R., Mukherjee A. K., Adhikari J.

Acta Physiologiae Plantarum

2006

tom 28

nr 2

Myo-Inositol is an important metabolite for normal growth and development of all living organisms. The cellular level of myo-inositol is con-rolled by the enzyme L-myo- inositol-1-phosphate synthase (MIPS) [EC 5.5.1.4]. Appreciable level of MIPS activity was detected from the common pteridophytes like Dicranopteris, Diplazium, Diplopterygium, Equisetum, Lycopodium, Polypodium, Pteridium, Selaginella etc. available in Darjeeling Himalayas. The enzyme was partially purified from the reproduc-ive pinnules of Diplopterygium glaucum (Thunb.) Nakai. The purification obtained was about 81 fold and the recovery was about 13.5 %. The final enzyme preparation specifically utilized D-Glucose-6-phosphte and NAD+ as its substrate and co-factor respectively. It shows pH optima between 7.0 and 7.5 while the temperature maximum was at 35 °C. The enzyme activity was slightly inhibited by Na+ and Cd2+ and highly inhibited by Li+ and Hg2+. The Krn values for D-glucose-6-phosphate and NAD+ was found to be as 0.83 mM and 0.44 mM respectively while the Vmax values were 1.42 mM and 1.8 mM for D-glucose-6-phosphate and NAD+ respectively. The present study indicates the universal occurrence of this enzyme in all plant groups.

Ograniczanie wyników

2 Acta Physiologiae Plantarum

2 Adhikari J.

1 Basak A.

1 Chhetri D. R.

1 Jha T. B.

1 Mukherjee A. K.

1 2012

1 2006

Wyniki wyszukiwania

Biosynthesis of myo-inositol in jycopods: characteristics of the pteridophytic L-Myo-inositol-1-phosphate synthase and myo-inositol-1-phosphate phosphatase from the strobili of Lycopodium clavatum and Selaginella monospora

Partial purification and characterization of L-myo-inositol-1-phosphate synthase of pteridophytic origin