Myo-inositol content in pteridophytes and the isolation and characterization of L-myo-inositol-1-phosphate synthase from Diplopterygium glaucum

Chhetri, Dhani Raj; Mukherjee, Asok K.; Adhikari, Jukta

doi:10.1590/s1677-04202006000200005

Cited by 9 publications

(8 citation statements)

References 38 publications

(38 reference statements)

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“…Our results are however in complete agreement with the reports published earlier (Chettri et al 2006a;2006b;Basak et al 2012). The plastidial MIPS exhibited a temperature optima of 35 °C, which is also in complete congruence with majority of the published reports sans a few where a lower temperature maxima for MIPS has been recorded (Chettri et al 2005;2006a;2009). This may be attributed to the variation in the habitat of the experimental sample(s).…”

Section: Mips Activitysupporting

confidence: 93%

Isolation, partial purification and biochemical characterization of chloroplastic L-myo-inositol-1-phosphate synthase from a macro alga Enteromorpha intestinalis under high salinity

2018

EEB

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Induction of higher myo-inositol biosynthesis in a salinity driven macro-alga, Enteromorpha intestinalis (L.) Nees, as a model macrophyte, grown under natural conditions was established on the basis of a study on its prime enzyme, L-myo-inositol-1-phosphate synthase (MIPS) and the accumulation of free myo-inositol in chloroplasts. This enzyme was partially purified from isolated chloroplasts obtained from the plant grown under higher salinity to about 41-fold over homogenate following low-speed centrifugation, high-speed centrifugation, 0 to 80 % ammonium sulfate precipitation, successive chromatography through DEAE-cellulose, Sephadex G-200 and BioGel 0.5m columns. The apparent M r of the native enzyme was about 164 kDa. Temperature and pH optima were found to be 35 °C and 7.5 respectively. D-glucose-6-phosphate and NAD were its exclusive substrate and coenzyme, respectively, with K m value 0.1761 mM for D-glucsoe-6-phosphate and 0.1695 mM for β-NAD as determined by non-linear regression kinetics method. Among the important monovalent and divalent cations tested, K + had trivial stimulatory effect while Li + was sturdily inhibitory. Divalent cations recorded variable effects. Ca 2+ exhibited slight stimulatory effect and Cd 2+ reduced MIPS activity faintly. Salts of Cu 2+ and Hg 2+ were found to be potent inhibitors of this enzyme. The concentration of free myo-inositol was found to increase proportionately with salinity at least up to 12 PSU.

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Section: Mips Activitysupporting

confidence: 93%

Isolation, partial purification and biochemical characterization of chloroplastic L-myo-inositol-1-phosphate synthase from a macro alga Enteromorpha intestinalis under high salinity

2018

EEB

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“…Secondly, an excellent metabolic and structural synchronization can be established from this present study based on myo-inositol biosynthesis. We have observed previously (Chhetri et al, 2006) that MIPS activity is highest during the early stage of development of the strobilus or sorus in a pteridophyte. The content of free myo-inositol increases during late stages of development of the strobilus or sorus.…”

Section: Discussionmentioning

confidence: 83%

“…Results presented here show the existence of MIPP in a variety of vascular cryptogams. Chhetri et al (2005Chhetri et al ( , 2006 have already established the occurrence of the prime enzyme of myo-inositol biosynthesis, MIPS, in pteridophytes. Therefore, the presence of MIPP adds (Eisenberg Jr. 1967, Attwood et al, 1988Gee et al, 1988;Honchar et al, 1989;Leech et al, 1993;Pollack et al, 1994;Caselli et al, 1996, Fujimoto et al, 1996, Nigou and Besra, 2002Wang et al, 2006;Patra et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

“…However, only a few reports are available of this enzyme from plant systems (Loewus and Loewus, 1983;Gumber et al, 1984). Therefore, although the inositol biosynthetic pathway is necessarily functional in the vascular cryptogams, the supporting evidence is based only on MIPS (Chhetri et al, 2005(Chhetri et al, , 2006 without any information on MIPP. Hence the present investigation on MIPP is an attempt to bridge that gap and proceed with the study of this biosynthetic pathway through the evolutionary scale in pteridophytes centered on myoinositol.…”

Section: Introductionmentioning

confidence: 99%

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Occurrence of myo-inositol-1-phosphate phosphatase in pteridophytes: characteristics of the enzyme from the reproductive pinnules of Dryopteris filix-mas (L.) Schott

Banerjee

Chhetri²,

Adhikari

2007

Braz. J. Plant Physiol.

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Evident myo-inositol-1-phosphate phosphatase (MIPP) activity has been detected both in the vegetative as well as in the spore-bearing organs of some selected pteridophytes having wide phylogenetic diversity. The basic characterization of this enzyme was carried out using the cosmopolitan fern Dryopteris filix-mas. The enzyme was partially purified from the cytosol fraction obtained from the reproductive pinnules of the plant to about 41-fold over the initial homogenate following low-speed centrifugation, streptomycin sulfate precipitation, 25-70% ammonium sulfate fractionation, CM Sephadex C-50 chromatography and finally gel-filtration on Ultrogel AcA 34. The apparent molecular weight of the native MIPP was estimated to be 94 kDa. The enzyme activity increased linearly with respect to protein concentration to about 150 µg and with respect to time up to 75 min. The temperature optimum was found at 40ºC. However, the enzyme showed good activity over the temperature range of 30-50ºC. This enzyme used D/L-myo-inositol-1-phosphate as its principal substrate (95-100%), however, about 16% activity was recorded when D-myo-inositol-3-phosphate substituted as substrate. Furthermore, weak (3%) activity of this MIPP was observed with 2-glycerophosphate as substrate. The apparent K m for pteridophytic MIPP was 0.083 mM. The enzyme was functional in a narrow pH range of 7.5 to 8.5. The activity of this MIPP enzyme was remarkably inhibited by the presence of a monovalent cation, lithium, and even moderately so at a low concentration such as 1 mM. On the other hand, magnesium, a divalent cation, enhanced activity at least up to 10 mM. Calcium diminished MIPP activity at concentrations over 4 mM. Key words: Dryopteris filix-mas, myo-inositol-1-phosphate phosphatase, pteridophytes, reproductive pinnulesOcorrência da fosfatase do mio-inositol-1-fosfato em pteridófitas: características da enzima a partir de pínulas reprodutivas de Dryopteris filix-mas (L.) Schott: Tem-se detectado atividade da fosfatase do mio-inositol-1-fosfato (FMIF) tanto em órgãos vegetativos como em estruturas esporulantes de algumas pteridófitas com ampla diversidade filogenética. Neste estudo, procedeu-se à caracterização básica dessa enzima utilizando-se da pteridófita cosmopolita Dryopteris filix-mas. Após centrifugação em baixa velocidade, precipitação com sulfato de estreptomicina, fracionamento com sulfato de amônio (25-70%), cromatografia em CM Sephadex C-50 e, finalmente, filtração gélica em Ultrogel AcA 34, conseguiu-se uma purificação parcial da enzima (a partir da fração citossólica obtida de pínulas reprodutivas da planta) de cerca de 41 vezes em relação ao homogenato inicial. O peso molecular aparente da FMIF nativa foi estimado em 94 kDa. A atividade da enzima aumentou linearmente com relação ao conteúdo de proteína (cerca de 150 µg) e com relação ao tempo (até 75 min). A temperatura ótima foi de 40ºC. Entretanto, a enzima exibiu atividade razoável na faixa de temperatura entre 30 e 50ºC. O D/L-mio-inositol-1-fosfato foi o principal substrato (9...

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“…The effects of temperature and rainfall influence phytic acid synthesis, which starts with a rate limiting step involving the enzyme myo-inositol-3-phosphate synthase (MIPS). MIPS is highly affected by temperature and pH, with its optimum temperature in plants being 35 o C, while the pH is around 7.0 to 7.5 (Chhetri et al, 2006). The high levels of phytic acid content for varieties grown in Naivasha may be attributed to the high temperatures (25 to 29 o C) experienced in the area throughout the year.…”

Section: Wheat Varietiesmentioning

confidence: 99%

Evaluation of grain nutritional quality and resistant starch content in Kenyan bread wheat varieties

Kariithi¹,

Abwao²,

Ndung’u³

2016

Afr. Crop Sci. J.

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Myo-inositol content in pteridophytes and the isolation and characterization of L-myo-inositol-1-phosphate synthase from Diplopterygium glaucum

Cited by 9 publications

References 38 publications

Isolation, partial purification and biochemical characterization of chloroplastic L-myo-inositol-1-phosphate synthase from a macro alga Enteromorpha intestinalis under high salinity

Isolation, partial purification and biochemical characterization of chloroplastic L-myo-inositol-1-phosphate synthase from a macro alga Enteromorpha intestinalis under high salinity

Occurrence of myo-inositol-1-phosphate phosphatase in pteridophytes: characteristics of the enzyme from the reproductive pinnules of Dryopteris filix-mas (L.) Schott

Evaluation of grain nutritional quality and resistant starch content in Kenyan bread wheat varieties

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