2006
DOI: 10.1007/s11738-006-0036-8
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Partial purification and characterization of L-myo-inositol-1-phosphate synthase of pteridophytic origin

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Cited by 6 publications
(7 citation statements)
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“…The K m value for G-6-P, as determined by Lineweaver-Burk plot was 0.80 mM which is comparable to the same for the pteridophytic enzyme having a value of 0.83 (Chhetri et al, 2006a). The V max value of this bryophytic enzyme was calculated as 2.80 mM as against 1.6 mM for the yeast enzyme (Donahue and Henry, 1981b) and 1.42 mM for the pteridophytic enzyme (Chhetri et al 2006a). Though this value differs widely from other plant species, it corresponds to the V max value of 2.95 reported for Taxus baccata (Chhetri and Chiu, 2004).…”
Section: Characterization Of the Purified Enzymesupporting
confidence: 64%
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“…The K m value for G-6-P, as determined by Lineweaver-Burk plot was 0.80 mM which is comparable to the same for the pteridophytic enzyme having a value of 0.83 (Chhetri et al, 2006a). The V max value of this bryophytic enzyme was calculated as 2.80 mM as against 1.6 mM for the yeast enzyme (Donahue and Henry, 1981b) and 1.42 mM for the pteridophytic enzyme (Chhetri et al 2006a). Though this value differs widely from other plant species, it corresponds to the V max value of 2.95 reported for Taxus baccata (Chhetri and Chiu, 2004).…”
Section: Characterization Of the Purified Enzymesupporting
confidence: 64%
“…The reaction rate was found to increase linearly with respect to G-6-P up to a concentration of 4mM. The K m value for G-6-P, as determined by Lineweaver-Burk plot was 0.80 mM which is comparable to the same for the pteridophytic enzyme having a value of 0.83 (Chhetri et al, 2006a). The V max value of this bryophytic enzyme was calculated as 2.80 mM as against 1.6 mM for the yeast enzyme (Donahue and Henry, 1981b) and 1.42 mM for the pteridophytic enzyme (Chhetri et al 2006a).…”
Section: Characterization Of the Purified Enzymementioning
confidence: 54%
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“…Since the enzyme did not exhibit any activity in absence of NAD + , it can be safely concluded that the plastidial MIPS from E. intestinalis did not possess any 'built in' NAD + in its molecular architecture, unlike the MIPS obtained from mammalian adult brain (Adhikari, Majumder 1983) and from Euglena gracilis (Dasgupta et al 1984). 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).…”
Section: Mips Activitysupporting
confidence: 93%