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Current IssueEditorial BoardOnline First ArticlesArchive

volume 40 issue 4 (december 2006) : 267 - 271

EFFECT OF METAL IONS ON THE CYTOSOLIC NADP+- DEPENDENT ISOCITRATE DEHYDROGENASE FROM GERMINATING BLACKGRAM, VIGNA MUNGO (L.) HEPPER

M
M. Ayub Ali*
W
W. Joykumar Singh
L
L. Inaotombi Devi
S
S. Kunjeshwori Devi
L
L. Rupachandra Singh
1Department of Biochemistry, Manipur University, Canchipur - 795 003, Manipur

  • Submitted|

  • First Online |

  • doi

Cite article:- Ali* Ayub M., Singh Joykumar W., Devi Inaotombi L., Devi Kunjeshwori S., Singh Rupachandra L. (2025). EFFECT OF METAL IONS ON THE CYTOSOLIC NADP+- DEPENDENT ISOCITRATE DEHYDROGENASE FROM GERMINATING BLACKGRAM, VIGNA MUNGO (L.) HEPPER. Indian Journal of Agricultural Research. 40(4): 267 - 271. doi: .

ABSTRACT

The cytosolic NADP+-dependent isocitrate dehydrogenase from germinating blackgram shows
an absolute requirement of a divalent metal ion such as Mn2+ or Mg2+ for expression of its full
activity. Other metal ions like Co2+, Zn2+ and Cu2+ could also activate the enzyme, though the
degree of activation was lower than that of either Mn2+ or Mg2+ at the same concentration. In
contrast, three metal ions Sn2+, Ba2+ and Ca2+ were found to be inhibitory. The kinetics analysis with Mn2+ shows sigmoidal response suggestive of a positive co-operativity in metal ion binding. The A0.5 was 3.3 μM as deduced from a Hill plot with a Hill coefficient value of 2.1.

KEYWORDS

    REFERENCES

    1. Chen, R. et al. (1988). Eur. J. Biol. Chem., 175: 565-572.
    2. Curry, R.A. and Ting, I.P. (1976). Biochem Biophys., 176: 501-509
    3. Henson, C.A. et al. (1986). Physiol. Plant., 67: 538-544.
    4. Kaur, A. et al. (1996). J. Plant Biochem. Biotechnol., 5: 55-58.
    5. Kratochvil, B. et al. (1967). Anal. Chem., 39: 45-51.
    6. Lowry, O.H. et al. (1951). J. Biol. Chem., 193: 265-275.
    7. Murakami, K. et al. (1997). Biometals., 10: 169-174.
    8. Randall, D.D. and Givan, C.V. (1981). Plant Physiol., 68: 70-73.
    9. Satoh, Y. (1972). Plant Cell Physiol., 13: 493-503.
    10. Satoh, Y. and Nakamura, Y. (1984). Physiol. Plant., 62: 561-565
    11. Srivastava, P.K. and Singh, D.S. (2001). Indian J. Biochem. Biophys., 38: 335-341.
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    Indian Journal of Agricultural Research
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      volume 40 issue 4 (december 2006) : 267 - 271

      EFFECT OF METAL IONS ON THE CYTOSOLIC NADP+- DEPENDENT ISOCITRATE DEHYDROGENASE FROM GERMINATING BLACKGRAM, VIGNA MUNGO (L.) HEPPER

      M
      M. Ayub Ali*
      W
      W. Joykumar Singh
      L
      L. Inaotombi Devi
      S
      S. Kunjeshwori Devi
      L
      L. Rupachandra Singh
      1Department of Biochemistry, Manipur University, Canchipur - 795 003, Manipur

      • Submitted|

      • First Online |

      • doi

      Cite article:- Ali* Ayub M., Singh Joykumar W., Devi Inaotombi L., Devi Kunjeshwori S., Singh Rupachandra L. (2025). EFFECT OF METAL IONS ON THE CYTOSOLIC NADP+- DEPENDENT ISOCITRATE DEHYDROGENASE FROM GERMINATING BLACKGRAM, VIGNA MUNGO (L.) HEPPER. Indian Journal of Agricultural Research. 40(4): 267 - 271. doi: .

      ABSTRACT

      The cytosolic NADP+-dependent isocitrate dehydrogenase from germinating blackgram shows
      an absolute requirement of a divalent metal ion such as Mn2+ or Mg2+ for expression of its full
      activity. Other metal ions like Co2+, Zn2+ and Cu2+ could also activate the enzyme, though the
      degree of activation was lower than that of either Mn2+ or Mg2+ at the same concentration. In
      contrast, three metal ions Sn2+, Ba2+ and Ca2+ were found to be inhibitory. The kinetics analysis with Mn2+ shows sigmoidal response suggestive of a positive co-operativity in metal ion binding. The A0.5 was 3.3 μM as deduced from a Hill plot with a Hill coefficient value of 2.1.

      KEYWORDS

        REFERENCES

        1. Chen, R. et al. (1988). Eur. J. Biol. Chem., 175: 565-572.
        2. Curry, R.A. and Ting, I.P. (1976). Biochem Biophys., 176: 501-509
        3. Henson, C.A. et al. (1986). Physiol. Plant., 67: 538-544.
        4. Kaur, A. et al. (1996). J. Plant Biochem. Biotechnol., 5: 55-58.
        5. Kratochvil, B. et al. (1967). Anal. Chem., 39: 45-51.
        6. Lowry, O.H. et al. (1951). J. Biol. Chem., 193: 265-275.
        7. Murakami, K. et al. (1997). Biometals., 10: 169-174.
        8. Randall, D.D. and Givan, C.V. (1981). Plant Physiol., 68: 70-73.
        9. Satoh, Y. (1972). Plant Cell Physiol., 13: 493-503.
        10. Satoh, Y. and Nakamura, Y. (1984). Physiol. Plant., 62: 561-565
        11. Srivastava, P.K. and Singh, D.S. (2001). Indian J. Biochem. Biophys., 38: 335-341.
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