THE RELATIONSHIP BETWEEN CATION-INDUCED SUBSTRATE CONFIGURATION AND ENZYMATIC ACTIVITY OF PHOSPHATIDATE PHOSPHOHYDROLASE FROM HUMAN LIVER

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HAGHIGHI B.; YARI M.; TORI SH.

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Journal: Iranian Biomedical Journal Year:2000 | Volume:4 | Issue:1 Page(s): 13-19

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Title

THE RELATIONSHIP BETWEEN CATION-INDUCED SUBSTRATE CONFIGURATION AND ENZYMATIC ACTIVITY OF PHOSPHATIDATE PHOSPHOHYDROLASE FROM HUMAN LIVER

Author(s)

HAGHIGHI B. | YARI M. | TORI SH. | Issue Writer Certificate

Keywords

PHOSPHATIDATE

PHOSPHOHYDROLASE

PHOSPHATIDIC ACID

Abstract

The mechanism by which bi-and trivalent cations affect human liver PHOSPHATIDATE PHOSPHOHYDROLASE (PAP) activity was investigated. Bivalent cations up to 1 mM increased PAP activity whereas at higher concentrations the activity of the enzyme decreased. The stimulatory concentration for trivalent cations such as Al3+ and Cr3+, however, was much lower being 2 m M and 1 m M, respectively. All cations affecting PAP activity were also able to induce phase transition of PHOSPHATIDATE from lamellar (La) to inverted hexagonal (HII) form. The rate of La-HII transition was different for each cation. At 100 mM concentration of Mg2+ only 26% of the original PHOSPHATIDATE remained in La form and for other cations tested ranged from 14.5% to 76%. The phase transition was blocked by EDTA. Magnesium from 0.8 to 1.5 mM concentration raised PAP activity (3-fold) with La form of substrate but not with the HII phase. Monovalent cations such as Na+ and K+ neither affected enzyme activity nor substrate configuration. These data suggest that cation-induced PAP activation is not as a result of cation-protein interaction, but is due to formation of a suitable substrate configuration for the enzyme catalysis during PHOSPHATIDATE phase transition. It appears that the real substrate configuration for PAP activity is situated between La and HII phases.

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APA: Copy

HAGHIGHI, B., YARI, M., & TORI, SH.. (2000). THE RELATIONSHIP BETWEEN CATION-INDUCED SUBSTRATE CONFIGURATION AND ENZYMATIC ACTIVITY OF PHOSPHATIDATE PHOSPHOHYDROLASE FROM HUMAN LIVER . IRANIAN BIOMEDICAL JOURNAL, 4(1), 13-19. SID. https://sid.ir/paper/277027/en

Vancouver: Copy

HAGHIGHI B., YARI M., TORI SH.. THE RELATIONSHIP BETWEEN CATION-INDUCED SUBSTRATE CONFIGURATION AND ENZYMATIC ACTIVITY OF PHOSPHATIDATE PHOSPHOHYDROLASE FROM HUMAN LIVER . IRANIAN BIOMEDICAL JOURNAL[Internet]. 2000;4(1):13-19. Available from: https://sid.ir/paper/277027/en

IEEE: Copy

B. HAGHIGHI, M. YARI, and SH. TORI, “THE RELATIONSHIP BETWEEN CATION-INDUCED SUBSTRATE CONFIGURATION AND ENZYMATIC ACTIVITY OF PHOSPHATIDATE PHOSPHOHYDROLASE FROM HUMAN LIVER ,” IRANIAN BIOMEDICAL JOURNAL, vol. 4, no. 1, pp. 13–19, 2000, [Online]. Available: https://sid.ir/paper/277027/en

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