IDENTIFYING OF ESSENTIAL HISTIDIN RESIDUES IN CATALYTIC FUNCTION OF PHOSPHATIDATE PHOSPHOHYDROLASE ENZYME AT THE ACTIVE SITE OF RAT LIVER PLASMA MEMBRANE

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HEYDARIAN ESFANDIAR; HAGHIGHI BAHRAM

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Journal: Feyz Medical Sciences Journal Year:2008 | Volume:12 | Issue:2 (SERIAL 46) Page(s): 0-0

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Title

IDENTIFYING OF ESSENTIAL HISTIDIN RESIDUES IN CATALYTIC FUNCTION OF PHOSPHATIDATE PHOSPHOHYDROLASE ENZYME AT THE ACTIVE SITE OF RAT LIVER PLASMA MEMBRANE

Author(s)

HEYDARIAN ESFANDIAR | HAGHIGHI BAHRAM | Issue Writer Certificate

Keywords

PHOSPHATIDATE PHOSPHATASEQ3

HISTIDINEQ2

DIETHYL PYROCARBONATEQ3

PHOSPHATIDIC ACIDQ3

Abstract

Background: Phosphatidate phosphohydrolase enzyme (PAP) catalyzes the transformation of PHOSPHATIDIC ACID to Pi and diacylglycerol. Two different forms of PAP have been reported in rat hepatocytes: PAP1 which participates in the synthesis of phospholipids and triacylglycerols, and PAP2 which is primarily involved in lipid signaling transduction. PAP2 has two isoforms n amely PAP2a and PAP2b. In this study, the role of essential HISTIDINE residues in PAP2b was assessed.Materials and Methods: The rat liver plasma membrane was solved using N-octyle glycoside and PAP2b purified during several chromatography steps. The fixed kenitics were assessed based on superficial kenitic dilution model. Gel electrophoresis (SDS-PAGE) was discontinually performed to evaluate the purity, quantity and molecular weight measurement of enzyme subunit in gel 10%. The number of existing HISTIDINE moles in one enzyme mole (purification) was determined based on the formation of N-carbetoxy HISTIDINE.Results: Specific activity of the purified enzyme (PAP2b) was 7350 mu/mg protein. PAP2b electrophoresis showed only a single band on SDS-PAGE with a mass weight of 33.8 Kd. The PAP2b was inactivated by diethylpyrocarbonate (DEPC). The inhibition was competitive with respect to phosphatidate and there were 6 modified moles of HISTIDINE residues per mole of PAP2b.Conclusion: The data have shown that the incubation of PAP2b by DEPC plus phosphatidate can prevent the inhibitory effect of DEPC on enzyme activity. Our findings also revealed the role of HISTIDINE in the active site of PAP2b.This enzyme is likely to have the same hydrolysis catalytic mechanism as its super family through a phosphohistidine intermediate.

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APA: Copy

HEYDARIAN, ESFANDIAR, & HAGHIGHI, BAHRAM. (2008). IDENTIFYING OF ESSENTIAL HISTIDIN RESIDUES IN CATALYTIC FUNCTION OF PHOSPHATIDATE PHOSPHOHYDROLASE ENZYME AT THE ACTIVE SITE OF RAT LIVER PLASMA MEMBRANE. FEYZ, 12(2 (SERIAL 46)), 0-0. SID. https://sid.ir/paper/40628/en

Vancouver: Copy

HEYDARIAN ESFANDIAR, HAGHIGHI BAHRAM. IDENTIFYING OF ESSENTIAL HISTIDIN RESIDUES IN CATALYTIC FUNCTION OF PHOSPHATIDATE PHOSPHOHYDROLASE ENZYME AT THE ACTIVE SITE OF RAT LIVER PLASMA MEMBRANE. FEYZ[Internet]. 2008;12(2 (SERIAL 46)):0-0. Available from: https://sid.ir/paper/40628/en

IEEE: Copy

ESFANDIAR HEYDARIAN, and BAHRAM HAGHIGHI, “IDENTIFYING OF ESSENTIAL HISTIDIN RESIDUES IN CATALYTIC FUNCTION OF PHOSPHATIDATE PHOSPHOHYDROLASE ENZYME AT THE ACTIVE SITE OF RAT LIVER PLASMA MEMBRANE,” FEYZ, vol. 12, no. 2 (SERIAL 46), pp. 0–0, 2008, [Online]. Available: https://sid.ir/paper/40628/en

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