探討人類粒線體蘋果酸酶之Arg67反丁烯二酸位點突變酶對結構之影響

陳韋霖

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探討人類粒線體蘋果酸酶之Arg67反丁烯二酸位點突變酶對結構之影響

Structural Studies of Arg67 Fumarate-Site Mutants of Human mitochondrial NAD(P)+-Dependent Malic Enzyme

陳韋霖 , Masters　　Advisor：洪慧芝　　

繁體中文

蘋果酸酶；結構； malic enzyme ； structure

Abstract │ Reference (40) │ Altmetrics

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Human mitochondrial NAD(P)+-dependent malic enzyme (m-NAD-ME, ME2) is a homotetramers structural protein. ME2 is one of three isoforms of malic enzyme. Human mitochondrial NAD(P)+-dependent malic enzyme compared to Human cytosolic NAD(P)+-dependent malic enzyme (c-NAD-ME, ME1) has allosteric site and exo-site. ME2 can regulate its enzyme activity by binding an allosteric regulatory of fumarate. There are four different types of structural configurations. Open I, II, and closed I, II will change according to the combination of fumarate and substrates. In order to investigate the difference in enzyme activity between human ME2 allosteric site mutants and wild type (WT), R67A, L79F, I88L and Y175N and the important single nucleotide polymorphism mutation R67Q, Q89P, was studied. By crystallization experiments, and use there crystal structure to further explore why these important enzymes have significant differences in enzyme activity when compared to WT. R67A, R67Q and I88L have very low enzyme activities. The structure of R67A and R67Q transit the closed form to the open form. I88L structure had no significant. The enzyme activity of Y175N is low, but it is activated by fumarate, and its configuration does not change significant; The structure of L79F and Q89P do not have higher electron signals for resulting the structure-related data even the crystal formation. The effects of ME2 structure changes and enzyme activity were explored by mutants of R67A, R67Q, I88L and Y175N.

Reference ( 40 ) 〈TOP〉

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