...Ju-Yi Hsieh; Jyung-Hurng Liu; Yi-Wen Fang; Hui-Chih Hung Human m-NAD(P)-ME [mitochondrial NAD(P) + -dependent ME (malic enzyme)] is a homotetramer, which is allosterically activated by the binding of fumarate. The fumarate-binding site is located at the dimer interface of the NAD(P)-ME...

...Cheng-Chin Kuo; Kuan-Yu Lin; Yau-Jung Hsu; Shu-Yu Lin; Yu-Tsen Lin; Gu-Gang Chang; Wei-Yuan Chou The role of general acid–base catalysis in the enzymatic mechanism of NADP + -dependent malic enzyme was examined by detailed steady-state kinetic studies through site-directed mutagenesis of the Tyr 91...

...Hui-Chih Hung; Meng-Wei Kuo; Gu-Gang Chang; Guang-Yaw Liu Human mitochondrial NAD(P) + -dependent malate dehydrogenase (decarboxylating) (malic enzyme) can be specifically and allosterically activated by fumarate. X-ray crystal structures have revealed conformational changes in the enzyme...

...Enrique DETARSIO; Carlos S. ANDREO; María F. DRINCOVICH C 4 -specific (photosynthetic) NADP + -dependent malic enzyme (NADP + -ME) has evolved from C 3 -malic enzymes and represents a unique and specialized form, as indicated by its particular kinetic and regulatory properties. In the present paper...

...Yen-I CHEN; Yu-Hou CHEN; Wei-Yuan CHOU; Gu-Gang CHANG The cytosolic malic enzyme from pigeon liver is very sensitive to the metal-catalysed oxidation systems. Our previous studies using the Cu 2+ –ascorbate as the oxidation system showed that the enzyme was oxidized and cleaved at several positions...