Leucine Dehydrogenase; Chain A, domain 1
malate dehydrogenase (oxaloacetate-decarboxylating)
GLU 271;ASP 272;ASP 295(Divalent metal binding)
GLU 255;ASP 256;ASP 279(Divalent metal binding)
GLU 1255;ASP 1256;ASP 1279(Divalent metal binding)
GLU 2255;ASP 2256;ASP 2279(Divalent metal binding)
GLU 3255;ASP 3256;ASP 3279(Divalent metal binding)
GLU 4255;ASP 4256;ASP 4279(Divalent metal binding)
GLU 5255;ASP 5256;ASP 5279(Divalent metal binding)
GLU 6255;ASP 6256;ASP 6279(Divalent metal binding)
GLU 7255;ASP 7256;ASP 7279(Divalent metal binding)
Modification of a thiol at the active site of the Ascaris suum NAD-malic enzyme results in changes in the rate-determining steps for oxidative decarboxylation of L-malate.
Kinetic mechanism of NAD:malic enzyme from Ascaris suum in the direction of reductive carboxylation.
Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation.
A comparison of the secondary structure of human brain mitochondrial and cytosolic 'malic' enzyme investigated by Fourier-transform infrared spectroscopy.
Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex.
Mapping the active site topography of the NAD-malic enzyme via alanine-scanning site-directed mutagenesis.
Crystal structure of human mitochondrial NAD(P)(+)-dependent malic enzyme: a new class of oxidative decarboxylases.
Potent and competitive inhibition of malic enzymes by lanthanide ions.
Structure of a closed form of human malic enzyme and implications for catalytic mechanism.
Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution.
Molecular mechanism for the regulation of human mitochondrial NAD(P)+-dependent malic enzyme by ATP and fumarate.
Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site.
Crystal structures of substrate complexes of malic enzyme and insights into the catalytic mechanism.
Dual functional roles of ATP in the human mitochondrial malic enzyme.
Metal-Induced reversible structural interconversion of human mitochondrial NAD(P)+-dependent malic enzyme.
There are several types of malate deydrogenases. 1.1.1.37: Malate dehydrogenase / bacteria, rat, porcine 1.1.1.38: Malate dehydrogenase (oxaloacetate decarboxylating) / Human, Ascaris suum 1.1.1.39: Malate dehydrogenase (decarboxylating) 1.1.1.82: Malate dehydrogenase (NADP+) / Archaea, plant 1.1.1.40: Malate dehydrogenase (oxaloacetate decarboxylating) (NADP+) / pigeon 1.1.1.83: D-malate dehydrogenase (decarboxylating) This enzyme catalyzes the following reactions: (A) Hydride transfer from substrate, (S)-Malate, to NAD+, giving oxaloacetate and NADH: (B) Eliminative double-bond formation; Elimination of CO2 from oxaloacetate, giving enolpyruvate: (C) Isomerization (shift of double-bond position; from C=C-O to C-C=O):