Ribonucleotide Reductase Protein R1; domain 1
Reductive carboxylate cycle (CO2 fixation)
Enzyme catalysis: conflicting requirements of substrate access and transition state affinity.
Physicochemical, catalytic, and immunochemical properties of fumarases crystallized separately from mitochondrial and cytosolic fractions of rat liver.
Spin ECHO proton NMR studies of the metabolism of malate and fumarate in human erythrocytes. Dependence on free NAD levels.
Purification, crystallization, and preliminary X-ray data for porcine fumarase.
Proton transfer in catalysis by fumarase.
Purification, characterization and preliminary X-ray study of fumarase from Saccharomyces cerevisiae.
Purification and crystallization of fumarase C from Escherichia coli.
Kinetics of enzymes with iso-mechanisms: dead-end inhibition of fumarase and carbonic anhydrase II.
The multisubunit active site of fumarase C from Escherichia coli.
Importance of historical contingency in the stereochemistry of hydratase-dehydratase enzymes.
Purification and characterization of fumarase from the syntrophic propionate-oxidizing bacterium strain MPOB.
Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli.
Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site.
Pig heart fumarase contains two distinct substrate-binding sites differing in affinity.
Crystal structures of native and recombinant yeast fumarase.
The pi-helix translates structure into function.
Conversion of fumaric acid to L-malic by sol-gel immobilized Saccharomyces cerevisiae in a supported liquid membrane bioreactor.
X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation.
The role of the allosteric B site in the fumarase reaction.
Structure of free fumarase C from Escherichia coli.
This enzyme has got two binding sites for malate, site A and site B. The site A is close to the catalytic site, whereas the site B seems to be allosteric site. Although the PDB structures, 1fuo, 1fup, 1fur and 1kq7, bind malate (MLT), they are bound to the site B. This enzyme is homologous to argininosuccinate lyase (T00094 in EzCatDB), and the catalytic residues are conserved. Thus, the reaction might be similar to that of the homologue.