Ribonucleotide Reductase Protein R1; domain 1
6-N-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming)
Metabolism of threo-beta-fluoroaspartate by H4 cells. Inhibition of adenylosuccinate lyase by fluoro analogs of its substrates.
The multisubunit active site of fumarase C from Escherichia coli.
The purB gene of Escherichia coli K-12 is located in an operon.
Crystallization and preliminary structural analysis of Bacillus subtilis adenylosuccinate lyase, an enzyme implicated in infantile autism.
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of Bacillus subtilis.
A key role in catalysis for His89 of adenylosuccinate lyase of Bacillus subtilis.
The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds.
The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway.
Three subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are required.
This enzyme catalyzes two similar reactions, in which fumarate will be cut from nucleotide derivatives. The active site and catalytic mechanism seem to be shared by these reactions.