Ontology highlight
ABSTRACT:
SUBMITTER: Di Costanzo L
PROVIDER: S-EPMC2850953 | biostudies-literature | 2010 Apr
REPOSITORIES: biostudies-literature
Archives of biochemistry and biophysics 20100212 2
Human arginase I is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of L-arginine to generate L-ornithine and urea. We demonstrate that N-hydroxy-L-arginine (NOHA) binds to this enzyme with K(d)=3.6 microM, and nor-N-hydroxy-L-arginine (nor-NOHA) binds with K(d)=517 nM (surface plasmon resonance) or K(d) approximately 50 nM (isothermal titration calorimetry). Crystals of human arginase I complexed with NOHA and nor-NOHA afford 2.04 and 1.55 A resolution structures, respectively ...[more]