D-hydantoinase Protein, Arthrobacter crystallopoietes (His)

D-hydantoinase exhibits a unique carbamylation profile in which a single lysine residue coordinates two divalent metal cations. This protein belongs to the metal-dependent hydrolase superfamily, specifically to the hydantoinase/dihydropyrimidase family. D-hydantoinase Protein, Arthrobacter crystallopoietes (His) is the recombinant D-hydantoinase protein, expressed by E. coli , with N-6*His labeled tag. The total length of D-hydantoinase Protein, Arthrobacter crystallopoietes (His) is 457 a.a., .

D-hydantoinase, a protein belonging to the metallo-dependent hydrolases superfamily and the hydantoinase/dihydropyrimidinase family, plays a crucial role in carbamylation, a process where a single lysine residue coordinates two divalent metal cations. This protein is involved in hydantoin hydrolysis, participating in the conversion of hydantoins to alpha-amino acids. The dual metal coordination underscores its significance in catalyzing these reactions. As a member of the metallo-dependent hydrolases superfamily, D-hydantoinase likely shares conserved structural and functional features with related enzymes. The ability to coordinate two metal cations further suggests a unique mechanism for substrate binding and catalysis within this enzyme family.

Others

E. coli

N-6*His

A0A1H1C1X0 (M1-R457)

/

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.