Disease relevance of Atu3039

• In an attempt to select more efficient biocatalysts, the hydantoinase and carbamylase genes from Agrobacterium tumefaciens (formerly A. radiobacter) were cloned in Escherichia coli [1].
• One-step purification of insoluble hydantoinase overproduced in Escherichia coli [2].
• A hydantoinase from Arthrobacter aurescens DSM 3745 has been purified to homogeneity with a yield of 77% using a three-step purification procedure [3].

High impact information on Atu3039

• Hydantoin racemase enzyme together with a stereoselective hydantoinase and a stereospecific D-carbamoylase guarantee the total conversion from D,L-5-monosubstituted hydantoins with a low velocity of racemization to optically pure D-amino acids [4].
• D-Amino acids, important intermediates in the production of semisynthetic penicillins and cephalosporins, are currently prepared from the corresponding hydantoins using bacterial biomass containing two enzymes, hydantoinase and carbamylase [1].
• A. tumefacins hydantoinase was most active on 5,6-dihydrouracil and DL-5-methylhydantoin with only slight activity on DL-benzylhydantoin [5].
• The recombinant hydantoinase did not contain any affinity tags from the plasmid [6].
• D-Hydantoinase only was inactivated in the presence of 70 mM EDTA and at over 40 degrees C. The enzyme showed both hydantoinase and pyrimidinase activities, but only with the D-enantiomers of the substrates [7].

References