Abstract
The complete amino acid sequence of the hydantoinase from Arthrobacter
aurescens DSM 3745 has been derived by automated Edman degradation. This
is the fi rst ever reported amino acid sequence of a non-ATP-dependent
hydantoinase, which hydrolyzes 5'-monosubstituted hydantoin derivatives
L-selectively, A homology search performed in protein and nucleic acid
databases retrieved only distantly related proteins. All of these are
members of the recently described protein superfamily of amidohydrolases
related to ureases (Holm and Sander, Proteins 28: 72-82, 1997).
Phylogenetic analysis revealed that the novel hydantoinase forms a new
branch separate from other hydantoin cleaving enzymes like
dihydropyrimidinases (EC 3.5.2.2) and allantoinases (EC 3,5,2.5), Our
results suggests that the enzymes of this protein superfamily have
evolved from a common ancestor and therefore are the product of
divergent evolution, We show further that the enclosed gene families
developed very early in evolution, probably prior to the formation of
the three domains, Archaea, Eukarya and Bacteria, Hydantoinases related
to ATP-depdent N-methylhydantoinases (EC 3.5.2.14) or 5-oxoprolinases
(EC 3.5.2.9) do not belong to this superfamily.
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