Subunit dissociation and stability alteration of d-hydantoinase deleted at the terminal amino acid residue

Abstract

Two variants of d-hydantoinase (HYD), created by deletion of one amino acid residue of at either the N- or C-terminus, were expressed in Escherichia coli and purified by two-step chromatography. Compared with HYD, HYDc1 with the C-terminal Arg deletion retained 43% activity, while HYDn1 with the N-terminal Ser deletion had no activity using dl-Hydantoin as… (More)
DOI: 10.1007/s10529-006-9238-9

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