Article
Subunit dissociation and stability alteration of D hydantoinase deleted at the terminal amino acid residue.
Biotechnology letters - 1 Feb 2007
Niu Lixi, Zhang Xueyao, Shi Yawei, Yuan Jingming
Abstract excerpt
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 substrate. Based on HYD dimer with a molecular weight of...
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