An essential tryptophan residue in alkaline phosphatase from pearl oyster (Pinctada fucata)

Alkaline phosphatases are ubiquitous enzymes found in most species including the pearl oyster, Pinctada fucata, where it is presumably involved in nacreous biomineralization processes. In the present study, we have purified alkaline phosphatases from the pearl oyster and modified the tryptophan resi...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2008-01, Vol.73 (1), p.87
Main Authors: Xie, Li-ping, Xu, Guang-rui, Cao, Wei-zhong, Zhang, Jin, Zhang, Rong-qing
Format: Article
Language:English
Subjects:
Binding sites
Biochemistry
Enzymes
Inactivation
Mineralization
Oysters
Residues
Substrates
Online Access:Get full text
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Summary:Alkaline phosphatases are ubiquitous enzymes found in most species including the pearl oyster, Pinctada fucata, where it is presumably involved in nacreous biomineralization processes. In the present study, we have purified alkaline phosphatases from the pearl oyster and modified the tryptophan residues using N-bromosuccinimide (NBS). We show that the resulting inactivation of purified alkaline phosphatase by NBS is dependent on modification of only one of five tryptophan residues in the enzyme. Substrate protection experiments showed that the tryptophan residue was not located at the substrate-binding site but was involved in the catalytic activity. [PUBLICATION ABSTRACT]
ISSN:0006-2979
1608-3040
DOI:10.1007/s10541-008-1013-1