Journal : Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology , vol. 129 , p. 853–861 , 2001
Publisher : Elsevier
International Standard Numbers
Printed : 1096-4959
Electronic : 1879-1107
Publication type : Academic article
Issue : 4
If you have questions about the publication, you may contact Nofima’s Chief Librarian.
Sequence analysis of short fragments resulting from trypsin digestion of the thermolabile shrimp alkaline phosphatase (SAP) from Northern shrimp Pandalus borealis formed the basis for amplification of its encoding cDNA. The predicted protein sequence was recognized as containing the consensus alkaline phosphatase motif comprising the active site of this protein family. Protein sequence homology searches identified several eukaryote alkaline phosphatases with which the 475-amino acid SAP polypeptide revealed shares 45% amino;acid sequence identity. Residues for potential metal binding seem to be conserved in these proteins. The predicted 54-kDa molecular mass of SAP is smaller than previously reported, but is consistent with our recent SDS-PAGE analysis of the native protein. Compared to its homologs, the shrimp enzyme has a surplus of negatively charged amino acids, while the relative number of prolines is lower and the frequency of aromatic residues is higher than in mesophilic counterparts. (C) 2001 Elsevier Science Inc. All rights reserved.