Thermolabile alkaline phosphatase from Northern shrimp ( Pandalus borealis): protein and cDNA sequence analyses

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 alkali...

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Bibliographic Details
Published in:Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 2001-07, Vol.129 (4), p.853-861
Main Authors: Nilsen, Inge W., Øverbø, Kersti, Olsen, Ragnar L.
Format: Article
Language:English
Subjects:
alkaline phosphatase
Alkaline phosphatase (EC 3.1.3.1)
Alkaline Phosphatase - chemistry
Alkaline Phosphatase - genetics
Amino Acid Sequence
Amino Acids - chemistry
Animals
Base Sequence
Binding Sites
cDNA
Cold Temperature
DNA, Complementary - metabolism
Electrophoresis, Polyacrylamide Gel
Hepatopancreas
Marine
Molecular Sequence Data
Pandalidae
Pandalus borealis
Protein
Sequence alignment
Sequence Homology, Amino Acid
Shrimp
Software
Temperature
Thermolabile
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Summary: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.
ISSN:1096-4959
1879-1107
DOI:10.1016/S1096-4959(01)00391-8