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

Comp Biochem Physiol B Biochem Mol Biol. 2001 Jul;129(4):853-61. doi: 10.1016/s1096-4959(01)00391-8.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaline Phosphatase / chemistry*
  • Alkaline Phosphatase / genetics*
  • Amino Acid Sequence
  • Amino Acids / chemistry
  • Animals
  • Base Sequence
  • Binding Sites
  • Cold Temperature
  • DNA, Complementary / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Molecular Sequence Data
  • Pandalidae
  • Sequence Homology, Amino Acid
  • Software
  • Temperature

Substances

  • Amino Acids
  • DNA, Complementary
  • Alkaline Phosphatase