Iw. Nilsen et al., Thermolabile alkaline phosphatase from Northern shrimp (Pandalus borealis): protein and cDNA sequence analyses, COMP BIOC B, 129(4), 2001, pp. 853-861
Citations number
34
Categorie Soggetti
Biochemistry & Biophysics
Journal title
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
Sequence analysis of short fragments resulting from trypsin digestion of th
e thermolabile shrimp alkaline phosphatase (SAP) from Northern shrimp Panda
lus borealis formed the basis for amplification of its encoding cDNA. The p
redicted protein sequence was recognized as containing the consensus alkali
ne phosphatase motif comprising the active site of this protein family. Pro
tein sequence homology searches identified several eukaryote alkaline phosp
hatases with which the 475-amino acid SAP polypeptide revealed shares 45% a
mino;acid sequence identity. Residues for potential metal binding seem to b
e conserved in these proteins. The predicted 54-kDa molecular mass of SAP i
s smaller than previously reported, but is consistent with our recent SDS-P
AGE analysis of the native protein. Compared to its homologs, the shrimp en
zyme has a surplus of negatively charged amino acids, while the relative nu
mber of prolines is lower and the frequency of aromatic residues is higher
than in mesophilic counterparts. (C) 2001 Elsevier Science Inc. All rights
reserved.