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

被引：33

作者：

Nilsen, IW ^{[1
]}

Overbo, K ^{[1
]}

Olsen, RL ^{[1
]}

机构：

[1] Norwegian Inst Fisheries & Aquaculture Ltd, Ctr Marine Biotechnol, N-9291 Tromso, Norway

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 2001年 / 129卷 / 04期

关键词：

shrimp; hepatopancreas; alkaline phosphatase (EC 3.1.3.1); thermolabile; cDNA; protein; sequence alignment;

D O I：

10.1016/S1096-4959(01)00391-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：853 / 861

页数：9

共 34 条

[1] Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].

Altschul, SF ;

Madden, TL ;

Schaffer, AA ;

Zhang, JH ;

Zhang, Z ;

Miller, W ;

Lipman, DJ .

NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402

[2]

[Anonymous], METHOD ENZYMOL

[3] ALKALINE-PHOSPHATASE FROM ATLANTIC COD (GADUS-MORHUA) - KINETIC AND STRUCTURAL-PROPERTIES WHICH INDICATE ADAPTATION TO LOW-TEMPERATURES [J].

ASGEIRSSON, B ;

HARTEMINK, R ;

CHLEBOWSKI, JF .

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 1995, 110 (02) :315-329

[4] FUNCTION OF ARGININE-166 IN THE ACTIVE-SITE OF ESCHERICHIA-COLI ALKALINE-PHOSPHATASE [J].

CHAIDAROGLOU, A ;

BREZINSKI, DJ ;

MIDDLETON, SA ;

KANTROWITZ, ER .

BIOCHEMISTRY, 1988, 27 (22) :8338-8343

[5] Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B [J].

Chessa, JP ;

Feller, G ;

Gerday, C .

CANADIAN JOURNAL OF MICROBIOLOGY, 1999, 45 (06) :452-457

[6] TISSUE-NONSPECIFIC ALKALINE-PHOSPHATASE PARTICIPATES IN THE ESTABLISHMENT AND GROWTH OF FEATHER GERMS IN EMBRYONIC CHICK SKIN CULTURES [J].

CRAWFORD, K ;

WEISSIG, H ;

BINETTE, F ;

MILLAN, JL ;

GOETINCK, PF .

DEVELOPMENTAL DYNAMICS, 1995, 204 (01) :48-56

[7] Purification and characterization of two extracellular alkaline phosphatases from a psychrophilic Arthrobacter isolate [J].

dePrada, P ;

Brenchley, JE .

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1997, 63 (07) :2928-2931

[8]

Fernley H., 1971, The Enzymes, V4, P417

[9] ISOLATION AND PROPERTIES OF A SMALL MANGANESE-ION-STIMULATED BACTERIAL ALKALINE-PHOSPHATASE [J].

FITT, PS ;

PETERKIN, PI .

BIOCHEMICAL JOURNAL, 1976, 157 (01) :161-167

[10] A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases [J].

Galperin, MY ;

Bairoch, A ;

Koonin, EV .

PROTEIN SCIENCE, 1998, 7 (08) :1829-1835

← 1 2 3 4 →