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PMID: 7022451 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Amino acid sequence of Escherichia coli alkaline phosphatase.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 78 ·No. 6 ·1981-06-00 ·Pages 3473-7

Bradshaw RA, Cancedda F, Ericsson LH, Neumann PA, Piccoli SP, Schlesinger MJ, Shriefer K, Walsh KA

Abstract

The complete amino acid sequence of the Escherichia coli alkaline phosphatase subunit [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1, isozyme 3] has been determined. The monomer contains 449 amino acid residues in a single unglycosylated polypeptide chain having a calculated Mr of 47,029. Isozyme 1 has an additional arginine residue at the NH2 terminus that presumably results from variability in processing of precursor molecules. Sequence data were obtained from both manual and automatic Edman degradation of the tryptic and cyanogen bromide peptides, as well as other peptides derived therefrom. The two disulfide bonds were determined from analyses of the appropriate peptic peptides. This structure confirms earlier reports of the sequence surrounding the active-site serine and both the NH2- and COOH-terminal cyanogen bromide fragments. A secondary structure prediction places nearly half the residues in alpha-helical segments that have 13% and 16%, respectively, in beta-strand and beta-turn orientations.

MeSH Terms
Alkaline Phosphatase Amino Acid Sequence Binding Sites Catalysis Escherichia coli/enzymology Isoenzymes Peptide Fragments Structure-Activity Relationship
Chemicals
Isoenzymes Peptide Fragments Alkaline Phosphatase
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Bradshaw R A
Cancedda F
Ericsson L H
Neumann P A
Piccoli S P
Schlesinger M J
Shriefer K
Walsh K A
References (32)
32 references, click to expand
  1. Escherichia coli alkaline phosphatase. Metal binding, protein conformation, and quaternary structure.
    J Biol Chem. 1969 Jan 25;244(2):308-18 PMID: 4886432
  2. THE AMINO ACID SEQUENCE OF A TETRADECAPEPTIDE CONTAINING THE REACTIVE SERINE IN E. COLI ALKALINE PHOSPHATASE.
    Proc Natl Acad Sci U S A. 1963 May;49(5):722-9 PMID: 16591094
  3. A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase.
    Biochim Biophys Acta. 1960 Mar 11;38:470-83 PMID: 13826559
  4. Essential arginyl residues in Escherichia coli alkaline phosphatase.
    Biochemistry. 1974 Jul 2;13(14):2865-71 PMID: 4601722
  5. Fluorotyrosine alkaline phosphatase from Escherichia coli: preparation, properties, and fluorine-19 nuclear magnetic resonance spectrum.
    Proc Natl Acad Sci U S A. 1974 Feb;71(2):469-73 PMID: 4592693
  6. Effect of magnesium on the properties of zinc alkaline phosphatase.
    Biochemistry. 1977 Feb 22;16(4):610-4 PMID: 13822
  7. Alkaline phosphatase of Escherichia coli. Composition.
    Biochemistry. 1968 Dec;7(12):4336-42 PMID: 4882707
  8. On the active site of horse-liver ali esterase. II. Amino acid sequence in the DFP-binding site of the enzyme.
    Biochim Biophys Acta. 1959 Jun;33(2):396-403 PMID: 13670910
  9. Spectroscopic determination of tryptophan and tyrosine in proteins.
    Biochemistry. 1967 Jul;6(7):1948-54 PMID: 6049437
  10. Alkaline phosphatase of Escherichia coli: a zinc metalloenzyme.
    Biochemistry. 1962 May 25;1:373-8 PMID: 14487220
  11. Characterization of the histidine residues in alkaline phosphatase by carbon-13 nuclear magnetic resonance.
    Biochemistry. 1980 Aug 19;19(17):4011-21 PMID: 6996713
  12. Peptide separations on substituted polystyrene resins. Effect of cross-linkage.
    J Chromatogr. 1980 Jan 4;187(1):27-33 PMID: 7358820
  13. Two differentiable classes of metal atoms in alkaline phosphatase of Escherichia coli.
    Biochemistry. 1968 Dec;7(12):4343-50 PMID: 4882708
  14. Chemical nature of the DFP-binding site of pseudocholinesterase.
    Biochim Biophys Acta. 1959 Aug;34:573-5 PMID: 14406769
  15. A crystallographic study of alkaline phosphatase at 7-7 Angstrom resolution.
    J Mol Biol. 1973 Mar 15;74(4):533-45 PMID: 4580906
  16. PURIFICATION AND CRYSTALLIZATION OF THE ALKALINE PHOSPHATASE OF ESCHERICHIA COLI.
    Biochemistry. 1964 Dec;3:1893-7 PMID: 14269306
  17. Molecular heterogeneity in the amino-terminal region of alkaline phosphatase.
    J Mol Biol. 1970 May 14;49(3):577-88 PMID: 4916549
  18. The reversible dissociation of the alkaline phosphatase of Escherichia coli. I. Formation and reactivation of subunits.
    J Biol Chem. 1965 Nov;240(11):4284-92 PMID: 4954367
  19. THE AMINO ACID SEQUENCE AROUND THE REACTIVE SERINE IN CALF-INTESTINAL ALKALINE PHOSPHATASE.
    Biochim Biophys Acta. 1964 Oct 23;92:79-84 PMID: 14243791
  20. The amino acid sequence around the reactive serine residue in alkaline phosphatase of Serratia marcescens.
    Biochem J. 1964 Aug;92(2):421-2 PMID: 5320081
  21. Protein fingerprinting by SDS-gel electrophoresis after partial fragmentation with CNBr.
    Anal Biochem. 1979 Sep 1;97(2):382-6 PMID: 525799
  22. Molecular heterogeneity of alkaline phosphatase.
    FEBS Lett. 1973 Jan 1;29(1):55-57 PMID: 11946907
  23. Characterization of the properties of the multiple metal binding sites in alkaline phosphatase by carbon-13 nuclear magnetic resonance.
    Biochemistry. 1980 Aug 19;19(17):4021-30 PMID: 6996714
  24. [The alkaline isophosphatases of Escherichia coli. Isolation, kinetic and structural properties].
    Biochim Biophys Acta. 1967 Oct 23;147(2):280-8 PMID: 4864146
  25. Amino-acid sequence about the reactive serine of a proteolytic enzyme from Bacillus subtilis.
    Nature. 1960 Sep 3;187:872-3 PMID: 14441480
  26. On the structure of chymotrypsin.
    Brookhaven Symp Biol. 1962 Dec;15:85-100 PMID: 13953113
  27. Prediction of the secondary structure of proteins from their amino acid sequence.
    Adv Enzymol Relat Areas Mol Biol. 1978;47:45-148 PMID: 364941
  28. Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: the influence of zinc on protein structure and a conformational change induced by phosphate binding.
    Biochemistry. 1976 Apr 6;15(7):1535-46 PMID: 4091
  29. Fingerprint analysis of alkaline phosphatase of Escherichia coli K12.
    J Mol Biol. 1963 Apr;6:330-40 PMID: 13975373
  30. Amino acid sequence of Escherichia coli alkaline phosphatase. Amino- and carboxyl-terminal sequences and variations between two isozymes.
    Biochemistry. 1973 Aug 28;12(18):3499-503 PMID: 4581334
  31. Multiple molecular forms of the alkaline phosphatase of Escherichia coli.
    Ann N Y Acad Sci. 1968 Jun 14;151(1):159-70 PMID: 4887360
  32. Conformational states of the subunit of Escherichia coli alkaline phosphatase.
    Biochemistry. 1967 Nov;6(11):3552-9 PMID: 4864145
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.78.6.3473
Published
1981-06-00
Pages
3473-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC319591
Subset
IM
Grants
NIADDK NIH HHS · AM 13362 · United States
NIGMS NIH HHS · GM 15731 · United States
External Links
PubMed source DOI: 10.1073/pnas.78.6.3473 PMC Full Text View journal details
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