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PMID: 2166336 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia.

Science (New York, N.Y.) ·Vol. 249 ·No. 4968 ·1990-08-03 ·Pages 553-6

Guan KL, Dixon JE

Abstract

Yersinia is the genus of bacteria that is the causative agent in plague or the black death, and on several occasions this organism has killed a significant portion of the world's population. An essential virulence determinant of Yersinia was shown to be a protein tyrosine phosphatase. The recombinant 50-kilodalton Yersinia phosphatase had a specificity for removal of phosphate from Tyr-containing as opposed to Ser/Thr-containing phosphopeptides and proteins. Site-directed mutagenesis was used to show that the Yersinia phosphatase possesses an essential Cys residue required for catalysis. Amino acids surrounding an essential Cys residue are highly conserved, as are other amino acids in the Yersinia and mammalian protein tyrosine phosphatases, suggesting that they use a common catalytic mechanism.

MeSH Terms
Amino Acid Sequence Kinetics Molecular Sequence Data Phosphoprotein Phosphatases/genetics,metabolism Protein Tyrosine Phosphatases Sequence Homology, Nucleic Acid Virulence/genetics Yersinia/enzymology,genetics,pathogenicity
Chemicals
Phosphoprotein Phosphatases Protein Tyrosine Phosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Guan K L
Department of Biochemistry, Purdue University, West Lafayette, IN 47907.
Dixon J E
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1990-08-03
Pages
553-6
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
PHS HHS · 18849 · United States
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