Document Detail


Amino acid residues essential for catalysis by peptidyl dipeptidase-4 from Pseudomonas maltophilia.
MedLine Citation:
PMID:  2563225     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
To assess residues essential for catalysis by prokaryotic peptidyl dipeptidase-4, the enzyme was subjected to chemical modification by a series of reagents. Treatment with either tetranitromethane or N-acetylimidazole abolished catalytic activity. Hydroxylamine reversed inactivation by acetylimidazole only. Thus, an essential tyrosine is indicated. Enzymatic activity also was quenched by either trinitrobenzenesulfonic acid or diethyl pyrocarbonate. Inactivation by these reagents was not reversed by hydroxylamine. These data suggest an essential lysine. The competitive inhibitor Phe-Arg protected partially against inactivation by tetranitromethane, and fully against inactivation by N-acetylimidazole. The substrate Hip-Phe-Arg protected against inactivation by trinitrobenzenesulfonic acid and diethyl pyrocarbonate. Thus, both tyrosine and lysine are located at the catalytic site.
Authors:
J J Lanzillo; Y Dasarathy; B L Fanburg
Related Documents :
7861715 - Acquired essential fatty acid depletion in the remnant kidney: amelioration with u-63557a.
583255 - The effect of essential fatty acid deprivation on the metabolic transformations of [1(-...
7300595 - Desaturation of endogenous and exogenous palmitate in lung tissue in vitro.
40605 - Studies on the nature of the catalytically essential ionizing group of plasmin with pk ...
15133155 - Metabolic fate of jasmonates in tobacco bright yellow-2 cells.
1805795 - Effect on immunoreactivity of gonadotropin releasing hormone (gnrh) in the gnrh-bsa con...
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  158     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1989 Jan 
Date Detail:
Created Date:  1989-02-17     Completed Date:  1989-02-17     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  45-51     Citation Subset:  IM    
Affiliation:
New England Medical Center Hospital, Department of Medicine, Boston, MA 02111.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Antigens, CD26
Catalysis
Diethyl Pyrocarbonate / pharmacology
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / antagonists & inhibitors,  metabolism*
Kinetics
Pseudomonas / enzymology*
Substrate Specificity
Tetranitromethane / pharmacology
Trinitrobenzenesulfonic Acid / pharmacology
Grant Support
ID/Acronym/Agency:
HL07053/HL/NHLBI NIH HHS; HL14456/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
1609-47-8/Diethyl Pyrocarbonate; 2508-19-2/Trinitrobenzenesulfonic Acid; 509-14-8/Tetranitromethane; EC 3.4.14.-/Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; EC 3.4.14.5/Antigens, CD26

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Metabolic responsiveness to phorbol ester and activity of protein kinase C in isolated hepatocytes f...
Next Document:  Infectious complications of cyclophosphamide treatment for vasculitis.