The amidase domain of lipoamidase specifically inactivates lipolated proteins in vivo

PLoS ONE

Volumn 4, Issue 10, 2009, Pages

  Spalding, Maroya D ^a   Prigge, Sean T ^a  

^a JOHNS HOPKINS BLOOMBERG SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOACID DEHYDROGENASE; ALANINE; AMIDASE; BIOTIN; LIPOAMIDASE; UNCLASSIFIED DRUG; 2 OXOISOVALERATE DEHYDROGENASE (LIPOAMIDE); BIOTINIDASE; PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; BIOTINYLATION; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; IN VIVO STUDY; LIPOYLATION; MOLECULAR PROBE; NONHUMAN; PROTEIN CLEAVAGE; PROTEIN DOMAIN; PROTEIN EXPRESSION; AMINO ACID SEQUENCE; CHEMISTRY; ENTEROCOCCUS FAECALIS; ENZYME ACTIVE SITE; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; MUTATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

ENTEROCOCCUS FAECALIS; ESCHERICHIA; ESCHERICHIA COLI; ESCHERICHIA FAECALIS;

3-METHYL-2-OXOBUTANOATE DEHYDROGENASE (LIPOAMIDE); AMIDOHYDROLASES; AMINO ACID SEQUENCE; BIOTINIDASE; BIOTINYLATION; CATALYTIC DOMAIN; CLONING, MOLECULAR; ENTEROCOCCUS FAECALIS; ESCHERICHIA COLI; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN STRUCTURE, TERTIARY; PROTEINS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 70350244434     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0007392     Document Type: Article

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