Active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N- acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions

Journal of Biological Chemistry

Volumn 285, Issue 44, 2010, Pages 33788-33796

  Gattis, Samuel G ^a   Hernick, Marcy ^b,c   Fierke, Carol A ^a,b  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

^c VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVITY ASSAYS; ANAEROBIC CONDITIONS; CELLULAR CONDITIONS; COFACTORS; DEACETYLASE; DEACETYLATION; E. COLI; ENVIRONMENTAL CONDITIONS; GRAM-NEGATIVE BACTERIA; GROWTH CONDITIONS; HYDROXYMYRISTOYL; IN-VIVO; LIPID A; METAL BOUNDS; METAL CONTENT; METALLOENZYMES; N-ACETYLGLUCOSAMINE; PULL-DOWN METHODS;

ACETYLATION; BACTERIA; BIOCHEMISTRY; ESCHERICHIA COLI; INTERNET PROTOCOLS; METAL IONS; OXYGEN; ZINC; ZINC COMPOUNDS;

METALS;

FERROUS ION; HISTONE DEACETYLASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE 3 O (3 HYDROXYMYRISTOYL) N ACETYLGLUCOSAMINE DEACETYLASE; ZINC ION;

ANAEROBIC CELL CULTURE; ARTICLE; BACTERIAL GROWTH; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME REGULATION; ESCHERICHIA COLI; IN VIVO STUDY; METAL BINDING; NONHUMAN; PRIORITY JOURNAL; REGULATORY MECHANISM; THERMODYNAMICS;

AMIDOHYDROLASES; CATALYTIC DOMAIN; ESCHERICHIA COLI; IMMUNOGLOBULIN G; IRON; KINETICS; METALLOPROTEINS; METALS; MODELS, CHEMICAL; MODELS, STATISTICAL; PLASMIDS; PROTEIN BINDING; THERMODYNAMICS; ZINC;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 77958585295     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.147173     Document Type: Article

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