The divalent metal ion in the active site of uteroferrin modulates substrate binding and catalysis

Journal of the American Chemical Society

Volumn 132, Issue 20, 2010, Pages 7049-7054

  Mitić, Nataša ^a,b   Hadler, Kieran S ^a,b   Gahan, Lawrence R ^a,b   Hengge, Alvan C ^a,b   Schenk, Gerhard ^a,b  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b UTAH STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; COORDINATION SPHERE; DIVALENT METAL ION; FASTER RATES; FASTER REACTIONS; HYDROGEN BOND NETWORKS; INORGANIC PHOSPHATES; METAL ION SUBSTITUTION; PHOSPHATE COMPLEXES; PURPLE ACID PHOSPHATASE; RATE OF INTERACTIONS; STOPPED-FLOW MEASUREMENTS; SUBSTRATE BINDING; WATER MOLECULE;

CATALYSIS; COORDINATION REACTIONS; HYDROGEN BONDS; HYDROLYSIS; MANGANESE; MANGANESE COMPOUNDS; METAL IONS; METALS; NUCLEOPHILES; PHOSPHATASES;

SUBSTRATES;

METAL ION; NUCLEOPHILE; PHOSPHATE; UTEROFERRIN; WATER;

ARTICLE; CATALYSIS; CHEMICAL INTERACTION; CHEMICAL REACTION; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; FLOW MEASUREMENT; HYDROGEN BOND; HYDROLYSIS; MOLECULE; NONHUMAN; SWINE;

ACID PHOSPHATASE; ANIMALS; BIOCATALYSIS; CATALYTIC DOMAIN; ELECTRON TRANSPORT; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; IRON; ISOENZYMES; KINETICS; MANGANESE; PROTEIN BINDING; SWINE;

EID: 77952556804     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja910583y     Document Type: Article

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