Substitutions of glycine residues Gly100 and Gly147 in conservative loops decrease rates of conformational rearrangements of escherichia coli inorganic pyrophosphatase

Biochemistry (Moscow)

Volumn 70, Issue 8, 2005, Pages 858-866

  Moiseev, V M ^a   Rodina, E V ^a   Kurilova, S A ^a   Vorobyeva, N N ^a   Nazarova, T I ^a   Avaeva, S M ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Activity; Conformational flexibility; Dissociation constant; Glycine residues; Inorganic pyrophosphatase; Structure

Indexed keywords

BIOSYNTHESIS; CATALYSIS; CHEMICAL ACTIVATION; CONFORMATIONS; DISSOCIATION; ESCHERICHIA COLI; HYDROLYSIS; PH EFFECTS; SUBSTITUTION REACTIONS;

ACTIVITY; CONFORMATIONAL FLEXIBILITY; DISSOCIATION CONSTANTS; GLYCINE RESIDUES; INORGANIC PYROPHOSPHATASE; STRUCTURE;

ENZYMES;

ESCHERICHIA COLI;

EID: 24644500037     PISSN: 00062979     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10541-005-0195-z     Document Type: Article

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