Isoleucine 259 and isoleucine 260 residues in Streptococcus gordonii soluble inorganic pyrophosphatase play an important role in enzyme activity

Journal of Bioscience and Bioengineering

Volumn 112, Issue 1, 2011, Pages 8-13

  Ilias, Mohammad ^a,b   White, Scott A ^a   Young, Tom W ^a,c  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

^b UNIVERSITY OF DHAKA   (Bangladesh)

^c NONE   (United Kingdom)

Author keywords

Inorganic pyrophosphatase family II; Interdomain region; Streptococcus gordonii

Indexed keywords

ACIDIC AMINO ACIDS; ACTIVE SITE; ADVERSE EFFECT; AMINO ACID RESIDUES; ASPARTATES; C-TERMINAL DOMAINS; CATALYTIC EFFICIENCIES; FAMILY II; INORGANIC PYROPHOSPHATASES; INTER-DOMAIN; ISOLEUCINE 260; KINETIC PROPERTIES; OPEN CONFORMATION; SOLVENT ACCESSIBILITY; STREPTOCOCCUS GORDONII; WILD TYPES;

CATALYST ACTIVITY; ENZYME ACTIVITY; PLANTS (BOTANY);

AMINO ACIDS;

ASPARTIC ACID; ENZYME VARIANT; GLUTAMIC ACID; INORGANIC PYROPHOSPHATASE; ISOLEUCINE; ISOLEUCINE 259; ISOLEUCINE 260; SOLVENT; UNCLASSIFIED DRUG; VALINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL GENE; BACTERIAL MUTATION; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME MECHANISM; ESCHERICHIA COLI; GENE OVEREXPRESSION; GENETIC CONSERVATION; HINGE REGION; HYDROPHILICITY; MOLECULAR WEIGHT; NONHUMAN; SITE DIRECTED MUTAGENESIS; STREPTOCOCCUS GORDONII; WILD TYPE;

ASPARTIC ACID; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; GLUTAMIC ACID; INORGANIC PYROPHOSPHATASE; ISOLEUCINE; MUTAGENESIS, SITE-DIRECTED; STREPTOCOCCUS GORDONII; VALINE;

STREPTOCOCCUS GORDONII;

EID: 79960273954     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2011.02.011     Document Type: Article

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