Exploiting the high-resolution crystal structure of Staphylococcus aureus MenH to gain insight into enzyme activity

BMC Structural Biology

Volumn 11, Issue , 2011, Pages

  Dawson, Alice ^a   Fyfe, Paul K ^a   Gillet, Florian ^a   Hunter, William N ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CARBENE; HYDROGEN; MENAQUINONE; MENH ENZYME; PROTON; PYRUVIC ACID; UNCLASSIFIED DRUG; WATER; BACTERIAL PROTEIN; HISTIDINE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR RECOGNITION; NONHUMAN; SITE DIRECTED MUTAGENESIS; STAPHYLOCOCCUS AUREUS; STRUCTURE ACTIVITY RELATION; AMINO ACID SEQUENCE; BIOCATALYSIS; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; HYDROGEN BONDING; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTONS; PYRUVIC ACID; SEQUENCE ALIGNMENT; STAPHYLOCOCCUS AUREUS; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY;

EID: 79955043152     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-11-19     Document Type: Article

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