Molecular dissection of arginyltransferases guided by similarity to bacterial peptidoglycan synthases

EMBO Reports

Volumn 7, Issue 8, 2006, Pages 800-805

  Rai, Reena ^a   Mushegian, Arcady ^b,c   Makarova, Kira ^d   Kashina, Anna ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b STOWERS INSTITUTE FOR MEDICAL RESEARCH   (United States)

^c UNIVERSITY OF KANSAS SCHOOL OF MEDICINE   (United States)

^d NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGINYLTRANSFERASE; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE;

ANGIOGENESIS; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INACTIVATION; ENZYME SPECIFICITY; GENETIC CONSERVATION; HEART DEVELOPMENT; MOLECULAR RECOGNITION; MOUSE; NONHUMAN; POINT MUTATION; PREDICTION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN PROCESSING; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINOACYLTRANSFERASES; ANIMALS; CRYSTALLOGRAPHY, X-RAY; EVOLUTION, MOLECULAR; GENETIC COMPLEMENTATION TEST; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PENICILLIN-BINDING PROTEINS; POINT MUTATION; RNA, TRANSFER, ARG; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS);

EID: 33747754168     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7400747     Document Type: Article

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