A C-Terminal Phosphatase Module Conserved in Vertebrate CMP-Sialic Acid Synthetases Provides a Tetramerization Interface for the Physiologically Active Enzyme

Journal of Molecular Biology

Volumn 393, Issue 1, 2009, Pages 83-97

  Oschlies, Melanie ^a   Dickmanns, Achim ^b   Haselhorst, Thomas ^c   Schaper, Wiebke ^a   Stummeyer, Katharina ^a   Tiralongo, Joe ^c   Weinhold, Birgit ^a   Gerardy Schahn, Rita ^a   von Itzstein, Mark ^c   Ficner, Ralf ^b   Münster Kühnel, Anja K ^a  

^a HANNOVER MEDICAL SCHOOL   (Germany)

^b UNIVERSITY OF GÖTTINGEN   (Germany)

^c GRIFFITH UNIVERSITY   (Australia)

Author keywords

CMP sialic acid; CMP sialic acid synthetase; HAD phosphatase; sialic acid; type hydrolase fold

Indexed keywords

ACYLNEURAMINATE CYTIDYLYLTRANSFERASE; TETRAMER;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STRUCTURE; HAEMOPHILUS INFLUENZAE; IN VITRO STUDY; MATHEMATICAL MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN FUNCTION;

MURINAE; VERTEBRATA;

EID: 70349243063     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.08.003     Document Type: Article

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