The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase

Proceedings of the National Academy of Sciences of the United States of America

Volumn 100, Issue 4, 2003, Pages 1552-1557

  Cronin, Annette ^a   Mowbray, Sherry ^b   Dürk, Heike ^c   Homburg, Shirli ^c   Fleming, Ingrid ^d   Fisslthaler, Beate ^d   Oesch, Franz ^c   Arand, Michael ^a  

^a UNIVERSITY OF WÜRZBURG   (Germany)

^b SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^c JOHANNES GUTENBERG UNIVERSITY   (Germany)

^d GOETHE UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

4 NITROPHENYL PHOSPHATE; DIMER; EPOXIDE HYDROLASE; HALOACID; PHOSPHATASE;

AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DEPHOSPHORYLATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; MALE; MAMMAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RAT; REACTION ANALYSIS; REACTION TIME; XENOBIOTIC METABOLISM;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; DNA PRIMERS; EPOXIDE HYDROLASES; HUMANS; HYDROLASES; MALE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHOSPHORIC MONOESTER HYDROLASES; RATS; RATS, INBRED F344; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SOLUBILITY;

ANIMALIA; MAMMALIA;

EID: 0037452594     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0437829100     Document Type: Article

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