The highly exposed loop region in mammalian purple acid phosphatase controls the catalytic activity

ChemBioChem

Volumn 2, Issue 5, 2001, Pages 355-363

  Funhoff, Enrico G ^a   Klaassen, Corné H W ^b   Samyn, Bart ^c   van Beeumen, Jozef ^c   Averill, Bruce A ^a  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

^b RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

^c GHENT UNIVERSITY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ACID PHOSPHATASE; ACID PHOSPHATASE TARTRATE RESISTANT ISOENZYME; GLYCOPROTEIN; PEPTIDE HYDROLASE; RECOMBINANT PROTEIN;

ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; HUMAN; HYDROLYSIS; KINETICS; METABOLISM; PH; PROTEIN TERTIARY STRUCTURE;

ACID PHOSPHATASE; BINDING SITES; CATALYTIC DOMAIN; ENZYME ACTIVATION; GLYCOPROTEINS; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; PEPTIDE HYDROLASES; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

EID: 0035805651     PISSN: 14394227     EISSN: None     Source Type: Journal    
DOI: 10.1002/1439-7633(20010504)2:5<355::AID-CBIC355>3.0.CO;2-Q     Document Type: Article

References (4)

1. E. V. Koonin, Protein Sci. 1994, 3, 356-368.
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4. J. B. Vincent, G. L. Olivier-Lilley, B. A. Averill, Chem. Rev. 1990, 90, 1447-1467.